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Conserved domains on  [gi|973109792|gb|KUK66718|]
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Chromosome partitioning protein [Parcubacteria bacterium 34_609]

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 ...
 1-257 6.52e-106

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: 307.17  E-value: 6.52e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIK 80
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLL-----LDDAPLEDAIVP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  81 LKINsenNLFLAPSNIDFASAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:COG1192   76 TEIP---GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 161 ALRGIEEFIETTEIVRKNLNHSLKI-NILITIADTRSNLAKEVIDEIKQYFSDRLFKTIIRKNITLVEASSQGTPALHYS 239
Cdd:COG1192  153 SLEGLAQLLETIEEVREDLNPKLEIlGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYD 232

                        250
                 ....*....|....*...
gi 973109792 240 PKSHGAIDYYKLAQEVIS 257
Cdd:COG1192  233 PKSKGAKAYRALAEELLE 250
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-257 6.52e-106

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: 307.17  E-value: 6.52e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIK 80
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLL-----LDDAPLEDAIVP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  81 LKINsenNLFLAPSNIDFASAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:COG1192   76 TEIP---GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 161 ALRGIEEFIETTEIVRKNLNHSLKI-NILITIADTRSNLAKEVIDEIKQYFSDRLFKTIIRKNITLVEASSQGTPALHYS 239
Cdd:COG1192  153 SLEGLAQLLETIEEVREDLNPKLEIlGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYD 232

                        250
                 ....*....|....*...
gi 973109792 240 PKSHGAIDYYKLAQEVIS 257
Cdd:COG1192  233 PKSKGAKAYRALAEELLE 250
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-185 1.39e-66

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: 204.74  E-value: 1.39e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIK 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELL-----IGECNIEEAIIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   81 LKINsenNLFLAPSNIDFASAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:pfam13614  76 TVIE---NLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYY 152

                         170       180
                  ....*....|....*....|....*
gi 973109792  161 ALRGIEEFIETTEIVRKNLNHSLKI 185
Cdd:pfam13614 153 ALEGLSQLLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-207 4.12e-45

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: 148.07  E-value: 4.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLslepdslsktilnvlephrsknklkleeviikl 81
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  82 kinsennlflapsnidfasaeyklidqigredflgasireckvpFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFA 161
Cdd:cd02042   48 --------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFD 83

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 973109792 162 LRGIEEFIETTEIVRKNLNHSLKIN-ILITIADTRSNLAKEVIDEIK 207
Cdd:cd02042   84 LDGLAKLLDTLEELKKQLNPPLLILgILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
3-254 9.55e-31

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 113.42  E-value: 9.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   3 IISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAhttlglslepdSLSKTilnvlepHRSknklkleeviiklk 82
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG-----------SALDW-------AAA-------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  83 iNSENNLFlapsnidfasaeyKLIDqIGREDfLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF-- 160
Cdd:NF041546  49 -REDERPF-------------PVVG-LARPT-LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYdl 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 161 -ALRGIEEFIETteivRKNLNHSLKINILITIADTRSNLAKEVIDEIKQYfSDRLFKTIIRKNITLVEASSQGTPALHYS 239
Cdd:NF041546 113 wASADTVDLIKE----AREYTPGLKAAFVLNRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAE 187

                        250
                 ....*....|....*
gi 973109792 240 PKSHGAIDYYKLAQE 254
Cdd:NF041546 188 PDGKAAREIRALAKE 202
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-261 5.22e-23

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: 94.41  E-value: 5.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDpQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIKl 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD-ITMANLELILGMEDKPVTLHDVL-----AGEADIKDAIYE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   82 kinSENNLFLAPSNIDFASAEYKLIDQIgrEDFlgasIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFA 161
Cdd:TIGR01969  74 ---GPFGVKVIPAGVSLEGLRKADPDKL--EDV----LKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  162 lrgIEEFIETTEIVRKnlnhsLKINILITIADTRSNLAKEV-IDEIKQYFSDRLFKTiIRKNITLVEASSQGTPALHYSP 240
Cdd:TIGR01969 145 ---ITDALKTKIVAEK-----LGTAILGVVLNRVTRDKTELgREEIETILEVPVLGV-VPEDPEVRRAAAFGEPVVIYNP 215

                         250       260
                  ....*....|....*....|.
gi 973109792  241 KSHGAIDYYKLAQEVISFEKE 261
Cdd:TIGR01969 216 NSPAAQAFMELAAELAGIEYE 236
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 1-228 9.71e-20

