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Conserved domains on  [gi|445959476|ref|WP_000037331|]
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type 8 capsular polysaccharide synthesis protein Cap8B [Staphylococcus aureus]

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 ...
 23-226 6.49e-108

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: 308.98  E-value: 6.49e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   23 EKFRGIRSNIMFSKAngEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQN-NNGLSSLI 101
Cdd:TIGR01007   1 EYYNAIRTNIQFSGA--EIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  102 IGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVI 181
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 445959476  182 DSEKNDKNEVKKAKALMEKAGSNILGVILNKAKVDKSSS-YYHYYG 226
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYgYYGYYG 204
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 23-226 6.49e-108

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: 308.98  E-value: 6.49e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   23 EKFRGIRSNIMFSKAngEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQN-NNGLSSLI 101
Cdd:TIGR01007   1 EYYNAIRTNIQFSGA--EIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  102 IGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVI 181
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 445959476  182 DSEKNDKNEVKKAKALMEKAGSNILGVILNKAKVDKSSS-YYHYYG 226
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYgYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 23-212 4.59e-84

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: 247.87  E-value: 4.59e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  23 EKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLII 102
Cdd:cd05387    1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 103 GRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVID 182
Cdd:cd05387   81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 445959476 183 SEKNDKNEVKKAKALMEKAGSNILGVILNK 212
Cdd:cd05387  161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 40-228 1.36e-69

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: 214.67  E-value: 1.36e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  40 EVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIENL 119
Cdd:COG0489   91 LLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEVEGL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 120 DLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVIDSEKNDKNEVKKAKALME 199
Cdd:COG0489  171 DVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLE 250

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 445959476 200 KAGSNILGVILNKAKVDKSSSY-------YHYYGDE 228
Cdd:COG0489  251 KAGVPVLGVVLNMVCPKGERYYgggeeygYREYGDR 286
PRK09841 PRK09841
tyrosine-protein kinase;
15-226 1.17e-45

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 161.23  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  15 EKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNN 94
Cdd:PRK09841 505 DNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNE 584

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  95 NGLSSLIIGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAI 174
Cdd:PRK09841 585 HGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSV 664

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445959476 175 KDSLLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNkaKVDKSSSYYHYYG 226
Cdd:PRK09841 665 GTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILN--GVIKRASTAYSYG 714
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 46-180 3.36e-17

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: 76.08  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   46 VTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNN--NGLSSLIIGRTTMSEAITSTEIENLDLLt 123
Cdd:pfam13614   6 IANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNveKTIYELLIGECNIEEAIIKTVIENLDLI- 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445959476  124 agpvppnPS---------ELIGSE----RFKELVDLFNKRYDIIIVDTPP-VNTVTDAQLYAraiKDSLLV 180
Cdd:pfam13614  85 -------PSnidlagaeiELIGIEnrenILKEALEPVKDNYDYIIIDCPPsLGLLTINALTA---SDSVLI 145
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 39-160 9.26e-04

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.86  E-value: 9.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  39 GEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNyIF-----NEQNNNGLSSLIIGRTTMSEAITS 113
Cdd:NF041417 330 QKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQD-IFgtevgHEPTKVGVENLYAARIDQERALEE 408

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445959476 114 TEIENLDLLT------AGPV------------PPNPSELIGSERFKELVDLfnKRYDIIIVDTPP 160
Cdd:NF041417 409 YKTRMLDQVEqsfdkdQIDVeaakaqvreeleSPCAEEMAALEKFVSYFDV--DGYDVVVFDTAP 471
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 23-226 6.49e-108

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: 308.98  E-value: 6.49e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   23 EKFRGIRSNIMFSKAngEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQN-NNGLSSLI 101
Cdd:TIGR01007   1 EYYNAIRTNIQFSGA--EIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  102 IGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVI 181
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 445959476  182 DSEKNDKNEVKKAKALMEKAGSNILGVILNKAKVDKSSS-YYHYYG 226
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYgYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 23-212 4.59e-84

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: 247.87  E-value: 4.59e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  23 EKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLII 102
Cdd:cd05387    1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 103 GRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVID 182
Cdd:cd05387   81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 445959476 183 SEKNDKNEVKKAKALMEKAGSNILGVILNK 212
Cdd:cd05387  161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 40-228 1.36e-69

