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Conserved domains on  [gi|515722284|ref|WP_017154884|]
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MULTISPECIES: ParA family partition ATPase [Pseudomonadota]

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;
3-203 1.14e-108

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 309.87  E-value: 1.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVREDQ-PLTVVGIDRPTIDRDVKAIGR-RDFVV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDErPFPVVGLARPTLHRELPSLARdYDFVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  81 IDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGrLQAAFVVSRAIKGTRIGGEVAEALAGYE 160
Cdd:NF041546  81 IDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPG-LKAAFVLNRAIARTALGREVAEALAEYG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515722284 161 LPILESRITQRVSYPGTAAAGTTVLESEPEGDAAREVQALAAE 203
Cdd:NF041546 160 LPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
3-203 1.14e-108

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 309.87  E-value: 1.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVREDQ-PLTVVGIDRPTIDRDVKAIGR-RDFVV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDErPFPVVGLARPTLHRELPSLARdYDFVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  81 IDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGrLQAAFVVSRAIKGTRIGGEVAEALAGYE 160
Cdd:NF041546  81 IDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPG-LKAAFVLNRAIARTALGREVAEALAEYG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515722284 161 LPILESRITQRVSYPGTAAAGTTVLESEPEGDAAREVQALAAE 203
Cdd:NF041546 160 LPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 2-205 2.12e-70

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 213.17  E-value: 2.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVRE-DQPLTVVGIDRPTIDRDVKAIGRR-DFV 79
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREeGEPLIPVVRMGKSIRADLPKVASGyDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  80 VIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGRLQAAFVVSRAIKGTRIGGEVAEALAGY 159
Cdd:PHA02518  81 VVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALAGY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515722284 160 ELPILESRITQRVSYPGTAAAGTTVLESEPEGDAAREVQALAAEIK 205
Cdd:PHA02518 161 GLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLVKELF 206
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-157 6.00e-43

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: 140.75  E-value: 6.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAvredqpltvvgidrptidrdvkaigrrDFVVI 81
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWLY---------------------------DYILI 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515722284  82 DGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGRLQ-AAFVVSRAIKGTRIGGEVAEALA 157
Cdd:cd02042   54 DTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLiLGILLTRVDPRTKLAREVLEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-208 9.12e-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: 144.23  E-value: 9.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVR-EDQPLTVVG--IDRPTIDRDVK------ 71
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDpDDLDPTLYDllLDDAPLEDAIVpteipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  72 -------------------AIGRR--------------DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADL 118
Cdd:COG1192   81 ldlipanidlagaeielvsRPGRElrlkralapladdyDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284 119 VELVKQRIEVTDGRLQ-AAFVVSRAIKGTRIGGEVAEALAG-YELPILESRITQRVSYPGTAAAGTTVLESEPEGDAARE 196
Cdd:COG1192  161 LETIEEVREDLNPKLEiLGILLTMVDPRTRLSREVLEELREeFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|..
gi 515722284 197 VQALAAEIKSKL 208
Cdd:COG1192  241 YRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-164 9.49e-23

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: 91.64  E-value: 9.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    4 IAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQG--SARDWAAVREDQPL-TVVGIDRPTIDRD----------- 69
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnnSSVEGLEGDIAPALqALAEGLKGRVNLDpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   70 ------------------------------VKAIGRR-DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADL 118
Cdd:pfam01656  81 gldlipgnidlekfekellgprkeerlreaLEALKEDyDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 515722284  119 VELVKQ-RIEVTDGRLQAAFVVSRAIKGTRIGGEVAEALA--GYELPIL 164
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKIIGVVLNKVDGDNHGKLLKEALEelLRGLPVL 209
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 1-125 2.75e-14

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 70.39  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGS----------------ARDWAAVR-EDQPLTVVGIDR 63
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASlsalfgyqpefdvgenETLYGAIRyDDERRPISEIIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   64 PT----ID------------RDV-KAIGRR----------------------DFVVIDGAPQAADLAVSAIKAADFVLIP 104
Cdd:TIGR03453 184 KTyfpgLDlvpgnlelmefeHETpRALSRGqggdtiffarvgealaeveddyDVVVIDCPPQLGFLTLSALCAATGVLIT 263

