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Conserved domains on  [gi|572187173|gb|AHF51357|]
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wze, partial [synthetic construct]

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 ...
 1-203 4.18e-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: 359.06  E-value: 4.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173    1 YYNALCTNLQLSGDGLKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKITGLTEFLSGT 80
Cdd:TIGR01007   2 YYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   81 TDLSQGLCDTNIENLFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAG 160
Cdd:TIGR01007  82 TDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDAG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 572187173  161 EINRRDIQKAKEQLEHTGKPFLGVVLNKFNTSVDKYGFYGNYG 203
Cdd:TIGR01007 162 KIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG 204
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-203 4.18e-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: 359.06  E-value: 4.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173    1 YYNALCTNLQLSGDGLKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKITGLTEFLSGT 80
Cdd:TIGR01007   2 YYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   81 TDLSQGLCDTNIENLFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAG 160
Cdd:TIGR01007  82 TDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDAG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 572187173  161 EINRRDIQKAKEQLEHTGKPFLGVVLNKFNTSVDKYGFYGNYG 203
Cdd:TIGR01007 162 KIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-188 7.65e-75

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: 223.99  E-value: 7.65e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   2 YNALCTNLQLSGDG--LKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKaRDKITGLTEFLSG 79
Cdd:cd05387    3 FRTLRTNLLFAGSDagPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLG-LPNEPGLSEVLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  80 TTDLSQGLCDTNIENLFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEA 159
Cdd:cd05387   82 QASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVRA 161

                        170       180
                 ....*....|....*....|....*....
gi 572187173 160 GEINRRDIQKAKEQLEHTGKPFLGVVLNK 188
Cdd:cd05387  162 GKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 18-206 3.69e-66

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: 205.42  E-value: 3.69e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  18 VFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKItGLTEFLSGTTDLSQGLCDTNIENLFV 97
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP-GLSDVLAGEASLEDVIQPTEVEGLDV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  98 IQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAGEINRRDIQKAKEQLEHT 177
Cdd:COG0489  173 LPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKA 252

                        170       180
                 ....*....|....*....|....*....
gi 572187173 178 GKPFLGVVLNKFNTSVDKYgfYGNYGDYG 206
Cdd:COG0489  253 GVPVLGVVLNMVCPKGERY--YGGGEEYG 279
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
18-199 2.29e-27

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 108.70  E-value: 2.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  18 VFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSV---MLGVfkarDKITGLTEFLSGTTDLSQGLCDTNIEN 94
Cdd:PRK11519 528 VLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYtheLLGT----NNVNGLSDILIGQGDITTAAKPTSIAN 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  95 LFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAGEINRRDIQKAKEQL 174
Cdd:PRK11519 604 FDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRF 683

                        170       180
                 ....*....|....*....|....*...
gi 572187173 175 EHTGKPFLGVVLN---KFNTSVDKYGFY 199
Cdd:PRK11519 684 EQNGIPVKGVILNsifRRASAYQDYGYY 711
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 19-190 1.22e-18

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: 80.47  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   19 FSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDI--RNSVMLGV--FKARDKITgLTEFLSGTTDLSQGLC--DTNI 92
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPqsNNSSVEGLegDIAPALQA-LAEGLKGRVNLDPILLkeKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   93 ENLFVIQAGSVSPNPTALLQSKNFSTM----LETLRKYFDYIIVDTAPvGVVIDAAIITRNCDASILVTEAGEINRRDIQ 168
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKELLGPRKEERlreaLEALKEDYDYVIIDGAP-GLGELLRNALIAADYVIIPLEPEVILVEDAK 158

                         170       180
                  ....*....|....*....|....*....
gi 572187173  169 KAKEQLEHTGKPF-------LGVVLNKFN 190
Cdd:pfam01656 159 RLGGVIAALVGGYallglkiIGVVLNKVD 187
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-203 4.18e-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: 359.06  E-value: 4.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173    1 YYNALCTNLQLSGDGLKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKITGLTEFLSGT 80
Cdd:TIGR01007   2 YYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   81 TDLSQGLCDTNIENLFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAG 160
Cdd:TIGR01007  82 TDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDAG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 572187173  161 EINRRDIQKAKEQLEHTGKPFLGVVLNKFNTSVDKYGFYGNYG 203
Cdd:TIGR01007 162 KIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-188 7.65e-75

