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Conserved domains on  [gi|446390089|ref|WP_000467944|]
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MULTISPECIES: CpsD/CapB family tyrosine-protein kinase [Bacillus]

Protein Classification

CpsD/CapB family tyrosine-protein kinase( domain architecture ID 12941857)

CpsD/CapB family tyrosine-protein kinase is an autophosphorylating protein-tyrosine kinase that may be involved in the regulation of capsular polysaccharide biosynthesis

CATH:  3.40.50.300
EC:  2.7.10.2
Gene Ontology:  GO:0005524|GO:0004715|GO:0004713
PubMed:  22889913|19525115
SCOP:  4003987

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 25-214 4.49e-83

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: 245.17  E-value: 4.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  25 EQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLS 104
Cdd:cd05387    1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 105 GQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVVR 184
Cdd:cd05387   81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 446390089 185 SEKTEKDKIVKAKQILDKASGKILGVVLND 214
Cdd:cd05387  161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
 
Name Accession Description Interval E-value
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 25-214 4.49e-83

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: 245.17  E-value: 4.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  25 EQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLS 104
Cdd:cd05387    1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 105 GQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVVR 184
Cdd:cd05387   81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 446390089 185 SEKTEKDKIVKAKQILDKASGKILGVVLND 214
Cdd:cd05387  161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 25-225 2.54e-75

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: 226.16  E-value: 2.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   25 EQYRNIRTNIEFTSVDnhVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSN-GLTNLL 103
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAE--IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKItGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  104 SGQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVV 183
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446390089  184 RSEKTEKDKIVKAKQILDKASGKILGVVLNDKREEKEQYGYY 225
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYY 200
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 39-222 4.46e-73

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: 223.53  E-value: 4.46e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  39 VDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLSGQAKLMQCIQKTDI 118
Cdd:COG0489   88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEV 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 119 ENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVVRSEKTEKDKIVKAKQ 198
Cdd:COG0489  168 EGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALE 247

                        170       180
                 ....*....|....*....|....
gi 446390089 199 ILDKASGKILGVVLNDKREEKEQY 222
Cdd:COG0489  248 MLEKAGVPVLGVVLNMVCPKGERY 271
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
5-225 1.61e-39

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 143.75  E-value: 1.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   5 KKRKPLRQLITHKEPKSRITEQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRK 84
Cdd:PRK11519 488 IKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRK 567

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  85 PTIQNLFAIHSSNGLTNLLSGQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVL 164
Cdd:PRK11519 568 GYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPIL 647

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446390089 165 AVTDAQILANKCDGIVLVVRSEKTEKDKIVKAKQILDKASGKILGVVLND--KREEKEQ-YGYY 225
Cdd:PRK11519 648 AVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSifRRASAYQdYGYY 711
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 54-164 1.00e-11

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: 61.06  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLT--NLLSGQAKLMQCIQKTDIENVYLmaagpIPP 131
Cdd:pfam13614  12 GVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTiyELLIGECNIEEAIIKTVIENLDL-----IPS 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446390089  132 N------PAELLG----SRAMDEALLEAYNMFDIILIDTPPVL 164
Cdd:pfam13614  87 NidlagaEIELIGienrENILKEALEPVKDNYDYIIIDCPPSL 129
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 54-81 2.55e-03

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 37.77  E-value: 2.55e-03
                           10        20
                   ....*....|....*....|....*....
gi 446390089    54 GDGKTTTIANLAVVFGQQG-KKVLLIGAD 81
Cdd:smart00962  11 GVGKTTTIAKLAARLKLKGgKKVLLVAAD 39
 
Name Accession Description Interval E-value
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 25-214 4.49e-83

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: 245.17  E-value: 4.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  25 EQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLS 104
Cdd:cd05387    1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 105 GQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVVR 184
Cdd:cd05387   81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 446390089 185 SEKTEKDKIVKAKQILDKASGKILGVVLND 214
Cdd:cd05387  161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 25-225 2.54e-75

