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Conserved domains on  [gi|488233197|ref|WP_002304405|]
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MULTISPECIES: ParA family protein [Bacillota]

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

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 ...
 37-290 1.01e-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: 149.62  E-value: 1.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLAKTfKVELPRvNFYEGLKNGNLASSIVHLT--D 114
Cdd:COG1192    4 IAVAN--QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLD-PDDLDP-TLYDLLLDDAPLEDAIVPTeiP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 115 NLDLIPGTFDLMLLPKLTRSwtFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNI 194
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVS--RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 195 QNYISYLIDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEELYKQHKEdnLVFQNIIKRSNKVSTWSKNGITEHKgYDK- 273
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGD--KVLDTVIPRSVALAEAPSAGKPVFE-YDPk 234

                        250
                 ....*....|....*...
gi 488233197 274 -KVLSMYENVFFEMLERI 290
Cdd:COG1192  235 sKGAKAYRALAEELLERL 252
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 37-290 1.01e-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: 149.62  E-value: 1.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLAKTfKVELPRvNFYEGLKNGNLASSIVHLT--D 114
Cdd:COG1192    4 IAVAN--QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLD-PDDLDP-TLYDLLLDDAPLEDAIVPTeiP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 115 NLDLIPGTFDLMLLPKLTRSwtFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNI 194
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVS--RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 195 QNYISYLIDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEELYKQHKEdnLVFQNIIKRSNKVSTWSKNGITEHKgYDK- 273
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGD--KVLDTVIPRSVALAEAPSAGKPVFE-YDPk 234

                        250
                 ....*....|....*...
gi 488233197 274 -KVLSMYENVFFEMLERI 290
Cdd:COG1192  235 sKGAKAYRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 37-266 1.86e-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: 137.86  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197   37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLAKTFKVELPRVNFYEGLK-NGNLASSIVH---L 112
Cdd:pfam01656   1 IAIAG--TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKgRVNLDPILLKeksD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  113 TDNLDLIPGTFDLMLLPKLTRSWTFENesrLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTN 192
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGPRKEE---RLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488233197  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 3.41e-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: 100.31  E-value: 3.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLaktfkvelprvnfyeglkngnlassivhltdnl 116
Cdd:cd02042    3 IAVAN--QKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 117 dlipgtfdlmllpkltrswtfenesrllatllaplksdYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQN 196
Cdd:cd02042   48 --------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAK 89

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488233197 197 YISYLIDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEEL 236
Cdd:cd02042   90 LLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEEL 129
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 45-292 6.05e-07

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 50.36  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  45 KGGVGKSKLSTMFAYLTDKFNLKVLMID-KDLQATltkdlAKTFKVELPRVN---------FYEGLKNGnlASSIVHLT- 113
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGT-----ASMYHGWVPDLHihaedtllpFYLGEKDD--ATYAIKPTc 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 114 -DNLDLIPGTFDLM-----LLPKLTRSWTFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAE 187
Cdd:PRK13705 188 wPGLDIIPSCLALHrieteLMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 188 eestnnIQNYISYL--IDLQEQFNPGLDMIGFVP---YLVDTDSATIKSNLEELYKQHKE--DNLVFQNIIKRSNKVS-- 258
Cdd:PRK13705 268 ------LFDYTSALqfFDMLRDLLKNVDLKGFEPdvrILLTKYSNSNGSQSPWMEEQIRDawGSMVLKNVVRETDEVGkg 341

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488233197 259 -----TWSKNGITEHK--GYDKKVLSMYENVFFEMLERIIQ 292
Cdd:PRK13705 342 qirmrTVFEQAIDQRSstGAWRNALSIWEPVCNEIFDRLIK 382
ParA_partition NF041546
ParA family partition ATPase;
37-185 5.78e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 46.01  E-value: 5.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNNyfKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTK-----DLAKTFKVE-LPRvnfyeglkngnlassiv 110
Cdd:NF041546   2 IAVLNQ--KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDwaaarEDERPFPVVgLAR----------------- 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488233197 111 hltdnldlipgtfdlmllpkltrsWTfenesrlLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQ 185
Cdd:NF041546  63 ------------------------PT-------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 29-195 2.01e-05