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: 214.67  E-value: 1.36e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  40 EVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIENL 119
Cdd:COG0489   91 LLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEVEGL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 120 DLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDSLLVIDSEKNDKNEVKKAKALME 199
Cdd:COG0489  171 DVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLE 250

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 445959476 200 KAGSNILGVILNKAKVDKSSSY-------YHYYGDE 228
Cdd:COG0489  251 KAGVPVLGVVLNMVCPKGERYYgggeeygYREYGDR 286
PRK09841 PRK09841
tyrosine-protein kinase;
15-226 1.17e-45

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 161.23  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  15 EKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNN 94
Cdd:PRK09841 505 DNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNE 584

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  95 NGLSSLIIGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAI 174
Cdd:PRK09841 585 HGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSV 664

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445959476 175 KDSLLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNkaKVDKSSSYYHYYG 226
Cdd:PRK09841 665 GTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILN--GVIKRASTAYSYG 714
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
2-224 1.74e-43

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 155.31  E-value: 1.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   2 SKKENTTTTLFVYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMR 81
Cdd:PRK11519 487 GIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMR 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  82 KPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPV 161
Cdd:PRK11519 567 KGYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPI 646

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445959476 162 NTVTDAQLYARAIKDSLLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNkAKVDKSSSYYHY 224
Cdd:PRK11519 647 LAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILN-SIFRRASAYQDY 708
EpsG TIGR03029
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ...
 16-211 1.63e-40

chain length determinant protein tyrosine kinase EpsG; The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF).


Pssm-ID: 132074 [Multi-domain]  Cd Length: 274  Bit Score: 139.61  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   16 KPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNN 95
Cdd:TIGR03029  78 QPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNFKLSEQR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   96 GLSSLIIGRTTMsEAITST-EIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAI 174
Cdd:TIGR03029 158 GLSDILAGRSDL-EVITHIpALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQIVATRA 236

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 445959476  175 KDSLLVIDSEKNDKNEVKKAKALMEKAGSNILGVILN 211
Cdd:TIGR03029 237 RGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLN 273
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 13-228 8.66e-35

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: 130.61  E-value: 8.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   13 VYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQ 92
Cdd:TIGR01005 525 VPDAPRSTFAEAFRNAKLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKA 604

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   93 NNNGLSSLIIGRTTMSEAITSTEIENLDLLTAGPV---PPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQL 169
Cdd:TIGR01005 605 PKPGLLDLLAGEASIEAGIHRDQRPGLAFIAAGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAA 684

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 445959476  170 YARAIKDSLLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKAKVDKSSSYYHYYGDE 228
Cdd:TIGR01005 685 FAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFNALDMNELGKYGDFDGAE 743
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 42-180 1.60e-18

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: 81.06  E-value: 1.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  42 KRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDmrkP----TQNY-IFNEQNNNGLSSLIIGRTTMSEAITSTEI 116
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLD---PqgnlTSGLgLDPDDLDPTLYDLLLDDAPLEDAIVPTEI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445959476 117 ENLDLLTAGPvppnpsELIGSE-----------RFKELVDLFNKRYDIIIVDTPP-VNTVTDAQLYArAikDSLLV 180
Cdd:COG1192   79 PGLDLIPANI------DLAGAEielvsrpgrelRLKRALAPLADDYDYILIDCPPsLGLLTLNALAA-A--DSVLI 145
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 57-214 3.51e-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: 79.93  E-value: 3.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  57 TVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEiENLDLLTAGPVPPNPSELIG 136
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAELDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 137 SERFKELVDLFNKRYDIIIVDTPPvnTVTDAQLYARAIKDSLLVI-----DSekndkneVKKAKALME----KAGSNILG 207
Cdd:COG0455   80 EERLIRVLEELERFYDVVLVDTGA--GISDSVLLFLAAADEVVVVttpepTS-------ITDAYALLKllrrRLGVRRAG 150


                 ....*..
gi 445959476 208 VILNKAK 214
Cdd:COG0455  151 VVVNRVR 157
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 46-180 3.36e-17

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: 76.08  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   46 VTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNN--NGLSSLIIGRTTMSEAITSTEIENLDLLt 123
Cdd:pfam13614   6 IANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNveKTIYELLIGECNIEEAIIKTVIENLDLI- 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445959476  124 agpvppnPS---------ELIGSE----RFKELVDLFNKRYDIIIVDTPP-VNTVTDAQLYAraiKDSLLV 180
Cdd:pfam13614  85 -------PSnidlagaeiELIGIEnrenILKEALEPVKDNYDYIIIDCPPsLGLLTINALTA---SDSVLI 145
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 42-161 2.86e-16