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: 226.16  E-value: 2.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   25 EQYRNIRTNIEFTSVDnhVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSN-GLTNLL 103
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAE--IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKItGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  104 SGQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVV 183
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446390089  184 RSEKTEKDKIVKAKQILDKASGKILGVVLNDKREEKEQYGYY 225
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYY 200
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 39-222 4.46e-73

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: 223.53  E-value: 4.46e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  39 VDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLSGQAKLMQCIQKTDI 118
Cdd:COG0489   88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEV 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 119 ENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDGIVLVVRSEKTEKDKIVKAKQ 198
Cdd:COG0489  168 EGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALE 247

                        170       180
                 ....*....|....*....|....
gi 446390089 199 ILDKASGKILGVVLNDKREEKEQY 222
Cdd:COG0489  248 MLEKAGVPVLGVVLNMVCPKGERY 271
EpsG TIGR03029
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ...
 12-214 4.15e-43

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: 146.16  E-value: 4.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   12 QLITHKEPKSRITEQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLF 91
Cdd:TIGR03029  72 DLIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNF 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   92 AIHSSNGLTNLLSGQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQI 171
Cdd:TIGR03029 152 KLSEQRGLSDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQI 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446390089  172 LANKCDGIVLVVRSEKTEKDKIVKAKQILDKASGKILGVVLND 214
Cdd:TIGR03029 232 VATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLNQ 274
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
5-225 1.61e-39

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 143.75  E-value: 1.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   5 KKRKPLRQLITHKEPKSRITEQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRK 84
Cdd:PRK11519 488 IKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRK 567

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  85 PTIQNLFAIHSSNGLTNLLSGQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVL 164
Cdd:PRK11519 568 GYTHELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPIL 647

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446390089 165 AVTDAQILANKCDGIVLVVRSEKTEKDKIVKAKQILDKASGKILGVVLND--KREEKEQ-YGYY 225
Cdd:PRK11519 648 AVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSifRRASAYQdYGYY 711
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 18-225 1.66e-39

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: 144.09  E-value: 1.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   18 EPKSRITEQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSN 97
Cdd:TIGR01005 528 APRSTFAEAFRNAKLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKP 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   98 GLTNLLSGQAKLMQCIQKTDIENVYLMAAGPI---PPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILAN 174
Cdd:TIGR01005 608 GLLDLLAGEASIEAGIHRDQRPGLAFIAAGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAA 687

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446390089  175 KCDGIVLVVRSEKTEKDKIVKAKQILDKASGKILGVVLND-KREEKEQYGYY 225
Cdd:TIGR01005 688 LADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFNAlDMNELGKYGDF 739
PRK09841 PRK09841
tyrosine-protein kinase;
19-225 1.56e-36

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 135.42  E-value: 1.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  19 PKSRITEQYRNIRTNIEFTSVDNHVRSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNG 98
Cdd:PRK09841 507 PADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNEHG 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  99 LTNLLSGQAKLMQCIQKTDIENVYLMAAGPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANKCDG 178
Cdd:PRK09841 587 LSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGT 666

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446390089 179 IVLVVRSEKTEKDKIVKAKQILDKASGKILGVVLND--KREE---KEQYGYY 225
Cdd:PRK09841 667 SLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGviKRAStaySYGYNYY 718
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 59-220 8.35e-20

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: 84.17  E-value: 8.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  59 TTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLSGQAKLMQCIQKTDiENVYLMAAGPIPPNPAELLG 138
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAELDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 139 SRAMDEALLEAYNMFDIILIDTPP-VLAVTDAQILAnkCDGIVLVVRSEKTE-KDkIVKAKQILDKASG-KILGVVLNDK 215
Cdd:COG0455   80 EERLIRVLEELERFYDVVLVDTGAgISDSVLLFLAA--ADEVVVVTTPEPTSiTD-AYALLKLLRRRLGvRRAGVVVNRV 156


                 ....*
gi 446390089 216 REEKE 220
Cdd:COG0455  157 RSEAE 161
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 44-213 1.33e-17