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 87.81  E-value: 9.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTT--LGLSLEPDSLSKTILNVLEPHRSKNKlKLEEVI 78
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSalLGVLPETDVGANETLYAAIRYDDTRR-PLRDVI 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  79 iklKINSENNLFLAPSNIDFASAEYK----LIDQIGREDF----LGASIRECKVPFDYILIDCPPSLGILTVNALKACDE 150
Cdd:PRK13869 200 ---RPTYFDGLHLVPGNLELMEFEHTtpkaLSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATS 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 151 VIIPMQPHYFALRGIEEFIETTE----IVRK---NLNHSLkINILITIADTRSNLAKEVIDEIKQYFSDRLFKTIIRKNI 223
Cdd:PRK13869 277 MVITVHPQMLDIASMSQFLLMTRdllgVVKEaggNLQYDF-IRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSA 355


                 ....*
gi 973109792 224 TLVEA 228
Cdd:PRK13869 356 AVSDA 360
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-257 6.52e-106

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: 307.17  E-value: 6.52e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIK 80
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLL-----LDDAPLEDAIVP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  81 LKINsenNLFLAPSNIDFASAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:COG1192   76 TEIP---GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 161 ALRGIEEFIETTEIVRKNLNHSLKI-NILITIADTRSNLAKEVIDEIKQYFSDRLFKTIIRKNITLVEASSQGTPALHYS 239
Cdd:COG1192  153 SLEGLAQLLETIEEVREDLNPKLEIlGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYD 232

                        250
                 ....*....|....*...
gi 973109792 240 PKSHGAIDYYKLAQEVIS 257
Cdd:COG1192  233 PKSKGAKAYRALAEELLE 250
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-185 1.39e-66

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: 204.74  E-value: 1.39e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIK 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELL-----IGECNIEEAIIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   81 LKINsenNLFLAPSNIDFASAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:pfam13614  76 TVIE---NLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYY 152

                         170       180
                  ....*....|....*....|....*
gi 973109792  161 ALRGIEEFIETTEIVRKNLNHSLKI 185
Cdd:pfam13614 153 ALEGLSQLLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-207 4.12e-45

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: 148.07  E-value: 4.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLslepdslsktilnvlephrsknklkleeviikl 81
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  82 kinsennlflapsnidfasaeyklidqigredflgasireckvpFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFA 161
Cdd:cd02042   48 --------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFD 83

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 973109792 162 LRGIEEFIETTEIVRKNLNHSLKIN-ILITIADTRSNLAKEVIDEIK 207
Cdd:cd02042   84 LDGLAKLLDTLEELKKQLNPPLLILgILLTRVDPRTKLAREVLEELK 130
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-234 7.42e-43

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: 145.57  E-value: 7.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    4 ISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTT--LGLSLEPDSLSKTILNVLEPhrsknKLKLEEVIIKL 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKG-----RVNLDPILLKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   82 KINsENNLFLAPSNIDFASAEYKLIDqIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFA 161
Cdd:pfam01656  76 KSD-EGGLDLIPGNIDLEKFEKELLG-PRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVIL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973109792  162 LRGIEEFIETTEIVRKNLNHsLKINILITIAdTR---SNLAKEVIDEIKQYFSDRLFKTIIRKNITLVEASSQGTP 234
Cdd:pfam01656 154 VEDAKRLGGVIAALVGGYAL-LGLKIIGVVL-NKvdgDNHGKLLKEALEELLRGLPVLGVIPRDEAVAEAPARGLP 227
ParA_partition NF041546
ParA family partition ATPase;
3-254 9.55e-31

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 113.42  E-value: 9.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   3 IISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAhttlglslepdSLSKTilnvlepHRSknklkleeviiklk 82
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG-----------SALDW-------AAA-------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  83 iNSENNLFlapsnidfasaeyKLIDqIGREDfLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF-- 160
Cdd:NF041546  49 -REDERPF-------------PVVG-LARPT-LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYdl 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 161 -ALRGIEEFIETteivRKNLNHSLKINILITIADTRSNLAKEVIDEIKQYfSDRLFKTIIRKNITLVEASSQGTPALHYS 239
Cdd:NF041546 113 wASADTVDLIKE----AREYTPGLKAAFVLNRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAE 187

                        250
                 ....*....|....*
gi 973109792 240 PKSHGAIDYYKLAQE 254
Cdd:NF041546 188 PDGKAAREIRALAKE 202
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 17-262 2.78e-26