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: 76.31  E-value: 2.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  42 KRLLVTSEKPGAGKSTVVSNVAITYAQ-AGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLI--IGR--TTMSEAITSTEI 116
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLDLEPRRGLADALrnPDRldETLLDRALTRHS 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445959476 117 ENLDLLTAgPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPV 161
Cdd:COG4963  183 SGLSVLAA-PADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRG 226
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 44-212 2.09e-14

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: 69.68  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   44 LLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGD------MRKPTQNYIfnEQNNNGLSSLIIGRTTMSEAI--TSTE 115
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqsnnsSVEGLEGDI--APALQALAEGLKGRVNLDPILlkEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  116 IENLDLLTAGPV----PPNPSELIGSERFKELVDLFNKRYDIIIVDTPP------VNTVTDAQLYARaikdsllVIDSEK 185
Cdd:pfam01656  79 EGGLDLIPGNIDlekfEKELLGPRKEERLREALEALKEDYDYVIIDGAPglgellRNALIAADYVII-------PLEPEV 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 445959476  186 NDKNEVKKAKALMEK-------AGSNILGVILNK 212
Cdd:pfam01656 152 ILVEDAKRLGGVIAAlvggyalLGLKIIGVVLNK 185
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 46-160 4.19e-13

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: 66.05  E-value: 4.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  46 VTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEiENLDLLTAG 125
Cdd:cd02038    5 VTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGP-EGLDIIPGG 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 445959476 126 PVPPNPSELiGSERFKELVDLFNK---RYDIIIVDTPP 160
Cdd:cd02038   84 SGMEELANL-DPEQKAKLIEELSSlesNYDYLLIDTGA 120
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 46-220 4.30e-11

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: 60.68  E-value: 4.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  46 VTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGD--MRkptqnyifneqnnN-----GLSSLII--------GRTTMSEA 110
Cdd:cd02036    5 ITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADigLR-------------NldlilGLENRIVytlvdvleGECRLEQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 111 -ITSTEIENLDLLtAGPVPPNPSELiGSERFKELVDLFNKRYDIIIVDTPpvntvtdAQLYARAI------KDSLLVIDS 183
Cdd:cd02036   72 lIKDKRWENLYLL-PASQTRDKDAL-TPEKLEELVKELKDSFDFILIDSP-------AGIESGFInaiapaDEAIIVTNP 142

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 445959476 184 EKNDKNEVKKAKALMEKAGSNILGVILNKAKVDKSSS 220
Cdd:cd02036  143 EISSVRDADRVIGLLESKGIVNIGLIVNRYRPEMVKS 179
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 45-181 5.71e-09

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 54.59  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  45 LVTSEKPGAGKSTVVSNVAITYAQ-AGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLI-----IGRTTMSEAITSTEiEN 118
Cdd:cd03111    4 AVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIqnldrLDRTLLDSAVTRHS-SG 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445959476 119 LDLLtAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAikDSLLVI 181
Cdd:cd03111   83 LSLL-PAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAA--DEILLV 142
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 43-159 8.32e-09

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: 54.38  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   43 RLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFneqnNNGLSSLiiGRTTMSEAItsTEIENLDLL 122
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYF----ENRSATA--DRTGLSLPT--PEHLNLPDN 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 445959476  123 TAGPVPPNPSelIGSERFKELVDLFNKRYDIIIVDTP 159
Cdd:pfam09140  74 DVAEVPDGEN--IDDARLEEAFADLEARCDFIVIDTP 108
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 42-211 1.08e-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: 50.58  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  42 KRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSliigrttmSEAITSTEIENLDL 121
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQS--------EEGIVPVEVGGIKV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 122 LTAG-------PVP---PNPSELIgserfKELvdLFNKRY---DIIIVDTPPvNTvTDAQL-YARAIKDSLLVIDSEKND 187
Cdd:cd02037   73 MSIGfllpeddAVIwrgPMKSGAI-----KQF--LKDVDWgelDYLIIDLPP-GT-GDEHLsLVQLIPIDGAVVVTTPQE 143