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


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 78.62  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLrkpTIQNLFAIHSSNG----LTNLLSGQAKLMQCIQKTDiE 119
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADI---TMANLELILGMEDkpvtLHDVLAGEADIKDAIYEGP-F 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  120 NVYLMAAGpippnpAELLGSRAMD-----EALLEAYNMFDIILIDTPPVLAVTDAQILANKcDGIVLVVRSEKTEKDKIV 194
Cdd:TIGR01969  77 GVKVIPAG------VSLEGLRKADpdkleDVLKEIIDDTDFLLIDAPAGLERDAVTALAAA-DELLLVVNPEISSITDAL 149

                         170
                  ....*....|....*....
gi 446390089  195 KAKQILDKASGKILGVVLN 213
Cdd:TIGR01969 150 KTKIVAEKLGTAILGVVLN 168
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 44-213 1.63e-16

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: 75.32  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLrkpTIQNLFAIHSSNG-----LTNLLSGQAKLMQCIQKTD- 117
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADI---GLRNLDLILGLENrivytLVDVLEGECRLEQALIKDKr 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 118 IENVYLMAAGPIPPNPAelLGSRAMDEALLEAYNMFDIILIDTPPVLAvTDAQILANKCDGIVLVVRSEKTEKDKIVKAK 197
Cdd:cd02036   78 WENLYLLPASQTRDKDA--LTPEKLEELVKELKDSFDFILIDSPAGIE-SGFINAIAPADEAIIVTNPEISSVRDADRVI 154

                        170
                 ....*....|....*.
gi 446390089 198 QILDKASGKILGVVLN 213
Cdd:cd02036  155 GLLESKGIVNIGLIVN 170
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 56-216 1.15e-14

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: 70.66  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  56 GKTTTIANLAVVFGQQGKKVLLIGADlrkPtiQ-NL---FAIHSSN---GLTNLLSGQAKLMQCIQKTDIENVYLmaagp 128
Cdd:COG1192   14 GKTTTAVNLAAALARRGKRVLLIDLD---P--QgNLtsgLGLDPDDldpTLYDLLLDDAPLEDAIVPTEIPGLDL----- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 129 IPPNP----AELLGSRAMD------EALLEAYNMFDIILIDTPPVLAV-TDAQILAnkCDGIVLVVRSEKTE-------K 190
Cdd:COG1192   84 IPANIdlagAEIELVSRPGrelrlkRALAPLADDYDYILIDCPPSLGLlTLNALAA--ADSVLIPVQPEYLSleglaqlL 161

                        170       180
                 ....*....|....*....|....*...
gi 446390089 191 DKIVKAKQILDKASgKILGVVLN--DKR 216
Cdd:COG1192  162 ETIEEVREDLNPKL-EILGILLTmvDPR 188
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 44-183 1.80e-13

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: 68.22  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  44 RSIIVTSADPGDGKTTTIANLAVVFGQQ-GKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLSG-----QAKLMQCIQKTD 117
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNpdrldETLLDRALTRHS 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446390089 118 iENVYLMAAgPIPPNPAELLGSRAMDEALLEAYNMFDIILIDTPPVLAVTDAQILANkCDGIVLVV 183
Cdd:COG4963  183 -SGLSVLAA-PADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEA-ADEVVLVT 245
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 54-164 1.00e-11

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: 61.06  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLT--NLLSGQAKLMQCIQKTDIENVYLmaagpIPP 131
Cdd:pfam13614  12 GVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTiyELLIGECNIEEAIIKTVIENLDL-----IPS 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446390089  132 N------PAELLG----SRAMDEALLEAYNMFDIILIDTPPVL 164
Cdd:pfam13614  87 NidlagaEIELIGienrENILKEALEPVKDNYDYIIIDCPPSL 129
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 44-162 3.30e-10

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: 57.96  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNLLSGQAKLMQCIQKTDiENVYL 123
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGP-EGLDI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446390089 124 MAAGPIPPNPAElLGSRAMD---EALLEAYNMFDIILIDTPP 162
Cdd:cd02038   80 IPGGSGMEELAN-LDPEQKAkliEELSSLESNYDYLLIDTGA 120
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 46-218 1.38e-09