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: 102.66  E-value: 2.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  17 TTTINLGASLASLGRKVLLIDLDPQA---HTTLGlsLEPDslsKTILNVLephrsKNKLKLEEVIIKlkinSENNLFLAP 93
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLanlDVLLG--LEPK---ATLADVL-----AGEADLEDAIVQ----GPGGLDVLP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  94 SNIDFASAEyklidQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFALRGIEEFIettE 173
Cdd:COG0455   67 GGSGPAELA-----ELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALL---K 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 174 IVRKNLNHSlKINILITIADTRS---NLAKEVIDEIKQYFSDRL-FKTIIRKNITLVEASSQGTPALHYSPKSHGAIDYY 249
Cdd:COG0455  139 LLRRRLGVR-RAGVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIR 217

                        250
                 ....*....|...
gi 973109792 250 KLAQEVISFEKEE 262
Cdd:COG0455  218 ELAARLAGWPVPE 230
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-255 1.51e-25

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: 100.74  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD-PQAHTTLGLSLEpDSLSKTILNVLEphrskNKLKLEEVIIK 80
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLE-NRIVYTLVDVLE-----GECRLEQALIK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  81 LKINseNNLFLAPSNIDfasaEYKliDQIGREDFLgASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:cd02036   75 DKRW--ENLYLLPASQT----RDK--DALTPEKLE-ELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEIS 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 161 ALRG---IEEFIETTEIVRKNL------NHSLKINILITIADTRSNLAKEVIdeikqyfsdrlfkTIIRKNITLVEASSQ 231
Cdd:cd02036  146 SVRDadrVIGLLESKGIVNIGLivnryrPEMVKSGDMLSVEDIQEILGIPLL-------------GVIPEDPEVIVATNR 212

                        250       260
                 ....*....|....*....|....
gi 973109792 232 GTPALHYSPKSHGAIDYYKLAQEV 255
Cdd:cd02036  213 GEPLVLYKPNSLAAKAFENIARRL 236
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-261 5.22e-23

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: 94.41  E-value: 5.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDpQAHTTLGLSLEPDSLSKTILNVLephrsKNKLKLEEVIIKl 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD-ITMANLELILGMEDKPVTLHDVL-----AGEADIKDAIYE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   82 kinSENNLFLAPSNIDFASAEYKLIDQIgrEDFlgasIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFA 161
Cdd:TIGR01969  74 ---GPFGVKVIPAGVSLEGLRKADPDKL--EDV----LKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  162 lrgIEEFIETTEIVRKnlnhsLKINILITIADTRSNLAKEV-IDEIKQYFSDRLFKTiIRKNITLVEASSQGTPALHYSP 240
Cdd:TIGR01969 145 ---ITDALKTKIVAEK-----LGTAILGVVLNRVTRDKTELgREEIETILEVPVLGV-VPEDPEVRRAAAFGEPVVIYNP 215

                         250       260
                  ....*....|....*....|.
gi 973109792  241 KSHGAIDYYKLAQEVISFEKE 261
Cdd:TIGR01969 216 NSPAAQAFMELAAELAGIEYE 236
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 3-158 8.28e-21

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: 90.42  E-value: 8.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    3 IISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTT--LGLSLEPDSLS-KTILNVL---EPHRSknklkLEE 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSalFGYQPEFDVGEnETLYGAIrydDERRP-----ISE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   77 VIIKLKInseNNLFLAPSNIDFASAEYK----LIDQIGREDF----LGASIRECKVPFDYILIDCPPSLGILTVNALKAC 148
Cdd:TIGR03453 181 IIRKTYF---PGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAA 257

                         170
                  ....*....|
gi 973109792  149 DEVIIPMQPH 158
Cdd:TIGR03453 258 TGVLITVHPQ 267
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 1-228 9.71e-20

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 87.81  E-value: 9.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTT--LGLSLEPDSLSKTILNVLEPHRSKNKlKLEEVI 78
Cdd:PRK13869 121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSalLGVLPETDVGANETLYAAIRYDDTRR-PLRDVI 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  79 iklKINSENNLFLAPSNIDFASAEYK----LIDQIGREDF----LGASIRECKVPFDYILIDCPPSLGILTVNALKACDE 150
Cdd:PRK13869 200 ---RPTYFDGLHLVPGNLELMEFEHTtpkaLSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATS 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 151 VIIPMQPHYFALRGIEEFIETTE----IVRK---NLNHSLkINILITIADTRSNLAKEVIDEIKQYFSDRLFKTIIRKNI 223
Cdd:PRK13869 277 MVITVHPQMLDIASMSQFLLMTRdllgVVKEaggNLQYDF-IRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSA 355


