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Conserved domains on  [gi|488255619|ref|WP_002326827|]
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MULTISPECIES: ParA family protein [Bacteria]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

Gene Ontology:  GO:0005524
PubMed:  26339031|21963112|22672910|14584729

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 44-290 4.31e-43

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: 148.08  E-value: 4.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  44 FKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLAktFEVELPRVNFYEGLKNGNLASSIVHLT--DNLDLIPG 121
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLLDDAPLEDAIVPTeiPGLDLIPA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 122 TFDLMLLPKLTRSwtFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQNYISYL 201
Cdd:COG1192   87 NIDLAGAEIELVS--RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 202 IDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEELYKQHKEdnLVFQNIIKRSNKVSTWSKNGITEHKgYDK--KVLSMY 279
Cdd:COG1192  165 EEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGD--KVLDTVIPRSVALAEAPSAGKPVFE-YDPksKGAKAY 241

                        250
                 ....*....|.
gi 488255619 280 ENVFFEMLERI 290
Cdd:COG1192  242 RALAEELLERL 252
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 44-290 4.31e-43

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: 148.08  E-value: 4.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  44 FKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLAktFEVELPRVNFYEGLKNGNLASSIVHLT--DNLDLIPG 121
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLLDDAPLEDAIVPTeiPGLDLIPA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 122 TFDLMLLPKLTRSwtFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQNYISYL 201
Cdd:COG1192   87 NIDLAGAEIELVS--RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 202 IDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEELYKQHKEdnLVFQNIIKRSNKVSTWSKNGITEHKgYDK--KVLSMY 279
Cdd:COG1192  165 EEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGD--KVLDTVIPRSVALAEAPSAGKPVFE-YDPksKGAKAY 241

                        250
                 ....*....|.
gi 488255619 280 ENVFFEMLERI 290
Cdd:COG1192  242 RALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 37-266 5.24e-39

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: 136.71  E-value: 5.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619   37 IIILNnyFKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLAKTFEVELPRVNFYEGLK-NGNLASSIVH---L 112
Cdd:pfam01656   1 IAIAG--TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKgRVNLDPILLKeksD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  113 TDNLDLIPGTFDLMLLPKLTRSWTFENesrLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTN 192
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGPRKEE---RLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488255619  193 NIQNYISYLIDLQEQFNP-GLDMIGFVPYLVDTDSATikSNLEELYKQHKEDNLVFQnIIKRSNKVSTWSKNGIT 266
Cdd:pfam01656 156 DAKRLGGVIAALVGGYALlGLKIIGVVLNKVDGDNHG--KLLKEALEELLRGLPVLG-VIPRDEAVAEAPARGLP 227
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 37-236 3.67e-26

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: 99.92  E-value: 3.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  37 IIILNNyFKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLaktfevelprvnfyeglkngnlassivhltdnl 116
Cdd:cd02042    2 VIAVAN-QKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 117 dlipgtfdlmllpkltrswtfenesrllatllaplksdYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQN 196
Cdd:cd02042   48 --------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAK 89

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488255619 197 YISYLIDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEEL 236
Cdd:cd02042   90 LLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEEL 129
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 45-292 2.94e-07

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 51.13  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  45 KGGVGKSKLSTMFAYLTDKLNLKVLMID-KDLQATLT------KDLAKTFEVELprVNFYEGLKNGnlASSIVHLT--DN 115
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASmyhgwvPDLHIHAEDTL--LPFYLGEKDD--ATYAIKPTcwPG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 116 LDLIPGTFDLM-----LLPKLTRSWTFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEees 190
Cdd:PRK13705 191 LDIIPSCLALHrieteLMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE--- 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 191 tnnIQNYISYL--IDLQEQFNPGLDMIGFVP---YLVDTDSATIKSNLEELYKQHKE--DNLVFQNIIKRSNKVS----- 258
Cdd:PRK13705 268 ---LFDYTSALqfFDMLRDLLKNVDLKGFEPdvrILLTKYSNSNGSQSPWMEEQIRDawGSMVLKNVVRETDEVGkgqir 344

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488255619 259 --TWSKNGITEHK--GYDKKVLSMYENVFFEMLERIIQ 292
Cdd:PRK13705 345 mrTVFEQAIDQRSstGAWRNALSIWEPVCNEIFDRLIK 382
ParA_partition NF041546
ParA family partition ATPase;
37-185 2.35e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 47.16  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  37 IIILNNyfKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTK-----DLAKTFEVE-LPRvnfyeglkngnlassiv 110
Cdd:NF041546   2 IAVLNQ--KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDwaaarEDERPFPVVgLAR----------------- 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488255619 111 hltdnldlipgtfdlmllpkltrsWTfenesrlLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQ 185
Cdd:NF041546  63 ------------------------PT-------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 45-195 1.79e-04