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: 223.99  E-value: 7.65e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   2 YNALCTNLQLSGDG--LKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKaRDKITGLTEFLSG 79
Cdd:cd05387    3 FRTLRTNLLFAGSDagPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLG-LPNEPGLSEVLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  80 TTDLSQGLCDTNIENLFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEA 159
Cdd:cd05387   82 QASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVRA 161

                        170       180
                 ....*....|....*....|....*....
gi 572187173 160 GEINRRDIQKAKEQLEHTGKPFLGVVLNK 188
Cdd:cd05387  162 GKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 18-206 3.69e-66

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: 205.42  E-value: 3.69e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  18 VFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKItGLTEFLSGTTDLSQGLCDTNIENLFV 97
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP-GLSDVLAGEASLEDVIQPTEVEGLDV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  98 IQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAGEINRRDIQKAKEQLEHT 177
Cdd:COG0489  173 LPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKA 252

                        170       180
                 ....*....|....*....|....*....
gi 572187173 178 GKPFLGVVLNKFNTSVDKYgfYGNYGDYG 206
Cdd:COG0489  253 GVPVLGVVLNMVCPKGERY--YGGGEEYG 279
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 11-207 4.84e-32

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: 122.14  E-value: 4.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   11 LSGDGLKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFkARDKITGLTEFLSGTTDLSQGLCDT 90
Cdd:TIGR01005 548 LADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMF-GKAPKPGLLDLLAGEASIEAGIHRD 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   91 NIENLFVIQAGSVS---PNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAGEINRRDI 167
Cdd:TIGR01005 627 QRPGLAFIAAGGAShfpHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVTEFERSPLGEI 706

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 572187173  168 QKAKEQLEHTGKPFLGVVLNKfnTSVDKYGFYGNYGDYGK 207
Cdd:TIGR01005 707 RDLIHQEPHANSDVLGVIFNA--LDMNELGKYGDFDGAEK 744
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
18-199 2.29e-27

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 108.70  E-value: 2.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  18 VFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSV---MLGVfkarDKITGLTEFLSGTTDLSQGLCDTNIEN 94
Cdd:PRK11519 528 VLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYtheLLGT----NNVNGLSDILIGQGDITTAAKPTSIAN 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  95 LFVIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAGEINRRDIQKAKEQL 174
Cdd:PRK11519 604 FDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRF 683

                        170       180
                 ....*....|....*....|....*...
gi 572187173 175 EHTGKPFLGVVLN---KFNTSVDKYGFY 199
Cdd:PRK11519 684 EQNGIPVKGVILNsifRRASAYQDYGYY 711
PRK09841 PRK09841
tyrosine-protein kinase;
17-210 1.50e-24

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 100.75  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKiTGLTEFLSGTTDLSQGLCDTNIENLF 96
Cdd:PRK09841 532 NILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNE-HGLSEYLAGKDELNKVIQHFGKGGFD 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  97 VIQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRNCDASILVTEAGEINRRDIQKAKEQLEH 176
Cdd:PRK09841 611 VITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQ 690

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 572187173 177 TGKPFLGVVLNKFNTSVDKYGFYG-NYGDYGKNKK 210
Cdd:PRK09841 691 AGVNIKGAILNGVIKRASTAYSYGyNYYGYSYSEK 725
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 17-190 1.72e-22

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: 91.46  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRN--SVMLGVFKARDKITgLTEFLSGTTDLSQGLCDTNIEN 94
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnlTSGLGLDPDDLDPT-LYDLLLDDAPLEDAIVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  95 LFVIQAG-SVSPNPTALLQSKN----FSTMLETLRKYFDYIIVDTAP-VGVVIDAAIITrnCDASILVTEAGE------- 161
Cdd:COG1192   81 LDLIPANiDLAGAEIELVSRPGrelrLKRALAPLADDYDYILIDCPPsLGLLTLNALAA--ADSVLIPVQPEYlslegla 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 572187173 162 --INRrdIQKAKEQLEHtGKPFLGVVLNKFN 190
Cdd:COG1192  159 qlLET--IEEVREDLNP-KLEILGILLTMVD 186
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 17-199 9.11e-21