                 ....*
gi 973109792 224 TLVEA 228
Cdd:PRK13869 356 AVSDA 360
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-261 1.12e-19

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: 85.47  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHT-TLGLSLEpDSLSKTILNVLEphrskNKLKLEEVIIK 80
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNlDLLLGLE-NRIVYTLVDVVE-----GECRLQQALIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   81 LKinSENNLFLAPsnidfaSAEYKLIDQIGREDFLgASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:TIGR01968  76 DK--RLKNLYLLP------ASQTRDKDAVTPEQMK-KLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  161 ALRGIEEFI---ETTEIVRKNL------NHSLKINILITIADTRSNLAKEVIdeikqyfsdrlfkTIIRKNITLVEASSQ 231
Cdd:TIGR01968 147 AVRDADRVIgllEAKGIEKIHLivnrlrPEMVKKGDMLSVDDVLEILSIPLI-------------GVIPEDEAIIVSTNK 213

                         250       260       270
                  ....*....|....*....|....*....|
gi 973109792  232 GTPALhYSPKSHGAIDYYKLAQEVISFEKE 261
Cdd:TIGR01968 214 GEPVV-LNDKSRAGKAFENIARRILGEEVP 242
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-257 5.06e-19

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: 83.55  E-value: 5.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQahTTLGLSL-----EPDSLSKTILNVlEPHRsknklkle 75
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ--NLLRLHFgmdwsVRDGWARALLNG-ADWA-------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   76 eviiklkinseNNLFLAPSNIDF-----ASAEYKLIDQIGREDFLGASIRECKVPF-DYILIDCPPSLGILTVNALKACD 149
Cdd:TIGR03371  70 -----------AAAYRSPDGVLFlpygdLSADEREAYQAHDAGWLARLLQQLDLAArDWVLIDLPRGPSPITRQALAAAD 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  150 EVIIPMQP----HYFALRGIEEFietteivRKNLNHSLKINILITIADTRSNLAKEVIDEIKQYFSDRLFKTIIRKNITL 225
Cdd:TIGR03371 139 LVLVVVNAdaacYATLHQLALAL-------FAGSGPRDGPRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAV 211

                         250       260       270
                  ....*....|....*....|....*....|..
gi 973109792  226 VEASSQGTPALHYSPKSHGAIDYYKLAQEVIS 257
Cdd:TIGR03371 212 SEALARGTPVLNYAPHSQAAHDIRTLAGWLLS 243
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-255 4.78e-18

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: 82.47  E-value: 4.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLA-SLGRKVLLIDLDPQA-HTTLGLSLEPDslsKTILNVLE-PHRsknklkLEEVI 78
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFgDVALYLDLEPR---RGLADALRnPDR------LDETL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  79 IK-LKINSENNLFL--APSNIDFAsaeykliDQIGREDFlGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPM 155
Cdd:COG4963  174 LDrALTRHSSGLSVlaAPADLERA-------EEVSPEAV-ERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVT 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 156 QPHYFALRGIEEFIETteIVRKNLNHSlKINILITIADTRSNLAKEvidEIKQYFSDRLFKTIIRKNITLVEASSQGTPA 235
Cdd:COG4963  246 EPDLPSLRNAKRLLDL--LRELGLPDD-KVRLVLNRVPKRGEISAK---DIEEALGLPVAAVLPNDPKAVAEAANQGRPL 319

                        250       260
                 ....*....|....*....|
gi 973109792 236 LHYSPKShgaidyyKLAQEV 255
Cdd:COG4963  320 AEVAPKS-------PLAKAI 332
PHA02518 PHA02518
ParA-like protein; Provisional
 2-258 9.41e-18

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 79.12  E-value: 9.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTlglslepdslsktilnvlephrsknklkleeviikl 81
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  82 kinsennlflapSNIDFASAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYFA 161
Cdd:PHA02518  45 ------------DWAEAREEGEPLIPVVRMGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFD 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 162 LRGIEEFIETTEIVRKNLNHSLKINILITIADTRSNLAKEVIDEIKQYfSDRLFKTIIRKNITLVEASSQGTPALHYSPK 241
Cdd:PHA02518 113 IWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALAGY-GLPILRNGTTQRVAYADAAEAGGSVLELPED 191

