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Conserved domains on  [gi|742400850|ref|WP_038879975|]
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MULTISPECIES: AAA family ATPase [Serratia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA_partition super family cl49513
ParA family partition ATPase;
2-208 5.89e-47

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 153.48  E-value: 5.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAGYLILkQGKTAIIVDADDQKSIMTWYNDRqnvEGLPHIPVVAASG-KIKETLLELDRHY 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR-RGYRVLLVDADPQGSALDWAAAR---EDERPFPVVGLARpTLHRELPSLARDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEKVKGYIVLNMCPTNIFIneANEAAQV 160
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL--GREVAEA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 742400850 161 LSEYPeFTLVSHRLCDRKIYRDAWGEAITVHEAN-NEKAQSEIECLVKE 208
Cdd:NF041546 155 LAEYG-LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
2-208 5.89e-47

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 153.48  E-value: 5.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAGYLILkQGKTAIIVDADDQKSIMTWYNDRqnvEGLPHIPVVAASG-KIKETLLELDRHY 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR-RGYRVLLVDADPQGSALDWAAAR---EDERPFPVVGLARpTLHRELPSLARDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEKVKGYIVLNMCPTNIFIneANEAAQV 160
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL--GREVAEA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 742400850 161 LSEYPeFTLVSHRLCDRKIYRDAWGEAITVHEAN-NEKAQSEIECLVKE 208
Cdd:NF041546 155 LAEYG-LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-211 1.13e-37

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 129.97  E-value: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQKSIMTWYNDRQnvEGLPHIPVVAASGKIKETLLELDRHY 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWL-HADGHKVLLVDLDPQGSSTDWAEARE--EGEPLIPVVRMGKSIRADLPKVASGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEKVKGYIVLNMCPTNIFINEAnEAAQV 160
Cdd:PHA02518  78 DYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYR-EARKA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742400850 161 LSEYpEFTLVSHRLCDRKIYRDA--WGEAITVHEaNNEKAQSEIECLVKEVIL 211
Cdd:PHA02518 157 LAGY-GLPILRNGTTQRVAYADAaeAGGSVLELP-EDDKAAEEIIQLVKELFR 207
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-162 5.81e-34

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: 117.64  E-value: 5.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQKSIMTWYndrqnveglphipvvaasgkiketlleldrhY 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAAL-ALRGKRVLLIDLDPQGSLTSWL-------------------------------Y 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEK--VKGYIVLNMCPTNifINEANEAA 158
Cdd:cd02042   49 DYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPR--TKLAREVL 126


                 ....
gi 742400850 159 QVLS 162
Cdd:cd02042  127 EELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-210 1.77e-23

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: 94.15  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQ---------------KSIMTWYNDRQNVEGL------PH 59
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAAL-ARRGKRVLLIDLDPQgnltsglgldpddldPTLYDLLLDDAPLEDAivpteiPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  60 IPVVAASG-----------------KIKETLLELDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYL 122
Cdd:COG1192   81 LDLIPANIdlagaeielvsrpgrelRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850 123 SEMFSTAQE-YNEKVK-GYIVLNMcptniFINEANEAAQVLSEYPEFtlVSHRLCDRKI-----YRDAWGEAITVHE-AN 194
Cdd:COG1192  161 LETIEEVREdLNPKLEiLGILLTM-----VDPRTRLSREVLEELREE--FGDKVLDTVIprsvaLAEAPSAGKPVFEyDP 233

                        250
                 ....*....|....*.
gi 742400850 195 NEKAQSEIECLVKEVI 210
Cdd:COG1192  234 KSKGAKAYRALAEELL 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-141 2.25e-13