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: 86.49  E-value: 9.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDI--RN-SVMLGVfkARDKITGLTEFLSGTTDLSQGLC-DTNI 92
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIglRNlDLILGL--ENRIVYTLVDVLEGECRLEQALIkDKRW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  93 ENLFVIqAGSVSPNPTALLQSKnFSTMLETLRKYFDYIIVDtAPVGVVIDAAIITRNCDASILVTEAgEINR-RDIQKAK 171
Cdd:cd02036   79 ENLYLL-PASQTRDKDALTPEK-LEELVKELKDSFDFILID-SPAGIESGFINAIAPADEAIIVTNP-EISSvRDADRVI 154

                        170       180
                 ....*....|....*....|....*...
gi 572187173 172 EQLEHTGKPFLGVVLNKFNTSVDKYGFY 199
Cdd:cd02036  155 GLLESKGIVNIGLIVNRYRPEMVKSGDM 182
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 17-189 1.61e-19

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: 85.17  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFAR-AGYKTLLIDGDIRN---SVMLGVFKARdkitGLTEFLSGTTDLSQGLCDTNI 92
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFgdvALYLDLEPRR----GLADALRNPDRLDETLLDRAL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  93 ----ENLFVIqAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAPVGVVIDAAIITRnCDASILVTEAGEINRRDIQ 168
Cdd:COG4963  179 trhsSGLSVL-AAPADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEA-ADEVVLVTEPDLPSLRNAK 256

                        170       180
                 ....*....|....*....|...
gi 572187173 169 KAKEQLEHTGKPF--LGVVLNKF 189
Cdd:COG4963  257 RLLDLLRELGLPDdkVRLVLNRV 279
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 32-188 4.95e-19

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: 81.86  E-value: 4.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  32 TTSTNIAWAFARAGYKTLLIDGDIRN---SVMLGVfkaRDKITgLTEFLSGTTDLSQGLCDTNiENLFVIQAGSVSPNPT 108
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLanlDVLLGL---EPKAT-LADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173 109 ALLQSKNFSTMLETLRKYFDYIIVDTAPvGVVIDAAIITRNCDASILVTEAGEINRRDIQKAKEQLE-HTGKPFLGVVLN 187
Cdd:COG0455   76 ELDPEERLIRVLEELERFYDVVLVDTGA-GISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRrRLGVRRAGVVVN 154


                 .
gi 572187173 188 K 188
Cdd:COG0455  155 R 155
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 19-190 1.22e-18

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: 80.47  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   19 FSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDI--RNSVMLGV--FKARDKITgLTEFLSGTTDLSQGLC--DTNI 92
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPqsNNSSVEGLegDIAPALQA-LAEGLKGRVNLDPILLkeKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   93 ENLFVIQAGSVSPNPTALLQSKNFSTM----LETLRKYFDYIIVDTAPvGVVIDAAIITRNCDASILVTEAGEINRRDIQ 168
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKELLGPRKEERlreaLEALKEDYDYVIIDGAP-GLGELLRNALIAADYVIIPLEPEVILVEDAK 158

                         170       180
                  ....*....|....*....|....*....
gi 572187173  169 KAKEQLEHTGKPF-------LGVVLNKFN 190
Cdd:pfam01656 159 RLGGVIAALVGGYallglkiIGVVLNKVD 187
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 17-136 1.16e-14

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: 68.76  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFKARDKI-TGLTEFLSGTTDLSQGLCDTNIENL 95
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVeKTIYELLIGECNIEEAIIKTVIENL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 572187173   96 FVIQAG-SVSPNPTALLQSKN----FSTMLETLRKYFDYIIVDTAP 136
Cdd:pfam13614  82 DLIPSNiDLAGAEIELIGIENreniLKEALEPVKDNYDYIIIDCPP 127
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 17-136 2.16e-12

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: 63.74  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNS---VMLGVfkaRDKITgLTEFLSGTTDLSQGLCDTNiE 93
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLAnldILLGL---APKKT-LGDVLKGRVSLEDIIVEGP-E 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 572187173  94 NLFVIQAGSVSPNPTALLQSKN--FSTMLETLRKYFDYIIVDTAP 136
Cdd:cd02038   76 GLDIIPGGSGMEELANLDPEQKakLIEELSSLESNYDYLLIDTGA 120
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 17-192 1.33e-11