                        250
                 ....*....|....*..
gi 973109792 242 SHGAIDYYKLAQEVISF 258
Cdd:PHA02518 192 DKAAEEIIQLVKELFRG 208
minD CHL00175
septum-site determining protein; Validated
 2-163 9.53e-17

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 77.89  E-value: 9.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD-PQAHTTLGLSLEpDSLSKTILNVLEphrskNKLKLEEVIIK 80
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLE-NRVLYTAMDVLE-----GECRLDQALIR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  81 LKinSENNLFLapsnidFASAEYKLIDQIGRE--DFLGASIRECKvpFDYILIDCPPSLGILTVNALKACDEVIIPMQPH 158
Cdd:CHL00175  90 DK--RWKNLSL------LAISKNRQRYNVTRKnmNMLVDSLKNRG--YDYILIDCPAGIDVGFINAIAPAQEAIVVTTPE 159


                 ....*
gi 973109792 159 YFALR 163
Cdd:CHL00175 160 ITAIR 164
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-153 2.87e-16

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: 75.68  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD---PQAHTTLGLSLEpdslsKTILNVLephrsKNKLKLEEVI 78
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglANLDILLGLAPK-----KTLGDVL-----KGRVSLEDII 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973109792  79 IKlkinSENNLFLAPSNIDFasAEYKLIDQIGREDFLGaSIRECKVPFDYILIDCPPSLGILTVNALKACDEVII 153
Cdd:cd02038   71 VE----GPEGLDIIPGGSGM--EELANLDPEQKAKLIE-ELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-153 4.72e-16

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: 75.99  E-value: 4.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD---PQAHTTLGLSLEPdslskTILNVLEphrskNKLKLEEVI 78
Cdd:COG0489   93 EVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgPSLHRMLGLENRP-----GLSDVLA-----GEASLEDVI 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973109792  79 IKLKInseNNLFLAPS-NIDFASAEYKLIDQIgrEDFLgasiRECKVPFDYILIDCPPSLG-ILTVNALKACDEVII 153
Cdd:COG0489  163 QPTEV---EGLDVLPAgPLPPNPSELLASKRL--KQLL----EELRGRYDYVIIDTPPGLGvADATLLASLVDGVLL 230
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-153 7.37e-16

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 75.09  E-value: 7.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDpqahttLGL-------SLEpDSLSKTILNVLEphrskNKLKL 74
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD------IGLrnldlvmGLE-NRIVYDLVDVIE-----GECRL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  75 EEVIIKLKinSENNLFLAPS----NIDFASAE--YKLIDQIGREdflgasireckvpFDYILIDCPPslGILT--VNALK 146
Cdd:COG2894   71 KQALIKDK--RFENLYLLPAsqtrDKDALTPEqmKKLVEELKEE-------------FDYILIDSPA--GIEQgfKNAIA 133


                 ....*..
gi 973109792 147 ACDEVII 153
Cdd:COG2894  134 GADEAIV 140
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-242 2.00e-15

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: 73.47  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASL-GRKVLLIDLDPQAHT-TLGLSLEPDslsKTILNVLE-PHRsknklkLEEVI 78
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDlGLYLNLRPD---YDLADVIQnLDR------LDRTL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  79 IK---LKINSENNLFLAPSNI-DFASAEYKLIDQIgrEDFLGASireckvpFDYILIDCPPSLGILTVNALKACDEVIIP 154
Cdd:cd03111   72 LDsavTRHSSGLSLLPAPQELeDLEALGAEQVDKL--LQVLRAF-------YDHIIVDLGHFLDEVTLAVLEAADEILLV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792 155 MQPHYFALR---GIEEFIETTEIVRKnlnhslKINILITIADTRSNLAkevIDEIKQYFSDRLFKTIIRKNITLVEASSQ 231
Cdd:cd03111  143 TQQDLPSLRnarRLLDSLRELEGSSD------RLRLVLNRYDKKSEIS---PKDIEEALGLEVFATLPNDYKAVSESANT 213

                        250
                 ....*....|.
gi 973109792 232 GTPALHYSPKS 242
Cdd:cd03111  214 GRPLVEVAPRS 224
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-153 2.55e-14