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: 44.74  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197   29 ILNSKNEAIVILNNYFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLtkdLAKTFKVElprvNFYEGLKNgnlasS 108
Cdd:TIGR01007  10 IQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSV---MSGTFKSQ----NKITGLTN-----F 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  109 IVHLTDNLDLIPGTfDLMLLPKLTRSWTFENESRLLA-----TLLAPLKSDYDLIIIDTVPTpSVYTNNAIVAS--DYVM 181
Cdd:TIGR01007  78 LSGTTDLSDAICDT-NIENLDVITAGPVPPNPTELLQssnfkTLIETLRKRFDYIIIDTPPI-GTVTDAAIIARacDASI 155

                         170
                  ....*....|....
gi 488233197  182 IPLQAEEESTNNIQ 195
Cdd:TIGR01007 156 LVTDAGKIKKREVK 169
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 37-290 1.01e-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: 149.62  E-value: 1.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLAKTfKVELPRvNFYEGLKNGNLASSIVHLT--D 114
Cdd:COG1192    4 IAVAN--QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLD-PDDLDP-TLYDLLLDDAPLEDAIVPTeiP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 115 NLDLIPGTFDLMLLPKLTRSwtFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNI 194
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVS--RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 195 QNYISYLIDLQEQFNPGLDMIGFVPYLVDTDSATIKSNLEELYKQHKEdnLVFQNIIKRSNKVSTWSKNGITEHKgYDK- 273
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGD--KVLDTVIPRSVALAEAPSAGKPVFE-YDPk 234

                        250
                 ....*....|....*...
gi 488233197 274 -KVLSMYENVFFEMLERI 290
Cdd:COG1192  235 sKGAKAYRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 37-266 1.86e-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: 137.86  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197   37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLAKTFKVELPRVNFYEGLK-NGNLASSIVH---L 112
Cdd:pfam01656   1 IAIAG--TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKgRVNLDPILLKeksD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  113 TDNLDLIPGTFDLMLLPKLTRSWTFENesrLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTN 192
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGPRKEE---RLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488233197  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 2.18e-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: 109.98  E-value: 2.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197   37 IVILNNyfKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDL-AKTFKVELprvNFYEGL-KNGNLASSIVHL-T 113
Cdd:pfam13614   4 IAIANQ--KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLgIDKNNVEK---TIYELLiGECNIEEAIIKTvI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  114 DNLDLIPGTFDLMLLPKLTRswTFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNN 193
Cdd:pfam13614  79 ENLDLIPSNIDLAGAEIELI--GIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEG 156

                         170       180
                  ....*....|....*....|.
gi 488233197  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 3.41e-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: 100.31  E-value: 3.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNnyFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLaktfkvelprvnfyeglkngnlassivhltdnl 116
Cdd:cd02042    3 IAVAN--QKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 117 dlipgtfdlmllpkltrswtfenesrllatllaplksdYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEESTNNIQN 196
Cdd:cd02042   48 --------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAK 89

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488233197 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 2.80e-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: 57.43  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  45 KGGVGKSKLSTMFAY-LTDKFNLKVLMIDKDLQATltkDLAKTFKVElPRVNFYEGLKNGN------LASSIVHLTDNLD 117
Cdd:COG4963  111 KGGVGATTLAVNLAWaLARESGRRVLLVDLDLQFG---DVALYLDLE-PRRGLADALRNPDrldetlLDRALTRHSSGLS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 118 LIPGTFDLMLLPKLTRSWtfenesrlLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAeeeSTNNIQNY 197
Cdd:COG4963  187 VLAAPADLERAEEVSPEA--------VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP---DLPSLRNA 255

                        170       180
                 ....*....|....*....|.
gi 488233197 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 1.34e-07

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: 51.73  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  45 KGGVGKSKLSTMFAYLTDKFNLKVLMIDkdlqATLTK-DLAKTFKVElPRVNFYEGLKNGNLASSIVHLT--DNLDLIPG 121
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLID----ADLRGpSLHRMLGLE-NRPGLSDVLAGEASLEDVIQPTevEGLDVLPA 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488233197 122 TFDLmllpkltrswtfENESRLLAT-----LLAPLKSDYDLIIIDTVP 164
Cdd:COG0489  176 GPLP------------PNPSELLASkrlkqLLEELRGRYDYVIIDTPP 211
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 45-292 6.05e-07