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 66.22  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    3 VLIGSQKGGVGKSTKAVNIAGYLIlKQGKTAIIVDADDQKSIMTW----------------------------YNDRQNV 54
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALA-RRGLRVLLIDLDPQSNNSSVeglegdiapalqalaeglkgrvnldpilLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   55 EGLPHIP-------------VVAASGKIKETLLELDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGY 121
Cdd:pfam01656  80 GGLDLIPgnidlekfekellGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180
                  ....*....|....*....|....
gi 742400850  122 LSEMFSTAQEYNE----KVKGYIV 141
Cdd:pfam01656 160 LGGVIAALVGGYAllglKIIGVVL 183
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 2-90 1.72e-08

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: 52.41  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850     2 IVLIGSQkgGVGKSTKAVNIAGYLILKQGKTAIIVDAD-------DQksIMTWyNDRQNVEGLPHIPVVAASGKIKETL- 73
Cdd:smart00962   4 ILLVGPN--GVGKTTTIAKLAARLKLKGGKKVLLVAADtfraaavEQ--LKTY-AEILGVVPVAGGEGADPVAVAKDAVe 78

                           90
                   ....*....|....*..
gi 742400850    74 LELDRHYDYVIVDTAGR 90
Cdd:smart00962  79 LAKARGYDVVLIDTAGR 95
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 2-88 4.28e-06

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: 45.51  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    2 IVLIGSQKGGVGKSTKAVNIAgYLILKQGKTAIIVDADDQKSIMTWYNDRQN-----------------------VEGL- 57
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIA-IAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkitgltnflsgttdlsdaicdtnIENLd 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 742400850   58 --------PHIPVVAASGKIKETLLELDRHYDYVIVDTA 88
Cdd:TIGR01007  98 vitagpvpPNPTELLQSSNFKTLIETLRKRFDYIIIDTP 136
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
2-208 5.89e-47

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 153.48  E-value: 5.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAGYLILkQGKTAIIVDADDQKSIMTWYNDRqnvEGLPHIPVVAASG-KIKETLLELDRHY 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR-RGYRVLLVDADPQGSALDWAAAR---EDERPFPVVGLARpTLHRELPSLARDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEKVKGYIVLNMCPTNIFIneANEAAQV 160
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL--GREVAEA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 742400850 161 LSEYPeFTLVSHRLCDRKIYRDAWGEAITVHEAN-NEKAQSEIECLVKE 208
Cdd:NF041546 155 LAEYG-LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-211 1.13e-37

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 129.97  E-value: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQKSIMTWYNDRQnvEGLPHIPVVAASGKIKETLLELDRHY 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWL-HADGHKVLLVDLDPQGSSTDWAEARE--EGEPLIPVVRMGKSIRADLPKVASGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEKVKGYIVLNMCPTNIFINEAnEAAQV 160
Cdd:PHA02518  78 DYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYR-EARKA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742400850 161 LSEYpEFTLVSHRLCDRKIYRDA--WGEAITVHEaNNEKAQSEIECLVKEVIL 211
Cdd:PHA02518 157 LAGY-GLPILRNGTTQRVAYADAaeAGGSVLELP-EDDKAAEEIIQLVKELFR 207
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-162 5.81e-34

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: 117.64  E-value: 5.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQKSIMTWYndrqnveglphipvvaasgkiketlleldrhY 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAAL-ALRGKRVLLIDLDPQGSLTSWL-------------------------------Y 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  81 DYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAQEYNEK--VKGYIVLNMCPTNifINEANEAA 158
Cdd:cd02042   49 DYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPR--TKLAREVL 126


                 ....
gi 742400850 159 QVLS 162
Cdd:cd02042  127 EELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-210 1.77e-23

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: 94.15  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQ---------------KSIMTWYNDRQNVEGL------PH 59
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAAL-ARRGKRVLLIDLDPQgnltsglgldpddldPTLYDLLLDDAPLEDAivpteiPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  60 IPVVAASG-----------------KIKETLLELDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYL 122
Cdd:COG1192   81 LDLIPANIdlagaeielvsrpgrelRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850 123 SEMFSTAQE-YNEKVK-GYIVLNMcptniFINEANEAAQVLSEYPEFtlVSHRLCDRKI-----YRDAWGEAITVHE-AN 194
Cdd:COG1192  161 LETIEEVREdLNPKLEiLGILLTM-----VDPRTRLSREVLEELREE--FGDKVLDTVIprsvaLAEAPSAGKPVFEyDP 233