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: 56.20  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   46 IIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADlrkPTIQNLFAIHSSNG-------LTNLLSGQAKLMQCIQKTDI 118
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLD---PQSNNSSVEGLEGDiapalqaLAEGLKGRVNLDPILLKEKS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  119 E--NVYLMAAGPIPPNPAELLGSRAMDEALLEAYN----MFDIILIDTPP---------------VLAVTDAQILA-NKC 176
Cdd:pfam01656  78 DegGLDLIPGNIDLEKFEKELLGPRKEERLREALEalkeDYDYVIIDGAPglgellrnaliaadyVIIPLEPEVILvEDA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446390089  177 DGIVLVVRsektekdKIVKAKQILDKasgKILGVVLNDKREE 218
Cdd:pfam01656 158 KRLGGVIA-------ALVGGYALLGL---KIIGVVLNKVDGD 189
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 46-213 1.80e-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: 49.81  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  46 IIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFaihssnGLTNllsgqAKLMQC---IQKTDIENVY 122
Cdd:cd02037    3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLL------GVEG-----KPLHQSeegIVPVEVGGIK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089 123 LMAAGPI-PPNPAELLGSRAMDEALLE-----AYNMFDIILIDTPPvlAVTDAQI-LAN--KCDGIVLV----------V 183
Cdd:cd02037   72 VMSIGFLlPEDDAVIWRGPMKSGAIKQflkdvDWGELDYLIIDLPP--GTGDEHLsLVQliPIDGAVVVttpqevslidV 149

                        170       180       190
                 ....*....|....*....|....*....|
gi 446390089 184 RSEktekdkIVKAKqildKASGKILGVVLN 213
Cdd:cd02037  150 RKA------IDMCK----KLNIPVLGIVEN 169
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 44-81 2.09e-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: 47.81  E-value: 2.09e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446390089  44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PRK10818 PRK10818
septum site-determining protein MinD;
44-161 1.35e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 48.01  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLrkpTIQNLFAIHSSN-----GLTNLLSGQAKLMQC-IQKTD 117
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDI---GLRNLDLIMGCErrvvyDFVNVIQGDATLNQAlIKDKR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446390089 118 IENVYLMAAGPIPPNPAelLGSRAMDEALLEAYNM-FDIILIDTP 161
Cdd:PRK10818  80 TENLYILPASQTRDKDA--LTREGVAKVLDDLKAMdFEFIVCDSP 122
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 54-160 1.66e-06

GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349786  Cd Length: 193  Bit Score: 46.82  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNlfaihssngltnllsgqaKLMQCIQKTDIEnVYLMAAGPIPPNP 133
Cdd:cd18539   10 GSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIE------------------QLQTLGEQVGVP-VFESGDGQSPVDI 70

                         90       100
                 ....*....|....*....|....*..
gi 446390089 134 AEllgsRAMDEALLeayNMFDIILIDT 160
Cdd:cd18539   71 AK----RALEKAKE---EGFDVVIVDT 90
minD CHL00175
septum-site determining protein; Validated
 44-161 2.14e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 44.38  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFAIHSSNGLTNL--LSGQAKLMQC-IQKTDIEN 120
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMdvLEGECRLDQAlIRDKRWKN 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446390089 121 VYLMaagPIPPNPAELLGSRAMDEALLEAYNM--FDIILIDTP 161
Cdd:CHL00175  96 LSLL---AISKNRQRYNVTRKNMNMLVDSLKNrgYDYILIDCP 135
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 46-91 2.34e-05

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 44.44  E-value: 2.34e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446390089  46 IIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLF 91
Cdd:cd02033   33 IIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLF 78
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 54-81 2.43e-05

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 43.68  E-value: 2.43e-05
                          10        20
                  ....*....|....*....|....*...
gi 446390089   54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:pfam00448  10 GSGKTTTIAKLAAYLKKKGKKVLLVAAD 37
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
 54-81 2.48e-05

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 44.32  E-value: 2.48e-05
                         10        20
                 ....*....|....*....|....*...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:PRK10416 124 GVGKTTTIGKLAHKYKAQGKKVLLAAGD 151
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
 54-81 3.43e-05