                        170       180
                 ....*....|....*....|....*.
gi 445959476 188 --KNEVKKAKALMEKAGSNILGVILN 211
Cdd:cd02037  144 vsLIDVRKAIDMCKKLNIPVLGIVEN 169
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 42-79 1.96e-07

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: 48.31  E-value: 1.96e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 445959476  42 KRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGD 79
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 42-79 5.81e-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: 5.81e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 445959476  42 KRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGD 79
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
17-226 6.38e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 6.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  17 PKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPT--------QNYI 88
Cdd:COG3206  468 LLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLldllllllLLLL 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  89 FNEQNNNGLSSLIIGRTTMSEAITSTEIENLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQ 168
Cdd:COG3206  548 LLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLLAALLAAA 627

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445959476 169 LYARAIKDSLLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKAKVDKSSSYYHYYG 226
Cdd:COG3206  628 VLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYYY 685
minD CHL00175
septum-site determining protein; Validated
 35-209 4.20e-06

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 46.30  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  35 SKANGEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLII--GRTTMSEA-I 111
Cdd:CHL00175   9 EKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVleGECRLDQAlI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476 112 TSTEIENLDLLtagPVPPNPSEL-IGSERFKELVDLFNKR-YDIIIVD-----------------------TPPVNTVTD 166
Cdd:CHL00175  89 RDKRWKNLSLL---AISKNRQRYnVTRKNMNMLVDSLKNRgYDYILIDcpagidvgfinaiapaqeaivvtTPEITAIRD 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445959476 167 AQ-----LYARAIKDSLLVIDSEKND---KNEVKKAKALMEKAGSNILGVI 209
Cdd:CHL00175 166 ADrvaglLEANGIYNVKLLVNRVRPDmiqANDMMSVRDVQEMLGIPLLGAI 216
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 41-211 8.71e-06

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: 45.14  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476   41 VKR-LLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFN------EQNNNGLSSLII-GRTTMSeait 112
Cdd:pfam10609   2 VKHvIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGlegerpEQSDGGIIPVEAhGIKVMS---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  113 steienLDLLTagpvpPNPSELI---GSERFKELVDLFNKRY----DIIIVDTPPvNTvTDAQL-YARAIKDSLLVI--- 181
Cdd:pfam10609  78 ------IGFLL-----PDEDDAViwrGPMKSGAIKQFLTDVDwgelDYLIIDLPP-GT-GDEQLtLAQLLPLTGAVIvtt 144

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 445959476  182 -------DsekndkneVKKAKALMEKAGSNILGVILN 211
Cdd:pfam10609 145 pqdvallD--------VRKAIDMFKKVNVPVLGVVEN 173
PHA02518 PHA02518
ParA-like protein; Provisional
 42-88 6.11e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 42.53  E-value: 6.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 445959476  42 KRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYI 88
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWA 47
PRK10818 PRK10818
septum site-determining protein MinD;
44-159 8.84e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 42.62  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  44 LLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNN--NGLSSLIIGRTTMSEA-ITSTEIENLD 120
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRvvYDFVNVIQGDATLNQAlIKDKRTENLY 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 445959476 121 LLTAGPVpPNPSELIGSERFKELVDLFNKRYDIIIVDTP 159
Cdd:PRK10818  85 ILPASQT-RDKDALTREGVAKVLDDLKAMDFEFIVCDSP 122
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 39-160 9.26e-04

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.86  E-value: 9.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445959476  39 GEVKRLLVTSEKPGAGKSTVVSNVAITYAQAGYKTLVIDGDMRKPTQNyIF-----NEQNNNGLSSLIIGRTTMSEAITS 113
Cdd:NF041417 330 QKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQD-IFgtevgHEPTKVGVENLYAARIDQERALEE 408

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445959476 114 TEIENLDLLT------AGPV------------PPNPSELIGSERFKELVDLfnKRYDIIIVDTPP 160
Cdd:NF041417 409 YKTRMLDQVEqsfdkdQIDVeaakaqvreeleSPCAEEMAALEKFVSYFDV--DGYDVVVFDTAP 471
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 51-79 6.88e-03

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


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 36.22  E-value: 6.88e-03
                         10        20
                 ....*....|....*....|....*....
gi 445959476  51 PGAGKSTVVSNVAITYAQAGYKTLVIDGD 79
Cdd:COG0529   25 SGSGKSTLANALERRLFERGRHVYLLDGD 53
 
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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