                        250
                 ....*....|....*.
gi 742400850 195 NEKAQSEIECLVKEVI 210
Cdd:COG1192  234 KSKGAKAYRALAEELL 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-141 2.25e-13

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 66.22  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    3 VLIGSQKGGVGKSTKAVNIAGYLIlKQGKTAIIVDADDQKSIMTW----------------------------YNDRQNV 54
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALA-RRGLRVLLIDLDPQSNNSSVeglegdiapalqalaeglkgrvnldpilLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   55 EGLPHIP-------------VVAASGKIKETLLELDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGY 121
Cdd:pfam01656  80 GGLDLIPgnidlekfekellGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180
                  ....*....|....*....|....
gi 742400850  122 LSEMFSTAQEYNE----KVKGYIV 141
Cdd:pfam01656 160 LGGVIAALVGGYAllglKIIGVVL 183
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-120 2.51e-12

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: 64.01  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    2 IVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDADDQKSIMTWY-------NDRQNVEgLP-----HIPVVAAS--- 66
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVAL-LYKGARVAAIDLDLRQRTFHRYfenrsatADRTGLS-LPtpehlNLPDNDVAevp 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742400850   67 -------GKIKETLLELDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVG 120
Cdd:pfam09140  80 dgeniddARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLLG 140
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-148 5.37e-12

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: 63.28  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAgYLILKQGKTAIIVDAD-------------DQKSIMTWYNDRQNVE------GLPHIPV 62
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLA-LALAQSGKRVLLIDADlrgpslhrmlgleNRPGLSDVLAGEASLEdviqptEVEGLDV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  63 VAA------------SGKIKETLLELDRHYDYVIVDTA-GRDSAELRSGLLAAD--LFLSplRPSQMDLDTVGYLSEMFs 127
Cdd:COG0489  173 LPAgplppnpsellaSKRLKQLLEELRGRYDYVIIDTPpGLGVADATLLASLVDgvLLVV--RPGKTALDDVRKALEML- 249

                        170       180
                 ....*....|....*....|.
gi 742400850 128 taQEYNEKVKGyIVLNMCPTN 148
Cdd:COG0489  250 --EKAGVPVLG-VVLNMVCPK 267
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 1-161 2.07e-10

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: 58.97  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSqKGGVGKSTKAVNIAGYLILKQGKTAIIVDAD----------DQKSIMTWYNDRQNVEGL------------- 57
Cdd:COG4963  104 VIAVVGA-KGGVGATTLAVNLAWALARESGRRVLLVDLDlqfgdvalylDLEPRRGLADALRNPDRLdetlldraltrhs 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  58 PHIPVVAASGKIK----------ETLLE-LDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLrpsQMDL----DTVGYL 122
Cdd:COG4963  183 SGLSVLAAPADLEraeevspeavERLLDlLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVT---EPDLpslrNAKRLL 259

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 742400850 123 sEMFSTAQEYNEKVKgyIVLNMCPTNIFINeANEAAQVL 161
Cdd:COG4963  260 -DLLRELGLPDDKVR--LVLNRVPKRGEIS-AKDIEEAL 294
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-103 6.70e-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: 56.81  E-value: 6.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAgYLILKQGKTAIIVDAD-------------DQKSIMTWYNDRQN-----VEGLPHIPVV 63
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLA-LALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSlediiVEGPEGLDII 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 742400850  64 AAS--------------GKIKETLLELDRHYDYVIVDTAGRDSAELRSGLLAAD 103
Cdd:cd02038   81 PGGsgmeelanldpeqkAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAAD 134
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 2-90 1.72e-08