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 50.36  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  45 KGGVGKSKLSTMFAYLTDKFNLKVLMID-KDLQATltkdlAKTFKVELPRVN---------FYEGLKNGnlASSIVHLT- 113
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGT-----ASMYHGWVPDLHihaedtllpFYLGEKDD--ATYAIKPTc 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 114 -DNLDLIPGTFDLM-----LLPKLTRSWTFENESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAE 187
Cdd:PRK13705 188 wPGLDIIPSCLALHrieteLMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 188 eestnnIQNYISYL--IDLQEQFNPGLDMIGFVP---YLVDTDSATIKSNLEELYKQHKE--DNLVFQNIIKRSNKVS-- 258
Cdd:PRK13705 268 ------LFDYTSALqfFDMLRDLLKNVDLKGFEPdvrILLTKYSNSNGSQSPWMEEQIRDawGSMVLKNVVRETDEVGkg 341

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488233197 259 -----TWSKNGITEHK--GYDKKVLSMYENVFFEMLERIIQ 292
Cdd:PRK13705 342 qirmrTVFEQAIDQRSstGAWRNALSIWEPVCNEIFDRLIK 382
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 45-182 9.66e-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: 48.72  E-value: 9.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  45 KGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQA---------TLTKDLAKTFKvelprvnfyeglKNGNLASSIVHLTDN 115
Cdd:cd02038    9 KGGVGKTNVSANLALALSKLGKRVLLLDADLGLanldillglAPKKTLGDVLK------------GRVSLEDIIVEGPEG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 116 LDLIP---GTFDLMLLPKLTRSwtfenesrLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMI 182
Cdd:cd02038   77 LDIIPggsGMEELANLDPEQKA--------KLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 53-190 2.00e-06

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: 47.96  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  53 LSTMFAyltdKFNLKVLMIDKDLQATltkDLAKTFKVElPRVNFYEGLK-NGNLASSIVHLTDNLDLIPGTFDLMLLPKL 131
Cdd:COG0455    6 LAAALA----RLGKRVLLVDADLGLA---NLDVLLGLE-PKATLADVLAgEADLEDAIVQGPGGLDVLPGGSGPAELAEL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488233197 132 TrswtfenESRLLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQAEEES 190
Cdd:COG0455   78 D-------PEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTS 129
ParA_partition NF041546
ParA family partition ATPase;
37-185 5.78e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 46.01  E-value: 5.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  37 IVILNNyfKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTK-----DLAKTFKVE-LPRvnfyeglkngnlassiv 110
Cdd:NF041546   2 IAVLNQ--KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDwaaarEDERPFPVVgLAR----------------- 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488233197 111 hltdnldlipgtfdlmllpkltrsWTfenesrlLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPLQ 185
Cdd:NF041546  63 ------------------------PT-------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 33-292 1.40e-05

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 46.16  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  33 KNEAIVILNNYfKGGVGKSKLSTMFAYLTDKFNLKVLMID-KDLQATltkdlAKTFKVELPRVN---------FYEGLKN 102
Cdd:PHA02519 104 KNPVVLAVMSH-KGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGT-----ASMYHGYVPDLHihaddtllpFYLGERD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 103 GNLASSIVHLTDNLDLIPGTFDLMLLPklTRSWTFENESRL-------LATLLAPLKSDYDLIIIDTVPTPSVYTNNAIV 175
Cdd:PHA02519 178 NAEYAIKPTCWPGLDIIPSCLALHRIE--TDLMQYHDAGKLphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVC 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 176 ASDYVMIPLQAEEESTNNIQNYISYLIDLQEqfnpGLDMIGFVP--YLVDTDSATIKSNLEELYKQHKED---NLVFQNI 250
Cdd:PHA02519 256 AADVIVVATPAELFDYVSVLQFFTMLLDLLA----TVDLGGFEPvvRLLLTKYSLTVGNQSRWMEEQIRNtwgSMVLRQV 331