                         170       180
                  ....*....|....*....|....*...
gi 515722284  105 VQPSPYDIWA-------TADLVELVKQR 125
Cdd:TIGR03453 264 VHPQMLDVMSmsqfllmTGDLLGVVREA 291
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 12-94 3.92e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    12 GSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVREDQPLTVVGIDRPTIDRDVKAIGRR---DFVVIDGAPQAA 88
Cdd:smart00382  12 GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKlkpDVLILDEITSLL 91


                   ....*.
gi 515722284    89 DLAVSA 94
Cdd:smart00382  92 DAEQEA 97
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
3-203 1.14e-108

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 309.87  E-value: 1.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVREDQ-PLTVVGIDRPTIDRDVKAIGR-RDFVV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDErPFPVVGLARPTLHRELPSLARdYDFVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  81 IDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGrLQAAFVVSRAIKGTRIGGEVAEALAGYE 160
Cdd:NF041546  81 IDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPG-LKAAFVLNRAIARTALGREVAEALAEYG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515722284 161 LPILESRITQRVSYPGTAAAGTTVLESEPEGDAAREVQALAAE 203
Cdd:NF041546 160 LPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 2-205 2.12e-70

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 213.17  E-value: 2.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVRE-DQPLTVVGIDRPTIDRDVKAIGRR-DFV 79
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREeGEPLIPVVRMGKSIRADLPKVASGyDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  80 VIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGRLQAAFVVSRAIKGTRIGGEVAEALAGY 159
Cdd:PHA02518  81 VVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALAGY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515722284 160 ELPILESRITQRVSYPGTAAAGTTVLESEPEGDAAREVQALAAEIK 205
Cdd:PHA02518 161 GLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLVKELF 206
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-157 6.00e-43

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: 140.75  E-value: 6.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAvredqpltvvgidrptidrdvkaigrrDFVVI 81
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWLY---------------------------DYILI 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515722284  82 DGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGRLQ-AAFVVSRAIKGTRIGGEVAEALA 157
Cdd:cd02042   54 DTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLiLGILLTRVDPRTKLAREVLEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-208 9.12e-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: 144.23  E-value: 9.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVR-EDQPLTVVG--IDRPTIDRDVK------ 71
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDpDDLDPTLYDllLDDAPLEDAIVpteipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  72 -------------------AIGRR--------------DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADL 118
Cdd:COG1192   81 ldlipanidlagaeielvsRPGRElrlkralapladdyDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284 119 VELVKQRIEVTDGRLQ-AAFVVSRAIKGTRIGGEVAEALAG-YELPILESRITQRVSYPGTAAAGTTVLESEPEGDAARE 196
Cdd:COG1192  161 LETIEEVREDLNPKLEiLGILLTMVDPRTRLSREVLEELREeFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|..
gi 515722284 197 VQALAAEIKSKL 208
Cdd:COG1192  241 YRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-164 9.49e-23

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: 91.64  E-value: 9.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    4 IAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQG--SARDWAAVREDQPL-TVVGIDRPTIDRD----------- 69
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnnSSVEGLEGDIAPALqALAEGLKGRVNLDpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   70 ------------------------------VKAIGRR-DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADL 118
Cdd:pfam01656  81 gldlipgnidlekfekellgprkeerlreaLEALKEDyDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 515722284  119 VELVKQ-RIEVTDGRLQAAFVVSRAIKGTRIGGEVAEALA--GYELPIL 164
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKIIGVVLNKVDGDNHGKLLKEALEelLRGLPVL 209
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-126 1.83e-20

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: 84.17  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSA--------RDWA-----AVREDQPLT--VVGIDRPT 65
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAtsglgidkNNVEktiyeLLIGECNIEeaIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   66 ID-------------RDVKAIGRR--------------DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADL 118
Cdd:pfam13614  81 LDlipsnidlagaeiELIGIENREnilkealepvkdnyDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|.
gi 515722284  119 ---VELVKQRI 126
Cdd:pfam13614 161 lntIKLVKKRL 171
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 1-125 2.75e-14