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: 52.41  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850     2 IVLIGSQkgGVGKSTKAVNIAGYLILKQGKTAIIVDAD-------DQksIMTWyNDRQNVEGLPHIPVVAASGKIKETL- 73
Cdd:smart00962   4 ILLVGPN--GVGKTTTIAKLAARLKLKGGKKVLLVAADtfraaavEQ--LKTY-AEILGVVPVAGGEGADPVAVAKDAVe 78

                           90
                   ....*....|....*..
gi 742400850    74 LELDRHYDYVIVDTAGR 90
Cdd:smart00962  79 LAKARGYDVVLIDTAGR 95
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-132 3.42e-08

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: 51.05  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    2 IVLIGSQKGGVGKSTKAVNIAgYLILKQGKTAIIVDADDQ---------------KSIMTWYNDRQNVEG---------- 56
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLA-AALAKKGKKVLLIDLDPQgnatsglgidknnveKTIYELLIGECNIEEaiiktvienl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   57 --LP-HIPVVAASGK----------IKETLLELDRHYDYVIVDTAGRDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLS 123
Cdd:pfam13614  82 dlIPsNIDLAGAEIEligienreniLKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLL 161


                  ....*....
gi 742400850  124 EMFSTAQEY 132
Cdd:pfam13614 162 NTIKLVKKR 170
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-39 5.41e-08

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: 50.96  E-value: 5.41e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAGYLIlKQGKTAIIVDAD 39
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALA-KKGYKVGLLDAD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-39 1.16e-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: 47.45  E-value: 1.16e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 742400850    2 IVLIGSQKGGVGKSTKAVNIAGYLiLKQGKTAIIVDAD 39
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALAL-ARLGYKVGLLDAD 41
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 2-88 4.28e-06

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: 45.51  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    2 IVLIGSQKGGVGKSTKAVNIAgYLILKQGKTAIIVDADDQKSIMTWYNDRQN-----------------------VEGL- 57
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIA-IAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkitgltnflsgttdlsdaicdtnIENLd 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 742400850   58 --------PHIPVVAASGKIKETLLELDRHYDYVIVDTA 88
Cdd:TIGR01007  98 vitagpvpPNPTELLQSSNFKTLIETLRKRFDYIIIDTP 136
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 2-90 6.82e-06

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: 44.84  E-value: 6.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    2 IVLIGSQkgGVGKSTKAVNIAGYLiLKQGKTAIIVDAD-------DQksiMTWYNDRQNVEGLPHI----PVVAASGKIK 70
Cdd:pfam00448   3 ILLVGLQ--GSGKTTTIAKLAAYL-KKKGKKVLLVAADtfraaaiEQ---LKQLAEKLGVPVFGSKtgadPAAVAFDAVE 76

                          90       100
                  ....*....|....*....|
gi 742400850   71 EtllELDRHYDYVIVDTAGR 90
Cdd:pfam00448  77 K---AKAENYDVVLVDTAGR 93
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 7-184 7.62e-06

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 45.25  E-value: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850    7 SQKGGVGKSTKAVNIAGYLILKqGKTAIIVDADDQKSIMTW---------YNDRQNVEGLPHIPVVAASGKIKETlleld 77
Cdd:pfam07015   8 SFKGGAGKTTALMGLCSALASD-GKRVALFEADENRPLTKWrenalrkgtWDPACEIFNADELPLLEQAYEHAEG----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   78 RHYDYVIVDTAGrDSAELRSGLLA-ADLFLSP--LRPSQMD--LDTVGYLSEMFSTAqeyNEKVKGYIVLNMCPTNIFIN 152
Cdd:pfam07015  82 SGFDYALADTHG-GSSELNNTIIAsSDLLLIPtmLTPLDIDeaLATYRYVIELLLTE---NLAIPTAILRQRVPVGRLTS 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 742400850  153 EANEAAQVLSEYPEFTLVSHrlcdrkiYRDAW 184
Cdd:pfam07015 158 SQRFCSDMLEQLPVFDCPMH-------ERDAF 182
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-164 4.20e-05