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: 69.52  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD---PQAHTTLGLSLEPdslskTILNVLEphrskNKLKLEEV 77
Cdd:cd05387   19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGLPNEP-----GLSEVLS-----GQASLEDV 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973109792  78 IIklKINSENNLFLAPSNIDFASAEykLIDqigrEDFLGASIRECKVPFDYILIDCPPSLGILTVNAL-KACDEVII 153
Cdd:cd05387   89 IQ--STNIPNLDVLPAGTVPPNPSE--LLS----SPRFAELLEELKEQYDYVIIDTPPVLAVADALILaPLVDGVLL 157
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 3-220 1.98e-11

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 63.46  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   3 IISIANQKGGVAKTTTTINLGASLASLGRKVLLID-LDPQAHTTLGLSLEPDsLSKTILNVLEPHRSKNKlklEEVIIKL 81
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPD-LHIHAEDTLLPFYLGEK---DDATYAI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  82 KINSENNLFLAPSNIDFASAEYKLidqIGRED----------FLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEV 151
Cdd:PRK13705 184 KPTCWPGLDIIPSCLALHRIETEL---MGKFDegklptdphlMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVL 260

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973109792 152 IIPMQPHYFALRGIEEFIETTEIVRKNLN---HSLKINILIT-IADTRSNLAKEVIDEIKQYFSDRLFKTIIR 220
Cdd:PRK13705 261 IVPTPAELFDYTSALQFFDMLRDLLKNVDlkgFEPDVRILLTkYSNSNGSQSPWMEEQIRDAWGSMVLKNVVR 333
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-177 3.22e-09

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: 56.31  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDpqahttlglsLEPDSLSKTILNVLEPHRSKnKLKLEEVIIKL 81
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLD----------LRQRTFHRYFENRSATADRT-GLSLPTPEHLN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   82 KINSENNLFLAPSNIDFASAEyKLIDQIGREdflgasireckvpFDYILIDCPPSLGILTVNALKACDEVIIPM------ 155
Cdd:pfam09140  70 LPDNDVAEVPDGENIDDARLE-EAFADLEAR-------------CDFIVIDTPGSDSPLSRLAHSRADTLVTPLndsfvd 135

                         170       180
                  ....*....|....*....|....*....
gi 973109792  156 -------QPHYFALRGIEEFIETTEIVRK 177
Cdd:pfam09140 136 fdllgqvDPETFKVKRPSFYAEMVWEARK 164
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 3-220 6.19e-09

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 55.79  E-value: 6.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   3 IISIANQKGGVAKTTTTINLGASLASLGRKVLLID-LDPQAHTTLGLSLEPDslsktilnvLEPHRSKNKL-----KLEE 76
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVPD---------LHIHADDTLLpfylgERDN 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  77 VIIKLKINSENNLFLAPSNIDFASAEYKLIDQIGREDF-------LGASIRECKVPFDYILIDCPPSLGILTVNALKACD 149
Cdd:PHA02519 179 AEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKLphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAAD 258

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973109792 150 EVIIPMQPHYFALRGIEEFIETTEIVRKNLN---HSLKINILIT-IADTRSNLAKEVIDEIKQYFSDRLFKTIIR 220
Cdd:PHA02519 259 VIVVATPAELFDYVSVLQFFTMLLDLLATVDlggFEPVVRLLLTkYSLTVGNQSRWMEEQIRNTWGSMVLRQVVR 333
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-188 2.82e-08

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: 53.23  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD---PQAHTTLGLSLEPDSLSKtilNVLEPHRSKNklkleevi 78
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADiygPSIPRMLGLEGERPEQSD---GGIIPVEAHG-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   79 ikLKINSennlflapsnIDFasaeykLIDQ-----IGREDFLGASIRE--CKV---PFDYILIDCPPSLG--ILTVNALK 146
Cdd:pfam10609  73 --IKVMS----------IGF------LLPDeddavIWRGPMKSGAIKQflTDVdwgELDYLIIDLPPGTGdeQLTLAQLL 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 973109792  147 ACDEVIIPMQPHYFALrgieefiettEIVRKNLN--HSLKINIL 188
Cdd:pfam10609 135 PLTGAVIVTTPQDVAL----------LDVRKAIDmfKKVNVPVL 168
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 10-80 3.83e-08

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 53.24  E-value: 3.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSlepdslSKTILNVLEPHRSK--NKLKLEEVIIK 80
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV------GEKIPTVLDVLREKgiDNLGLEDIIYE 75
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
2-80 4.23e-08