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


Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 43.86  E-value: 3.43e-05
                         10        20
                 ....*....|....*....|....*...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:COG0552  110 GVGKTTTIGKLAHRLKAEGKSVLLAAGD 137
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
41-90 3.57e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.88  E-value: 3.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446390089  41 NHVRSII-VTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNL 90
Cdd:PRK11670 104 NGVKNIIaVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTM 154
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 56-81 3.92e-05

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: 42.14  E-value: 3.92e-05
                         10        20
                 ....*....|....*....|....*.
gi 446390089  56 GKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:cd02042   13 GKTTLAVNLAAALALRGKRVLLIDLD 38
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
 5-81 5.83e-05

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


Pssm-ID: 272883 [Multi-domain]  Cd Length: 277  Bit Score: 43.01  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089    5 KKRKPLRQLITHKEPKSRITEQYRNIRTNIEFTSVDNHVRS------IIVTSADPGDGKTTTIANLAVVFGQQGKKVLLI 78
Cdd:TIGR00064  32 KKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDLELIVeenkpnVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLA 111


                  ...
gi 446390089   79 GAD 81
Cdd:TIGR00064 112 AGD 114
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 43-213 7.37e-05

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 42.44  E-value: 7.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   43 VRSII-VTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFaihssnGLTNLLSGQAKLMqcIQKTDIENV 121
Cdd:pfam10609   2 VKHVIaVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRML------GLEGERPEQSDGG--IIPVEAHGI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  122 YLMAAGPIPPNPaellgsramDEALL-------EAYNMF---------DIILIDTPP-----VLAVtdAQILANkcDGIV 180
Cdd:pfam10609  74 KVMSIGFLLPDE---------DDAVIwrgpmksGAIKQFltdvdwgelDYLIIDLPPgtgdeQLTL--AQLLPL--TGAV 140

                         170       180       190
                  ....*....|....*....|....*....|...
gi 446390089  181 LVVRSEKTEKDKIVKAKQILDKASGKILGVVLN 213
Cdd:pfam10609 141 IVTTPQDVALLDVRKAIDMFKKVNVPVLGVVEN 173
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 54-160 8.38e-05

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 41.98  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTiqnlfAIHSSNGLTNLLsgQAKLMQCIQKTDienvylmaagpippnP 133
Cdd:cd03115   10 GSGKTTTLAKLARYYQEKGKKVLLIAADTFRAA-----AVEQLKTLAEKL--GVPVFESYTGTD---------------P 67

                         90       100
                 ....*....|....*....|....*..
gi 446390089 134 AELLgSRAMDEALLEAYnmfDIILIDT 160
Cdd:cd03115   68 ASIA-QEAVEKAKLEGY---DVLLVDT 90
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 54-81 1.84e-04

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 41.58  E-value: 1.84e-04
                         10        20
                 ....*....|....*....|....*...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:cd02117   10 GIGKSTTASNLSAALAEGGKKVLHVGCD 37
FtsY cd17874
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ...
 54-81 2.88e-04

signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.


Pssm-ID: 349783  Cd Length: 199  Bit Score: 40.25  E-value: 2.88e-04
                         10        20
                 ....*....|....*....|....*...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:cd17874   10 GVGKTTTIGKLAHYLKNQGKKVVLAAGD 37
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 54-81 5.01e-04

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: 40.19  E-value: 5.01e-04
                         10        20
                 ....*....|....*....|....*...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:cd02040   10 GIGKSTTASNLSAALAEMGKKVLHVGCD 37
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 54-90 6.30e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 39.75  E-value: 6.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNL 90
Cdd:PRK13230  11 GIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNL 47
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
54-159 8.32e-04

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 39.35  E-value: 8.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPTIQNLFaiHSSNGLTNL-LSGQAKLMQCIQKTDI-----ENVYLMAAG 127
Cdd:pfam00142  10 GIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLL--GGKLQPTVLdTAREKGYVEDVEVEDVvykgyGGVKCVESG 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446390089  128 piPPNPAELLGSRAMDEA--LLE---AYNMFDIILID 159
Cdd:pfam00142  88 --GPEPGVGCAGRGVITAinLLEelgAYDDLDFVLYD 122
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 46-183 1.20e-03