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: 42.95  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  18 AVNIAGYLIlKQGKTAIIVDAD-------------DQKSIMTWYNDRQNVE-----------------GLPHIPVVAASG 67
Cdd:COG0455    3 AVNLAAALA-RLGKRVLLVDADlglanldvllglePKATLADVLAGEADLEdaivqgpggldvlpggsGPAELAELDPEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850  68 KIKETLLELDRHYDYVIVDT-AGRdSAELRSGLLAADLFLSPLRPsqmDLDTVGYLSEMFSTAQEYNEKVKGYIVLNMC- 145
Cdd:COG0455   82 RLIRVLEELERFYDVVLVDTgAGI-SDSVLLFLAAADEVVVVTTP---EPTSITDAYALLKLLRRRLGVRRAGVVVNRVr 157

                        170
                 ....*....|....*....
gi 742400850 146 PTNIFINEANEAAQVLSEY 164
Cdd:COG0455  158 SEAEARDVFERLEQVAERF 176
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-88 5.03e-05

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: 42.56  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAgYLILKQGKTAIIVDADDQKSIMTWYNDRQNVEGL------------------------ 57
Cdd:cd05387   21 VIAVTSASPGEGKSTVAANLA-VALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLsevlsgqasledviqstnipnldv 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 742400850  58 -------PHIPVVAASGKIKETLLELDRHYDYVIVDTA 88
Cdd:cd05387  100 lpagtvpPNPSELLSSPRFAELLEELKEQYDYVIIDTP 137
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-39 9.56e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 42.34  E-value: 9.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAGYLIlKQGKTAIIVDAD 39
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALA-AEGAKVGILDAD 145
Ffh COG0541
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ...
 2-90 1.51e-04

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


Pssm-ID: 440307 [Multi-domain]  Cd Length: 423  Bit Score: 41.93  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQkgGVGKSTKAVNIAGYLIlKQGKTAIIVDAD-------DQKSIMTwynDRQNVEGLPHI----PVVAASGKIK 70
Cdd:COG0541  103 IMMVGLQ--GSGKTTTAAKLAKYLK-KKGKKPLLVAADvyrpaaiEQLKTLG---EQIGVPVFPEEdgkdPVDIAKRALE 176

                         90       100
                 ....*....|....*....|
gi 742400850  71 ETLLEldrHYDYVIVDTAGR 90
Cdd:COG0541  177 YAKKN---GYDVVIVDTAGR 193
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 2-90 1.63e-04

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: 41.04  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQkgGVGKSTKAVNIAGYLIlKQGKTAIIVDAD-------DQKSIMtwyNDRQNVEGLPHI----PVVAASGKIK 70
Cdd:cd18539    3 ILLVGLQ--GSGKTTTAAKLALYLK-KKGKKVLLVAADvyrpaaiEQLQTL---GEQVGVPVFESGdgqsPVDIAKRALE 76

                         90       100
                 ....*....|....*....|
gi 742400850  71 ETLLEldrHYDYVIVDTAGR 90
Cdd:cd18539   77 KAKEE---GFDVVIVDTAGR 93
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 2-104 2.00e-04

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: 40.61  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQkgGVGKSTKAVNIAGYLILKQGKTAIIVDAD-------DQksiMTWYNDRQNveglphIPVVAA-SGKIKETL 73
Cdd:cd17873    3 IALVGPT--GVGKTTTLAKLAARYVLKKGKKVALITTDtyrigavEQ---LKTYAEIMG------IPVEVAeDPEDLADA 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 742400850  74 LELDRHYDYVIVDTAGR------DSAELRsGLLAADL 104
Cdd:cd17873   72 LERLSDRDLILIDTAGRsprdkeQLEELK-ELLGAGE 107
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 2-90 2.90e-04