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: 59.48  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDirnsvmlgvfkardkitglteflsgttdlSQGlcdtnienlf 96
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD-----------------------------PQG---------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  97 viqagsvspnptallqskNFSTMLetlrkyFDYIIVDTAP-VGVVIDAAIITrnCDASILVTEAGEINRR-------DIQ 168
Cdd:cd02042   42 ------------------SLTSWL------YDYILIDTPPsLGLLTRNALAA--ADLVLIPVQPSPFDLDglaklldTLE 95

                        170       180
                 ....*....|....*....|....
gi 572187173 169 KAKEQLEhTGKPFLGVVLNKFNTS 192
Cdd:cd02042   96 ELKKQLN-PPLLILGILLTRVDPR 118
minD CHL00175
septum-site determining protein; Validated
 17-178 1.06e-10

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 59.40  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDI--RNSVMLGVFKARDKITGLtEFLSGTTDLSQGLC-DTNIE 93
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIglRNLDLLLGLENRVLYTAM-DVLEGECRLDQALIrDKRWK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  94 NLFVIqagSVSPNPTAL-LQSKNFSTMLETLRKY-FDYIIVDtAPVGvvIDAAIITRNCDA--SILVTEAGEINRRDIQK 169
Cdd:CHL00175  95 NLSLL---AISKNRQRYnVTRKNMNMLVDSLKNRgYDYILID-CPAG--IDVGFINAIAPAqeAIVVTTPEITAIRDADR 168


                 ....*....
gi 572187173 170 AKEQLEHTG 178
Cdd:CHL00175 169 VAGLLEANG 177
PHA02518 PHA02518
ParA-like protein; Provisional
 17-175 4.29e-08

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 51.39  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSvmlgvfkardkitglteflsgTTDLSQglcdtnienlf 96
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGS---------------------STDWAE----------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  97 viQAGSVSPNPTALLQSKNFSTMLETLRKYFDYIIVDTAP-VGVVIDAAIitRNCDASILVTEAgeiNRRDIQKAKEQLE 175
Cdd:PHA02518  49 --AREEGEPLIPVVRMGKSIRADLPKVASGYDYVVVDGAPqDSELARAAL--RIADMVLIPVQP---SPFDIWAAPDLVE 121
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 17-63 1.49e-07

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: 50.14  E-value: 1.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 572187173   17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRN-SV--MLGV 63
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGpSIprMLGL 53
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 17-55 7.83e-07

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: 47.88  E-value: 7.83e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDI 55
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADI 39
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 128-189 1.99e-06

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 46.99  E-value: 1.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572187173 128 DYIIVDTAP-VGVVIDAAIitRNCDASILVTEAGEINRRDIQKAKEQLEHTGKPFlGVVLNKF 189
Cdd:cd03110  161 DLAIIDGPPgTGCPVVASI--TGADAVLLVTEPTPSGLHDLKRAIELAKHFGIPT-GIVINRY 220
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 17-54 4.54e-06

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: 43.96  E-value: 4.54e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGD 54
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 13-68 1.69e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 44.67  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 572187173  13 GDGLKVFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSV--MLGVFKARD 68
Cdd:PRK13869 118 SEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLsaLLGVLPETD 175
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 25-195 3.79e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 43.23  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  25 KTGEGKSTTSTNIAWAFARAGYKTLLIDGDIrNS---VMLGVFKARDKITGLTEFL-----------SGTTDLSQGL--- 87
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADP-NAnlaEALGLEVEADLIKPLGEMRelikertgapgGGMFKLNPKVddi 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  88 ---CDTNIENLFVIQAGSVSPN-------PTALLQSknfstMLETLRKY-FDYIIVDTapvgvviDAAI------ITRNC 150
Cdd:COG3640   87 peeYLVEGDGVDLLVMGTIEEGgsgcycpENALLRA-----LLNHLVLGnYEYVVVDM-------EAGIehlgrgTAEGV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 572187173 151 DASILVTEAGeinRRDIQKAKEQLEHT---GKPFLGVVLNKFNTSVDK 195
Cdd:COG3640  155 DLLLVVSEPS---RRSIETARRIKELAeelGIKKIYLVGNKVREEEDE 199
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 25-138 4.12e-05