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 70.39  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGS----------------ARDWAAVR-EDQPLTVVGIDR 63
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASlsalfgyqpefdvgenETLYGAIRyDDERRPISEIIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   64 PT----ID------------RDV-KAIGRR----------------------DFVVIDGAPQAADLAVSAIKAADFVLIP 104
Cdd:TIGR03453 184 KTyfpgLDlvpgnlelmefeHETpRALSRGqggdtiffarvgealaeveddyDVVVIDCPPQLGFLTLSALCAATGVLIT 263

                         170       180
                  ....*....|....*....|....*...
gi 515722284  105 VQPSPYDIWA-------TADLVELVKQR 125
Cdd:TIGR03453 264 VHPQMLDVMSmsqfllmTGDLLGVVREA 291
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-208 3.24e-14

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


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 68.91  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSAR---------------------DWAAV--------- 50
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRlhfgmdwsvrdgwarallngaDWAAAayrspdgvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   51 -------REDQPLTVVGIDRPTIDRDVKAIGR--RDFVVIDGAPQAADLAVSAIKAADFVLIPVQPspyDIWATADLVEL 121
Cdd:TIGR03371  81 flpygdlSADEREAYQAHDAGWLARLLQQLDLaaRDWVLIDLPRGPSPITRQALAAADLVLVVVNA---DAACYATLHQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  122 VKQRIEVTDGRLQAAFVVSRAIKGTRIGGEVaEALAGYELP--ILESRITQRVSYPGTAAAGTTVLESEPEGDAAREVQA 199
Cdd:TIGR03371 158 ALALFAGSGPRDGPRFLINQFDPARQLSRDV-RAVLRQTLGsrLLPFVIHRDEAVSEALARGTPVLNYAPHSQAAHDIRT 236


                  ....*....
gi 515722284  200 LAAEIKSKL 208
Cdd:TIGR03371 237 LAGWLLSKL 245
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-204 4.13e-13

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 67.06  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARAL-QLAGADVLLVDSDPQG----------SARDWA-AVREDQPLTVVGIDR------ 63
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFgdvalyldlePRRGLAdALRNPDRLDETLLDRaltrhs 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  64 ---------PTIDR----DVKAIGR--------RDFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELV 122
Cdd:COG4963  183 sglsvlaapADLERaeevSPEAVERlldllrrhFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLL 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284 123 KqRIEVTDGRLQaaFVVSRAIKGTRIGGEVAEALAGYELPILESRITQRVsypGTAA-AGTTVLESEPEGDAAREVQALA 201
Cdd:COG4963  263 R-ELGLPDDKVR--LVLNRVPKRGEISAKDIEEALGLPVAAVLPNDPKAV---AEAAnQGRPLAEVAPKSPLAKAIRKLA 336


                 ...
gi 515722284 202 AEI 204
Cdd:COG4963  337 ARL 339
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 1-138 1.36e-11

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 62.77  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARD----------------WAAVRED---QPLTVV-- 59
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSAllgvlpetdvganetlYAAIRYDdtrRPLRDVir 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  60 -----GID-----------RPTIDRDVKAIGRR-------------------DFVVIDGAPQAADLAVSAIKAADFVLIP 104
Cdd:PRK13869 201 ptyfdGLHlvpgnlelmefEHTTPKALSDKGTRdglfftrvaqafdevaddyDVVVIDCPPQLGFLTLSGLCAATSMVIT 280

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 515722284 105 VQPSPYDIWA-------TADLVELVKQrievTDGRLQAAFV 138
Cdd:PRK13869 281 VHPQMLDIASmsqfllmTRDLLGVVKE----AGGNLQYDFI 317
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-202 3.39e-10

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


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 57.67  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARAL-QLAGADVLLVDSD-PQGSARDWAAVREDQ-PLTVVG----IDRPTIDRDVKAIG 74
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELaQRAKDKVLLIDLDlPFGDLGLYLNLRPDYdLADVIQnldrLDRTLLDSAVTRHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  75 RR--------------------------------DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELV 122
Cdd:cd03111   81 SGlsllpapqeledlealgaeqvdkllqvlrafyDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLLDSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284 123 KqRIEVTDGRLQaaFVVSRAIKGTRI---------GGEVAEALAGYELPILESritqrvsypgtAAAGTTVLESEPEGDA 193
Cdd:cd03111  161 R-ELEGSSDRLR--LVLNRYDKKSEIspkdieealGLEVFATLPNDYKAVSES-----------ANTGRPLVEVAPRSAL 226