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: 40.05  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQkgGVGKSTKAVNIAGYLILKQGKTAIIvdADDQKSIMTWYNDRQNVEGLpHIPVVAASGKIKETLLELD---- 77
Cdd:cd03115    3 ILLVGLQ--GSGKTTTLAKLARYYQEKGKKVLLI--AADTFRAAAVEQLKTLAEKL-GVPVFESYTGTDPASIAQEavek 77

                         90
                 ....*....|....*.
gi 742400850  78 ---RHYDYVIVDTAGR 90
Cdd:cd03115   78 aklEGYDVLLVDTAGR 93
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-39 6.39e-04

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: 39.49  E-value: 6.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIaGYLILKQGKTAIIVDAD 39
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANL-GVALAKLGKKVLLIDAD 38
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
2-90 8.05e-04

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.46  E-value: 8.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQkgGVGKSTKAVNIAGYLILKQGKT-AII-VD-----ADDQ-KS---IMtwyndrqnveGLPHIpVVAASGKIK 70
Cdd:COG1419  167 IALVGPT--GVGKTTTIAKLAARFVLRGKKKvALItTDtyrigAVEQlKTyarIL----------GVPVE-VAYDPEELK 233

                         90       100
                 ....*....|....*....|
gi 742400850  71 ETLLELdRHYDYVIVDTAGR 90
Cdd:COG1419  234 EALERL-RDKDLVLIDTAGR 252
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-144 1.63e-03

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 36.64  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   1 MIVLIGSQKGGVGKSTKAVNIAGYLILKqGKTAIIVDADdqksimtwyndrqnveglphipvvaasgkiketlleldrhy 80
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD----------------------------------------- 38

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742400850  81 DYVIVDTAG-------RDSAELRSGLLAADLFLSPLRPSQMDLDTVGYLSEMFSTAqeYNEKVKGYIVLNM 144
Cdd:cd01983   39 DYVLIDGGGgletgllLGTIVALLALKKADEVIVVVDPELGSLLEAVKLLLALLLL--GIGIRPDGIVLNK 107
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-39 3.69e-03

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 37.32  E-value: 3.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 742400850    2 IVLIGSQKGGVGKSTKAVNIaGYLILKQGKTAIIVDAD 39
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANL-GTALARLGKKVVLIDAD 39
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 9-89 4.09e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 37.07  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   9 KGGVGKSTKAVNIAGYLIlKQGKTAIIVDAD-------------DQKSIMT------------------WYNDRQNVEGL 57
Cdd:COG3640    8 KGGVGKTTLSALLARYLA-EKGKPVLAVDADpnanlaealglevEADLIKPlgemrelikertgapgggMFKLNPKVDDI 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 742400850  58 PHIPVV-------AASGKIKE----------TLLE------LDRHYDYVIVDT-AG 89
Cdd:COG3640   87 PEEYLVegdgvdlLVMGTIEEggsgcycpenALLRallnhlVLGNYEYVVVDMeAG 142
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 2-94 5.07e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 37.11  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742400850   2 IVLIGSQkgGVGKSTKAVNIAGYLIlKQGKTAIIVDAD-------DQKSIMTwynDRQNVE--GLPHI--PVvaasgKIK 70
Cdd:PRK00771  98 IMLVGLQ--GSGKTTTAAKLARYFK-KKGLKVGLVAADtyrpaayDQLKQLA---EKIGVPfyGDPDNkdAV-----EIA 166

                         90       100
                 ....*....|....*....|....
gi 742400850  71 ETLLELDRHYDYVIVDTAGRDSAE 94
Cdd:PRK00771 167 KEGLEKFKKADVIIVDTAGRHALE 190
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-39 6.14e-03

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 36.57  E-value: 6.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 742400850   2 IVLIGSQKGGVGKSTKAVNIAGYLIlKQGKTAIIVDAD 39
Cdd:COG2894    4 VIVVTSGKGGVGKTTTTANLGTALA-LLGKKVVLIDAD 40
 
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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