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 52.83  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    2 RIISIANqKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTT---LGLSLEPdslskTILNVLEPHRSKNKLKLEEVI 78
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrllLGGKLQP-----TVLDTAREKGYVEDVEVEDVV 74


                  ..
gi 973109792   79 IK 80
Cdd:pfam00142  75 YK 76
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 10-64 1.03e-07

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 51.89  E-value: 1.03e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSlepDSLSKTILNVLE 64
Cdd:PRK13185  10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLT---GKLVPTVIDILE 61
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 10-48 1.21e-07

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: 51.60  E-value: 1.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGL 48
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-187 1.25e-07

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 50.96  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD---PQAHTTLGLSLEPdslsktilnvlePHRSKNKLKLEEVi 78
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADiygPSIPRLLGVEGKP------------LHQSEEGIVPVEV- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  79 IKLKINSENNLfLAPSNIDfasaeyklidqIGREDFLGASIREckvpF---------DYILIDCPPSLG--ILTVNALKA 147
Cdd:cd02037   68 GGIKVMSIGFL-LPEDDAV-----------IWRGPMKSGAIKQ----FlkdvdwgelDYLIIDLPPGTGdeHLSLVQLIP 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 973109792 148 CDEVIIPMQPHYFALrgieefiettEIVRKNLNHSLKINI 187
Cdd:cd02037  132 IDGAVVVTTPQEVSL----------IDVRKAIDMCKKLNI 161
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 10-66 3.39e-07

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 49.99  E-value: 3.39e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSlepDSLSKTILNVLEPH 66
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLT---GFLIPTVIDVLQSV 61
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 10-135 4.94e-07

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: 49.43  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPqAHtTLGLSLEPDSLSKTILNV--------LEPHRS--KNKLKLEEVII 79
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP-AH-SLSDAFGQKLGGETPVKGapnlwameIDPEEAleEYWEEVKELLA 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973109792  80 KLKINSENNLF-----LAPSNIDFASAEYKLIDQIGREDflgasireckvpFDYILIDCPP 135
Cdd:cd02035   86 QYLRLPGLDEVyaeelLSLPGMDEAAAFDELREYVESGE------------YDVIVFDTAP 134
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-39 6.51e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 47.04  E-value: 6.51e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD 39
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 10-78 2.12e-06

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 47.89  E-value: 2.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLslepdsLS----KTILNVLEphRSKNKLKLEEVI 78
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLL------LGgkaiPTVLDTLR--EKGEVEELEDVI 72
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 1-253 2.25e-06

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: 47.37  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDpqahttlglslePDSLSKTILNVlePHRSKNKLKLEEViiK 80
Cdd:pfam06564   1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLS------------PDNLLRLHFNV--PFEHRQGWARAEL--D 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   81 LKINSENNLFLAPsNIDF------ASAEYKLIDQI-GREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVII 153
Cdd:pfam06564  65 GADWRDAALEYTP-GLDLlpfgrlSVEEQENLQQLqPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  154 PMQP----HyfalrgieefIETTEIVRKNLNHslkinILITIADTRSNLAKEVIDEIKQYFSDRLfKTIIRKNITLVEAS 229
Cdd:pfam06564 144 VVNPdancH----------VLLHQQPLPDADH-----LLINDFRPASQLQQDLLQLWRQSQRRLL-PLVIHRDEALAEAL 207

                         250       260
                  ....*....|....*....|....
gi 973109792  230 SQGTPALHYSPKSHGAIDYYKLAQ 253
Cdd:pfam06564 208 AAKQPLGEYRPDSLAAEEVLTLAN 231
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 10-59 3.29e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.08  E-value: 3.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAH--TTLGLSLEPDSLsKTI 59
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANlaEALGLEVEADLI-KPL 58
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 2-85 5.16e-06

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: 46.54  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANqKGGVAKTTTTINLGASLASLGRKVLLIDLDPQA--HTTLGLSLEPDSLSKTILNVLEPHRSKNKLKLEEVII 79
Cdd:cd02034    1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSnlAETLGVEVEKLPLIKTIGDIRERTGAKKGEPPEGMSL 79


                 ....*.
gi 973109792  80 KLKINS 85
Cdd:cd02034   80 NPYVDD 85
PRK10818 PRK10818
septum site-determining protein MinD;
2-163 5.76e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 46.47  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD-PQAHTTLGLSLEpDSLSKTILNVLEPHRSknklkLEEVIIK 80
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCE-RRVVYDFVNVIQGDAT-----LNQALIK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792  81 LKinSENNLFLAPsnidfaSAEYKLIDQIGREDFLGASIRECKVPFDYILIDCPPSLGILTVNALKACDEVIIPMQPHYF 160
Cdd:PRK10818  77 DK--RTENLYILP------ASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVS 148