                 ....*....
gi 515722284 194 AREVQALAA 202
Cdd:cd03111  227 VRALQDLAA 235
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-112 1.24e-06

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: 45.50  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDpqgsardwaavredqpltvvgidrptidrdvkaigrrDFVVI 81
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD-------------------------------------DYVLI 43

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515722284  82 DGAPQAADLA-------VSAIKAADFVLIPVQPSPYDI 112
Cdd:cd01983   44 DGGGGLETGLllgtivaLLALKKADEVIVVVDPELGSL 81
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 17-204 1.30e-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: 47.19  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  17 TIATHLARALQLAGADVLLVDSDPQGS-----------------ARDWAAVRE-----DQPLTVV-GIDRPT-------- 65
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLAnldvllglepkatladvLAGEADLEDaivqgPGGLDVLpGGSGPAelaeldpe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284  66 --IDRDVKAIGRR-DFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIWATADLVELVKQRIEVTDGRLqaafVVSRA 142
Cdd:COG0455   81 erLIRVLEELERFyDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRRAGV----VVNRV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515722284 143 iKGTRIGGEVAEALAGYELPILESRITQRVSYP------GTAAAGTTVLESEPEGDAAREVQALAAEI 204
Cdd:COG0455  157 -RSEAEARDVFERLEQVAERFLGVRLRVLGVIPedpavrEAVRRGRPLVLAAPDSPAARAIRELAARL 223
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-39 1.42e-06

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: 47.11  E-value: 1.42e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-39 1.78e-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: 47.06  E-value: 1.78e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 515722284    2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-117 2.24e-06

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: 47.06  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQ--------GSARDWAAVRE-------------DQPLTVVG- 60
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRqrtfhryfENRSATADRTGlslptpehlnlpdNDVAEVPDg 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515722284   61 --IDRPTIDRDVKAIGRR-DFVVIDGAPQAADLAVSAIKAADFVLIPVQPS--PYDIWATAD 117
Cdd:pfam09140  82 enIDDARLEEAFADLEARcDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSfvDFDLLGQVD 143
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-40 2.43e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 46.70  E-value: 2.43e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 515722284   1 MKvIAVlNQKGGSGKTTIATHLARALQLAGADVLLVDSDP 40
Cdd:COG3640    1 MK-IAV-AGKGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-39 4.19e-06

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: 46.02  E-value: 4.19e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 3-44 6.08e-06

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 46.12  E-value: 6.08e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVD-SDPQGSA 44
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTA 150
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-204 2.21e-05

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


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 43.95  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQ----------------------GSARDWAAVREDQ----- 54
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITmanlelilgmedkpvtlhdvlaGEADIKDAIYEGPfgvkv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   55 ---PLTVVGIDRPTIDR--DVKA--IGRRDFVVIDgAPQAADL-AVSAIKAADFVLIPVQPSPYDIwATADLVELVKQRI 126
Cdd:TIGR01969  81 ipaGVSLEGLRKADPDKleDVLKeiIDDTDFLLID-APAGLERdAVTALAAADELLLVVNPEISSI-TDALKTKIVAEKL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515722284  127 evtdGRLQAAFVVSRAIK-GTRIGGEVAEALagYELPILeSRITQRVSYPGTAAAGTTVLESEPEGDAAREVQALAAEI 204
Cdd:TIGR01969 159 ----GTAILGVVLNRVTRdKTELGREEIETI--LEVPVL-GVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELAAEL 230
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 3-44 2.32e-05

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 44.23  E-value: 2.32e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVD-SDPQGSA 44
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTA 150
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-39 2.53e-05

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: 44.02  E-value: 2.53e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDAD 130
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 1-40 5.59e-05

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 42.75  E-value: 5.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 515722284    1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDP 40
Cdd:pfam06564   1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSP 40
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-40 6.72e-05