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488233197 251 IKRSNKVSTWS--KNGITEHKGYDKKVL-------SMYENVFFEMLERIIQ 292
Cdd:PHA02519 332 VRVTDEVGKGQikMRTVFEQAANQRSTLnawrnavAIWEPVCAEIFNDLIK 382
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 29-195 2.01e-05

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: 44.74  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197   29 ILNSKNEAIVILNNYFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLtkdLAKTFKVElprvNFYEGLKNgnlasS 108
Cdd:TIGR01007  10 IQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSV---MSGTFKSQ----NKITGLTN-----F 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  109 IVHLTDNLDLIPGTfDLMLLPKLTRSWTFENESRLLA-----TLLAPLKSDYDLIIIDTVPTpSVYTNNAIVAS--DYVM 181
Cdd:TIGR01007  78 LSGTTDLSDAICDT-NIENLDVITAGPVPPNPTELLQssnfkTLIETLRKRFDYIIIDTPPI-GTVTDAAIIARacDASI 155

                         170
                  ....*....|....
gi 488233197  182 IPLQAEEESTNNIQ 195
Cdd:TIGR01007 156 LVTDAGKIKKREVK 169
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 47-218 6.87e-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: 42.94  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  47 GVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATltkDLAKTFKVElPRVNFYEGLKNGNLASSIVHLTD--NLDLIP-GTF 123
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRP---SLHRLLGLP-NEPGLSEVLSGQASLEDVIQSTNipNLDVLPaGTV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 124 DLMLLPKLtrswtfenESRLLATLLAPLKSDYDLIIIDTVPTpSVYTNNAIVAS--DYVMIPLQAEEESTNNIQNYISYL 201
Cdd:cd05387  106 PPNPSELL--------SSPRFAELLEELKEQYDYVIIDTPPV-LAVADALILAPlvDGVLLVVRAGKTRRREVKEALERL 176

                        170
                 ....*....|....*..
gi 488233197 202 idlqeqFNPGLDMIGFV 218
Cdd:cd05387  177 ------EQAGAKVLGVV 187
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 38-272 2.00e-04

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 42.35  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197  38 VILNNYFKGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATLTKDLAKTFKVELpRVN--FYEGLKNGNLA---SSIVHL 112
Cdd:PRK13869 123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDV-GANetLYAAIRYDDTRrplRDVIRP 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 113 T--DNLDLIPGTFDLMLLPKLTRSWTFENESR------LLATLLAPLKSDYDLIIIDTVPTPSVYTNNAIVASDYVMIPL 184
Cdd:PRK13869 202 TyfDGLHLVPGNLELMEFEHTTPKALSDKGTRdglfftRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITV 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488233197 185 QAEEESTNNIQNYISYLIDLQEQF-NPGLDM-IGFVPYLV------DTDSATIKSNLEELYKQHkednlVFQNIIKRSNK 256
Cdd:PRK13869 282 HPQMLDIASMSQFLLMTRDLLGVVkEAGGNLqYDFIRYLLtryepqDAPQTKVAALLRNMFEDH-----VLTNPMVKSAA 356

                        250
                 ....*....|....*.
gi 488233197 257 VstwSKNGITEHKGYD 272
Cdd:PRK13869 357 V---SDAGLTKQTLYE 369
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 45-101 2.10e-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: 38.83  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488233197  45 KGGVGKSKLSTMFAYLTDKFNLKVLMIDKDLQATltkdLAKTFKVELPRVNFYEGLK 101
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSN----LAETLGVEVEKLPLIKTIG 60
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 45-119 3.72e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 38.22  E-value: 3.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488233197  45 KGGVGKSKLSTMFA-YLTDKfNLKVLMIDKDLQAtltkDLAKTFKVELPrvnfyeglkngnlASSIVHLTDNLDLI 119
Cdd:COG3640    8 KGGVGKTTLSALLArYLAEK-GKPVLAVDADPNA----NLAEALGLEVE-------------ADLIKPLGEMRELI 65
 
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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