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: 42.88  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  25 KTGEGKSTTSTNIAWAFARAGYKTLLI--D-----GDIrnsvmLGVfkardKITGLTEflsgttdlsqglcdTNI-ENLF 96
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVstDpahslSDA-----FGQ-----KLGGETP--------------VKGaPNLW 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572187173  97 VIQagsvsPNPTALLQsKNFSTMLETLRKY-------------------------------------FDYIIVDTAPVG 138
Cdd:cd02035   64 AME-----IDPEEALE-EYWEEVKELLAQYlrlpgldevyaeellslpgmdeaaafdelreyvesgeYDVIVFDTAPTG 136
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
15-136 5.08e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.11  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  15 GLK-VFSITSVKTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRN-SV--MLGVFKAR------DKITGLteflsgttdLS 84
Cdd:PRK11670 105 GVKnIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGpSIptMLGAEDQRptspdgTHMAPI---------MA 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 572187173  85 QGLCDTNIENLFVIQAGSVSPNPTAllqSKNFSTML-ETLRKYFDYIIVDTAP 136
Cdd:PRK11670 176 HGLATNSIGYLVTDDNAMVWRGPMA---SKALMQMLqETLWPDLDYLVLDMPP 225
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
25-138 1.04e-04

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 42.11  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  25 KTGEGKSTTSTNIAWAFARAGYKTLLIdgdirnsvmlgvfkardkitglteflsgTTD----LSQGLcDTNI-------- 92
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLV----------------------------STDpahsLGDVL-GTELgnepteva 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572187173  93 -ENLFVIQ----------AGSVSPNPTALLQSKNFSTM------------LETLRKY-----FDYIIVDTAPVG 138
Cdd:COG0003   62 vPNLYALEidpeaeleeyWERVRAPLRGLLPSAGVDELaeslpgteelaaLDELLELleegeYDVIVVDTAPTG 135
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 17-196 9.99e-04

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 38.70  E-value: 9.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  17 KVFSITSVKTGEGKSTTSTNIAWAFARAGYKTllidgdirnsvmlGVFKArdkI-TGLTEFLSGTTD----LSQGLCDTN 91
Cdd:cd03109    1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKV-------------GYLKP---VqTGCPGLEDSDAEllrkLAGLLLDLE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173  92 IENLFVIQAgSVSPNPTALLQS-----KNFSTMLETLRKYFDYIIVDTA-PVGVVIDAAIIT----RNCDAS-ILVTEA- 159
Cdd:cd03109   65 LINPYRFEA-PLSPHLAAELEGrdidlEEIVRALEELAKSYDVVLVEGAgGLLVPLTEGYLNadlaRALGLPvILVARGg 143

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 572187173 160 -GEINrrDIQKAKEQLEHTGKPFLGVVLNKFNTSVDKY 196
Cdd:cd03109  144 lGTIN--HTLLTLEALKSRGLDVAGVVLNGIPPEPEAE 179
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 25-54 1.91e-03

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 38.05  E-value: 1.91e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 572187173  25 KTGEGKSTTSTNIAWAFARAGYKTLLIDGD 54
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCD 37
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 17-54 1.93e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 38.02  E-value: 1.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 572187173  17 KVFSITSvKTGEGKSTTSTNIAWAFARAGYKTLLIDGD 54
Cdd:PRK13185   3 LVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCD 39
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 25-51 4.04e-03

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 37.11  E-value: 4.04e-03
                         10        20
                 ....*....|....*....|....*..
gi 572187173  25 KTGEGKSTTSTNIAWAFARAGYKTLLI 51
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHV 34
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 25-134 6.45e-03

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: 36.66  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572187173   25 KTGEGKSTTSTNIAWAFARAGYKTLLIDGDIRNSVMLGVFK---ARDKITGLteflsgttDLSQGLCDTNIENLFVIQAG 101
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYFEnrsATADRTGL--------SLPTPEHLNLPDNDVAEVPD 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 572187173  102 SVSPnptallQSKNFSTMLETLRKYFDYIIVDT 134
Cdd:pfam09140  81 GENI------DDARLEEAFADLEARCDFIVIDT 107
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 25-52 9.05e-03

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 36.51  E-value: 9.05e-03
                         10        20
                 ....*....|....*....|....*...
gi 572187173  25 KTGEGKSTTSTNIAWAFARAGYKTLLID 52
Cdd:COG0433   55 ATGSGKSNTLQVLLEELSRAGVPVLVFD 82
 
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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