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: 42.30  E-value: 6.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 515722284   1 MKvIAVLNqKGGSGKTTIATHLARALQLAGADVLLVDSDP 40
Cdd:cd02034    1 MK-IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
3-39 1.06e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 42.34  E-value: 1.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 515722284   3 VIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-39 1.52e-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: 41.27  E-value: 1.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 515722284    1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:TIGR01007  17 IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD 55
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 12-39 4.24e-04

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 39.71  E-value: 4.24e-04
                         10        20
                 ....*....|....*....|....*...
gi 515722284  12 GSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:COG4088   14 GSGKTTFAKALAQRLYAEGIAVALLHSD 41
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 2-42 5.50e-04

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 39.66  E-value: 5.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 515722284   2 KVIAVLNqKGGSGKTTIATHLARALQLAGADVLLVDSDPQG 42
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKH 40
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-39 5.54e-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: 5.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-39 6.82e-04

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: 39.09  E-value: 6.82e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 515722284   1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:cd05387   19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD 57
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 10-46 1.30e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 38.64  E-value: 1.30e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 515722284  10 KGGSGKTTIATHLARALQLAGADVLLVDSDPQGSARD 46
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSD 44
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 1-46 1.38e-03

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 38.87  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 515722284    1 MKVIAVlNQKGGSGKTTIAThlARALQLA--GADVLLVDSDPQGSARD 46
Cdd:pfam02374   1 MRWIFF-GGKGGVGKTTVSA--ATAVQLSelGKKVLLISTDPAHSLSD 45
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-39 1.71e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 38.14  E-value: 1.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 515722284   4 IAVLNQKGGSGKTTIATHLARALqlagADVLLVDSD 39
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCD 33
PRK10037 PRK10037
cellulose biosynthesis protein BcsQ;
1-45 1.87e-03

cellulose biosynthesis protein BcsQ;


Pssm-ID: 182204  Cd Length: 250  Bit Score: 38.32  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 515722284   1 MKVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSDPQGSAR 45
Cdd:PRK10037   1 MAILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACPDNLLR 45
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-40 3.01e-03

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 38.15  E-value: 3.01e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 515722284   10 KGGSGKTTIATHLARALQLAGADVLLVDSDP 40
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP 359
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-39 3.18e-03

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 37.34  E-value: 3.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515722284   2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 12-94 3.92e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284    12 GSGKTTIATHLARALQLAGADVLLVDSDPQGSARDWAAVREDQPLTVVGIDRPTIDRDVKAIGRR---DFVVIDGAPQAA 88
Cdd:smart00382  12 GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKlkpDVLILDEITSLL 91


                   ....*.
gi 515722284    89 DLAVSA 94
Cdd:smart00382  92 DAEQEA 97
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-39 3.97e-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: 3.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 515722284    2 KVIAVLNQKGGSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 6-40 4.23e-03

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 36.55  E-value: 4.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515722284   6 VLNQKGGSGKTTIATHLARALQLAGADVLLVDSDP 40
Cdd:cd05386    5 VLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP 39
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 12-39 5.19e-03

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


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 36.61  E-value: 5.19e-03
                         10        20
                 ....*....|....*....|....*...
gi 515722284  12 GSGKTTIATHLARALQLAGADVLLVDSD 39
Cdd:COG0529   26 GSGKSTLANALERRLFERGRHVYLLDGD 53
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-40 7.75e-03

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 36.60  E-value: 7.75e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 515722284   10 KGGSGKTTIATHLARALQLAGADVLLVDSDP 40
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDP 41
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 76-123 8.62e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 36.21  E-value: 8.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515722284  76 RDFVVIDGAPQAADLAVSAIKAADFVLIPVQPSPYDIwatADL---VELVK 123
Cdd:cd03110  160 CDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGL---HDLkraIELAK 207
AAA_22 pfam13401
AAA domain;
12-84 9.23e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.01  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722284   12 GSGKTTIATHLARALQLAGADVLLVDSDPQGSARD-WAAVREDqpLTVVGIDRPTID-------RDVKAIGRRDFVVIDG 83
Cdd:pfam13401  15 GTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDlLRALLRA--LGLPLSGRLSKEellaalqQLLLALAVAVVLIIDE 92


                  .
gi 515722284   84 A 84
Cdd:pfam13401  93 A 93
 
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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