                 ...
gi 973109792 161 ALR 163
Cdd:PRK10818 149 SVR 151
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-66 7.65e-06

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 46.35  E-value: 7.65e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973109792   1 MRIISIANqKGGVAKTTTTINLGASLASLGRKVLLIDLDPqAHtTLGLSLEPDsLSKTILNVLEPH 66
Cdd:COG0003    3 TRIIFFTG-KGGVGKTTVAAATALALAERGKRTLLVSTDP-AH-SLGDVLGTE-LGNEPTEVAVPN 64
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 1-118 1.39e-05

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: 45.42  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    1 MRIISIANqKGGVAKTTTTINLGASLASLGRKVLLIDLDPqAHttlglslepdSLSKtILNVlephrsknKLKLEEVIIK 80
Cdd:pfam02374   1 MRWIFFGG-KGGVGKTTVSAATAVQLSELGKKVLLISTDP-AH----------SLSD-SFNQ--------KFGHEPTKVK 59

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 973109792   81 lkinseNNLFLAPSNIDFASAEYKLIDQIGREDFLGAS 118
Cdd:pfam02374  60 ------ENLSAMEIDPNMELEEYWQEVQKYMNALLGLR 91
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-153 3.52e-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: 43.58  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792    1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLsKTILNVLephrsKNKLKLEEVIIK 80
Cdd:TIGR01007  17 IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKI-TGLTNFL-----SGTTDLSDAICD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   81 LKInseNNLFLA--------PSNIDFASAEYKLIDQIGREdflgasireckvpFDYILIDCPPsLGILTVNAL--KACDE 150
Cdd:TIGR01007  91 TNI---ENLDVItagpvppnPTELLQSSNFKTLIETLRKR-------------FDYIIIDTPP-IGTVTDAAIiaRACDA 153


                  ...
gi 973109792  151 VII 153
Cdd:TIGR01007 154 SIL 156
chlL CHL00072
photochlorophyllide reductase subunit L
 10-64 1.79e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 42.03  E-value: 1.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 973109792  10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSlepDSLSKTILNVLE 64
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLT---GFLIPTIIDTLQ 59
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
3-47 2.15e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 41.95  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 973109792   3 IISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD---PQAHTTLG 47
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADiygPSIPTMLG 156
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-55 2.29e-04

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: 42.38  E-value: 2.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 973109792   10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSL 55
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNL 374
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 2-45 4.05e-04

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


Pssm-ID: 349753  Cd Length: 329  Bit Score: 40.97  E-value: 4.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 973109792   2 RIISIANqKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTT 45
Cdd:cd02033   32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTT 74
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-154 7.00e-04

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 39.83  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   2 RIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHTTLGLSLEPDSLSKTILNVLEPHRSKNKLKLEEVIikl 81
Cdd:cd17869    4 SVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLMSDHLYTLKSRKANLADKLESCV--- 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973109792  82 KINSENNLFLAPSNIDFASAEYKLIDQigreDFLGASIRECKVpFDYILIDCPPSLGILTVNALKACDEVIIP 154
Cdd:cd17869   81 KQHESGVYYFSPFKSALDILEIKKDDI----LHMITKLVEAHA-YDYIIMDLSFEFSSTVCKLLQASHNNVVI 148
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
1-39 3.86e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 37.90  E-value: 3.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 973109792   1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD 39
Cdd:PRK13849   1 MKLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEAD 39
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-104 5.65e-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: 37.76  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973109792   10 KGGVAKTTTTINLGASLASLGRKVLLIDLDPQAHttLGlslepDSLSKTILNVLEPhrsknklkleeviiklkINSENNL 89
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN--VG-----QVFGQTIGNKITA-----------------IAGVPGL 66

                          90
                  ....*....|....*..
gi 973109792   90 FLApsNID--FASAEYK 104
Cdd:TIGR04291  67 FAL--EIDpqAAAQAYR 81
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 1-39 6.47e-03

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


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 37.16  E-value: 6.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 973109792    1 MRIISIANQKGGVAKTTTTINLGASLASLGRKVLLIDLD 39
Cdd:pfam07015   1 MQLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEAD 39
 
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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