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: 41.65  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619   45 KGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLtkdLAKTFEVElprvNFYEGLKNgnlasSIVHLTDNLDLIPGTfD 124
Cdd:TIGR01007  26 KPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSV---MSGTFKSQ----NKITGLTN-----FLSGTTDLSDAICDT-N 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488255619  125 LMLLPKLTRSWTFENESRLLA-----TLLAPLKSDYDLIIIDTVPTpSVYTNNAIVAS--DYVMIPLQAEEESTNNIQ 195
Cdd:TIGR01007  93 IENLDVITAGPVPPNPTELLQssnfkTLIETLRKRFDYIIIDTPPI-GTVTDAAIIARacDASILVTDAGKIKKREVK 169
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 44-290 4.31e-43

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: 148.08  E-value: 4.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  44 FKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLAktFEVELPRVNFYEGLKNGNLASSIVHLT--DNLDLIPG 121
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLLDDAPLEDAIVPTeiPGLDLIPA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 122 TFDLMLLPKLTRSwtFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQNYISYL 201
Cdd:COG1192   87 NIDLAGAEIELVS--RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 202 IDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEELYKQHKEdnLVFQNIIKRSNKVSTWSKNGITEHKgYDK--KVLSMY 279
Cdd:COG1192  165 EEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGD--KVLDTVIPRSVALAEAPSAGKPVFE-YDPksKGAKAY 241

                        250
                 ....*....|.
gi 488255619 280 ENVFFEMLERI 290
Cdd:COG1192  242 RALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 37-266 5.24e-39

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: 136.71  E-value: 5.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619   37 IIILNnyFKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLAKTFEVELPRVNFYEGLK-NGNLASSIVH---L 112
Cdd:pfam01656   1 IAIAG--TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKgRVNLDPILLKeksD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  113 TDNLDLIPGTFDLMLLPKLTRSWTFENesrLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTN 192
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGPRKEE---RLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488255619  193 NIQNYISYLIDLQEQFNP-GLDMIGFVPYLVDTDSATikSNLEELYKQHKEDNLVFQnIIKRSNKVSTWSKNGIT 266
Cdd:pfam01656 156 DAKRLGGVIAALVGGYALlGLKIIGVVLNKVDGDNHG--KLLKEALEELLRGLPVLG-VIPRDEAVAEAPARGLP 227
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 37-214 9.99e-29

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: 108.44  E-value: 9.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619   37 IIILNNyfKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDL-AKTFEVELprvNFYEGL-KNGNLASSIVHL-T 113
Cdd:pfam13614   4 IAIANQ--KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLgIDKNNVEK---TIYELLiGECNIEEAIIKTvI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  114 DNLDLIPGTFDLMLLPKLTRswTFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNN 193
Cdd:pfam13614  79 ENLDLIPSNIDLAGAEIELI--GIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEG 156

                         170       180
                  ....*....|....*....|.
gi 488255619  194 IQNYISYLIDLQEQFNPGLDM 214
Cdd:pfam13614 157 LSQLLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 37-236 3.67e-26

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: 99.92  E-value: 3.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  37 IIILNNyFKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTKDLaktfevelprvnfyeglkngnlassivhltdnl 116
Cdd:cd02042    2 VIAVAN-QKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 117 dlipgtfdlmllpkltrswtfenesrllatllaplksdYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQN 196
Cdd:cd02042   48 --------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAK 89

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488255619 197 YISYLIDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEEL 236
Cdd:cd02042   90 LLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEEL 129
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 45-218 4.42e-09

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: 56.66  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  45 KGGVGKSKLSTMFAY-LTDKLNLKVLMIDKDLQATltkDLAKTFEVElPRVNFYEGLKNGN------LASSIVHLTDNLD 117
Cdd:COG4963  111 KGGVGATTLAVNLAWaLARESGRRVLLVDLDLQFG---DVALYLDLE-PRRGLADALRNPDrldetlLDRALTRHSSGLS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 118 LIPGTFDLMLLPKLTRSWtfenesrlLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAeeeSTNNIQNY 197
Cdd:COG4963  187 VLAAPADLERAEEVSPEA--------VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP---DLPSLRNA 255