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 38.87  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   46 IIVTSADPGDGKTTTIANLAVVFGQQGKKVLLIGADlrkptIQNLFAIH------SSNGLTNLLSGQAKLMQCIQKtDIE 119
Cdd:TIGR03371   4 IAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLD-----PQNLLRLHfgmdwsVRDGWARALLNGADWAAAAYR-SPD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446390089  120 NVYLMAAGpiPPNPAELLGSRAMDEALLeaYNMF--------DIILIDTPPVLAVTDAQILAnkCDGIVLVV 183
Cdd:TIGR03371  78 GVLFLPYG--DLSADEREAYQAHDAGWL--ARLLqqldlaarDWVLIDLPRGPSPITRQALA--AADLVLVV 143
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 44-223 2.20e-03

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 38.01  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089   44 RSIIVTSADPGDGKTTTIANLAVVFGQQGKKVlligaDLRKPTIQNLfaihSSNGLTNLLSGQAKLMQCIQktDIENVYL 123
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKV-----GYWKPVQTGL----VEDGDSELVKRLLGLDQSYE--DPEPFRL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  124 MAagpipPNPAELLGSRAMDEALLEAYNM-----FDIILI------DTPPVLAVTDAQILANKCDGIVLVVRSEKTEKDK 192
Cdd:pfam13500  70 SA-----PLSPHLAARQEGVTIDLEKIIYelpadADPVVVegagglLVPINEDLLNADIAANLGLPVILVARGGLGTINH 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446390089  193 IVKAKQILDKASGKILGVVLN-----DKREEKEQYG 223
Cdd:pfam13500 145 TLLTLEALRQRGIPVLGVILNgvpnpENVRTIFAFG 180
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 54-81 2.55e-03

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 37.77  E-value: 2.55e-03
                           10        20
                   ....*....|....*....|....*....
gi 446390089    54 GDGKTTTIANLAVVFGQQG-KKVLLIGAD 81
Cdd:smart00962  11 GVGKTTTIAKLAARLKLKGgKKVLLVAAD 39
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 56-162 3.51e-03

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: 37.49  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  56 GKTTTIANLAVVFGQQGKKVLLI----------------GADLRKPTIQNLFA--IHSSNGLTNLLSG-QAKLMQCIQKT 116
Cdd:cd02035   12 GKTTIAAATAVRLAEQGKRVLLVstdpahslsdafgqklGGETPVKGAPNLWAmeIDPEEALEEYWEEvKELLAQYLRLP 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446390089 117 DIENVYLMAAGPIPpnpaellGsraMDEA--------LLEAYNmFDIILIDTPP 162
Cdd:cd02035   92 GLDEVYAEELLSLP-------G---MDEAaafdelreYVESGE-YDVIVFDTAP 134
PHA02518 PHA02518
ParA-like protein; Provisional
 54-86 5.31e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 36.75  E-value: 5.31e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGADLRKPT 86
Cdd:PHA02518  11 GAGKTTVATNLASWLHADGHKVLLVDLDPQGSS 43
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 53-161 6.16e-03

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 36.37  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446390089  53 PGDGKTTTIANLAVVF-GQQGKKVLLIGAD-LRKPTIQNLFAIhssngltnllsgqAKLMqciqktdieNVYLMAAgpip 130
Cdd:cd17873    9 TGVGKTTTLAKLAARYvLKKGKKVALITTDtYRIGAVEQLKTY-------------AEIM---------GIPVEVA---- 62

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446390089 131 PNPAELlgsramdEALLEAYNMFDIILIDTP 161
Cdd:cd17873   63 EDPEDL-------ADALERLSDRDLILIDTA 86
SRP54_G cd17875
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ...
 54-81 7.82e-03

GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349784  Cd Length: 193  Bit Score: 36.02  E-value: 7.82e-03
                         10        20
                 ....*....|....*....|....*...
gi 446390089  54 GDGKTTTIANLAVVFGQQGKKVLLIGAD 81
Cdd:cd17875   10 GSGKTTTAAKLAYYYQKKGYKVGLVCAD 37
 
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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