                        170       180
                 ....*....|....*....|.
gi 488255619 198 ISyLIDLQEQFNPGLDMIGFV 218
Cdd:COG4963  256 KR-LLDLLRELGLPDDKVRLV 275
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 45-164 2.30e-08

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: 54.04  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  45 KGGVGKSKLSTMFAYLTDKLNLKVLMIDkdlqATLTK-DLAKTFEVElPRVNFYEGLKNGNLASSIVHLT--DNLDLIPG 121
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLID----ADLRGpSLHRMLGLE-NRPGLSDVLAGEASLEDVIQPTevEGLDVLPA 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488255619 122 TFDLmllpkltrswtfENESRLLAT-----LLAPLKSDYDLIIIDTVP 164
Cdd:COG0489  176 GPLP------------PNPSELLASkrlkqLLEELRGRYDYVIIDTPP 211
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 45-292 2.94e-07

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 51.13  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  45 KGGVGKSKLSTMFAYLTDKLNLKVLMID-KDLQATLT------KDLAKTFEVELprVNFYEGLKNGnlASSIVHLT--DN 115
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASmyhgwvPDLHIHAEDTL--LPFYLGEKDD--ATYAIKPTcwPG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 116 LDLIPGTFDLM-----LLPKLTRSWTFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEees 190
Cdd:PRK13705 191 LDIIPSCLALHrieteLMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE--- 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 191 tnnIQNYISYL--IDLQEQFNPGLDMIGFVP---YLVDTDSATIKSNLEELYKQHKE--DNLVFQNIIKRSNKVS----- 258
Cdd:PRK13705 268 ---LFDYTSALqfFDMLRDLLKNVDLKGFEPdvrILLTKYSNSNGSQSPWMEEQIRDawGSMVLKNVVRETDEVGkgqir 344

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488255619 259 --TWSKNGITEHK--GYDKKVLSMYENVFFEMLERIIQ 292
Cdd:PRK13705 345 mrTVFEQAIDQRSstGAWRNALSIWEPVCNEIFDRLIK 382
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 53-190 4.62e-07

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: 49.89  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  53 LSTMFAyltdKLNLKVLMIDKDLQATltkDLAKTFEVElPRVNFYEGLK-NGNLASSIVHLTDNLDLIPGTFDLMLLPKL 131
Cdd:COG0455    6 LAAALA----RLGKRVLLVDADLGLA---NLDVLLGLE-PKATLADVLAgEADLEDAIVQGPGGLDVLPGGSGPAELAEL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488255619 132 TrswtfenESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEES 190
Cdd:COG0455   78 D-------PEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTS 129
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 45-182 6.90e-07

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: 49.10  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  45 KGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLqatltkDLAkTFEVEL---PRVNFYEGLK-NGNLASSIVHLTDNLDLIP 120
Cdd:cd02038    9 KGGVGKTNVSANLALALSKLGKRVLLLDADL------GLA-NLDILLglaPKKTLGDVLKgRVSLEDIIVEGPEGLDIIP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488255619 121 ---GTFDLMLLPKLTRSwtfenesrLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMI 182
Cdd:cd02038   82 ggsGMEELANLDPEQKA--------KLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
ParA_partition NF041546
ParA family partition ATPase;
37-185 2.35e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 47.16  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  37 IIILNNyfKGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLTK-----DLAKTFEVE-LPRvnfyeglkngnlassiv 110
Cdd:NF041546   2 IAVLNQ--KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDwaaarEDERPFPVVgLAR----------------- 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488255619 111 hltdnldlipgtfdlmllpkltrsWTfenesrlLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQ 185
Cdd:NF041546  63 ------------------------PT-------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 31-292 3.99e-06

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 47.70  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  31 NNKNEAIIILNNYfKGGVGKSKLSTMFAYLTDKLNLKVLMID-KDLQATLT------KDL-AKTFEVELPrvnFYEGLKN 102
Cdd:PHA02519 102 DDKNPVVLAVMSH-KGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASmyhgyvPDLhIHADDTLLP---FYLGERD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 103 GNLASSIVHLTDNLDLIPGTFDLMLLPklTRSWTFENESRL-------LATLLAPLKSDYDLIIIDTVPTPSVYTNNAIV 175
Cdd:PHA02519 178 NAEYAIKPTCWPGLDIIPSCLALHRIE--TDLMQYHDAGKLphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVC 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 176 ASDYVMIPLQAEEESTNNIQNYISYLIDLQEqfnpGLDMIGFVP--YLVDTDSATIKSNLEELYKQHKED---NLVFQNI 250
Cdd:PHA02519 256 AADVIVVATPAELFDYVSVLQFFTMLLDLLA----TVDLGGFEPvvRLLLTKYSLTVGNQSRWMEEQIRNtwgSMVLRQV 331

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488255619 251 IKRSNKVSTWS--KNGITEHKGYDKKVL-------SMYENVFFEMLERIIQ 292
Cdd:PHA02519 332 VRVTDEVGKGQikMRTVFEQAANQRSTLnawrnavAIWEPVCAEIFNDLIK 382
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 37-272 2.96e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 45.05  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  37 IIILNNyFKGGVGKSKLStmfAYLTDKLNL---KVLMIDKDLQATLTKDLAKTFEVELpRVN--FYEGLKNGNLA---SS 108
Cdd:PRK13869 123 VIAVTN-FKGGSGKTTTS---AHLAQYLALqgyRVLAVDLDPQASLSALLGVLPETDV-GANetLYAAIRYDDTRrplRD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 109 IVHLT--DNLDLIPGTFDLMLLPKLTRSWTFENESR------LLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYV 180
Cdd:PRK13869 198 VIRPTyfDGLHLVPGNLELMEFEHTTPKALSDKGTRdglfftRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 181 MIPLQAEEESTNNIQNYISYLIDLQEQF-NPGLDM-IGFVPYLV------DTDSATIKSNLEELYKQHkednlVFQNIIK 252
Cdd:PRK13869 278 VITVHPQMLDIASMSQFLLMTRDLLGVVkEAGGNLqYDFIRYLLtryepqDAPQTKVAALLRNMFEDH-----VLTNPMV 352

                        250       260
                 ....*....|....*....|
gi 488255619 253 RSNKVstwSKNGITEHKGYD 272
Cdd:PRK13869 353 KSAAV---SDAGLTKQTLYE 369
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 47-218 5.04e-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: 43.33  E-value: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619  47 GVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATltkDLAKTFEVElPRVNFYEGLKNGNLASSIVHLTD--NLDLIP-GTF 123
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRP---SLHRLLGLP-NEPGLSEVLSGQASLEDVIQSTNipNLDVLPaGTV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619 124 DLMLLPKLtrswtfenESRLLATLLAPLKSDYDLIIIDTVPTpSVYTNNAIVAS--DYVMIPLQAEEESTNNIQNYISYL 201
Cdd:cd05387  106 PPNPSELL--------SSPRFAELLEELKEQYDYVIIDTPPV-LAVADALILAPlvDGVLLVVRAGKTRRREVKEALERL 176

                        170
                 ....*....|....*..
gi 488255619 202 idlqeqFNPGLDMIGFV 218
Cdd:cd05387  177 ------EQAGAKVLGVV 187
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 45-195 1.79e-04

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: 41.65  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488255619   45 KGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATLtkdLAKTFEVElprvNFYEGLKNgnlasSIVHLTDNLDLIPGTfD 124
Cdd:TIGR01007  26 KPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSV---MSGTFKSQ----NKITGLTN-----FLSGTTDLSDAICDT-N 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488255619  125 LMLLPKLTRSWTFENESRLLA-----TLLAPLKSDYDLIIIDTVPTpSVYTNNAIVAS--DYVMIPLQAEEESTNNIQ 195
Cdd:TIGR01007  93 IENLDVITAGPVPPNPTELLQssnfkTLIETLRKRFDYIIIDTPPI-GTVTDAAIIARacDASILVTDAGKIKKREVK 169
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 45-119 2.24e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 38.61  E-value: 2.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488255619  45 KGGVGKSKLSTMFA-YLTDKlNLKVLMIDKDLQAtltkDLAKTFEVELPrvnfyeglkngnlASSIVHLTDNLDLI 119
Cdd:COG3640    8 KGGVGKTTLSALLArYLAEK-GKPVLAVDADPNA----NLAEALGLEVE-------------ADLIKPLGEMRELI 65
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 45-101 3.52e-03

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 38.06  E-value: 3.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488255619  45 KGGVGKSKLSTMFAYLTDKLNLKVLMIDKDLQATltkdLAKTFEVELPRVNFYEGLK 101
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSN----LAETLGVEVEKLPLIKTIG 60
 
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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