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Conserved domains on  [gi|1584016544|ref|WP_130785434|]
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MULTISPECIES: plasmid partitioning protein RepA [Rhizobium]

Protein Classification

plasmid partitioning protein RepA( domain architecture ID 11496880)

plasmid partitioning protein RepA is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 13-397 0e+00

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: 643.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  13 DDKILMQGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTPITMSGNRRYYTAEQMLEL 92
Cdd:TIGR03453   1 DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPETLSNGRRSYTLEQINEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  93 RFFLDRTGKtEAKRYVPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELD- 171
Cdd:TIGR03453  81 RRHLAQRGR-EARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 172 -RNPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTPLAMQAGADGKR-FFTRLGKSLEEVDIRYDVVV 249
Cdd:TIGR03453 160 gENETLYGAIRYDDERRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRALSRGQGGDTiFFARVGEALAEVEDDYDVVV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 250 VDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRMDWLRYLITRFEPTDVPQVQMLG 329
Cdd:TIGR03453 240 IDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMVA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 330 FMQSMFAEEILKSPMVKTTAISDAGLTKRTLYELDRSNFTRETYDRAIECMDAVNFEIQGLIHRAWGR 397
Cdd:TIGR03453 320 FLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR 387
 
Name Accession Description Interval E-value
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 13-397 0e+00

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: 643.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  13 DDKILMQGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTPITMSGNRRYYTAEQMLEL 92
Cdd:TIGR03453   1 DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPETLSNGRRSYTLEQINEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  93 RFFLDRTGKtEAKRYVPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELD- 171
Cdd:TIGR03453  81 RRHLAQRGR-EARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 172 -RNPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTPLAMQAGADGKR-FFTRLGKSLEEVDIRYDVVV 249
Cdd:TIGR03453 160 gENETLYGAIRYDDERRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRALSRGQGGDTiFFARVGEALAEVEDDYDVVV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 250 VDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRMDWLRYLITRFEPTDVPQVQMLG 329
Cdd:TIGR03453 240 IDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMVA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 330 FMQSMFAEEILKSPMVKTTAISDAGLTKRTLYELDRSNFTRETYDRAIECMDAVNFEIQGLIHRAWGR 397
Cdd:TIGR03453 320 FLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR 387
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 7-397 6.74e-162

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 460.68  E-value: 6.74e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544   7 LPSFefDDKILMQGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTPITMSGNRRYYTA 86
Cdd:PRK13869   12 RPSV--DVTIGEHAEQLSSQLQAMSEALFPPTSHKSLRKFTSGEAARLMKISDSTLRKMTLAGEGPQPELASNGRRFYTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  87 EQMLELRFFLDRTGK-TEAKRYVPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHG 165
Cdd:PRK13869   90 GQINEIRQMLAGSTRgRESIDFVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 166 FQPELD--RNPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTPLAMQAGADGKR-FFTRLGKSLEEVD 242
Cdd:PRK13869  170 VLPETDvgANETLYAAIRYDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGlFFTRVAQAFDEVA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 243 IRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRMDWLRYLITRFEPTDV 322
Cdd:PRK13869  250 DDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFIRYLLTRYEPQDA 329

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1584016544 323 PQVQMLGFMQSMFAEEILKSPMVKTTAISDAGLTKRTLYELDRSNFTRETYDRAIECMDAVNFEIQGLIHRAWGR 397
Cdd:PRK13869  330 PQTKVAALLRNMFEDHVLTNPMVKSAAVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEALIKMAWGR 404
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 118-378 6.83e-70

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: 220.50  E-value: 6.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPElDRNPSLYDAIRyddERKSIADVILPTN 197
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD-DLDPTLYDLLL---DDAPLEDAIVPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 198 FPGLDIVPANLELQEYEYDtpLAMQAGADgkrffTRLGKSLEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQ 277
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIE--LVSRPGRE-----LRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 278 MLDLMSMSQFLLMLGNITKTIkkagaNVRMDWLRYLITRFEPTDVPQVQMLGFMQSMFAEEILKSPMVKTTAISDAGLTK 357
Cdd:COG1192   151 YLSLEGLAQLLETIEEVREDL-----NPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAG 225

                         250       260
                  ....*....|....*....|.
gi 1584016544 358 RTLYELDRSNFTRETYDRAIE 378
Cdd:COG1192   226 KPVFEYDPKSKGAKAYRALAE 246
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 120-360 8.03e-51

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: 170.22  E-value: 8.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 120 VAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELDRNP-SLYDAIRYDDERKSIADVIlPTNF 198
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqALAEGLKGRVNLDPILLKE-KSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 199 PGLDIVPANLELQEYEYDTPlamqagadGKRFFTRLGKSLEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQM 278
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKELL--------GPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 279 LDLMSMSQfllmLGNITKTIKKAGANVRMDWLRYLITRFEPTDVPQVQMLGFMQSMFAEEILKSpMVKTTAISDAGLTKR 358
Cdd:pfam01656 152 ILVEDAKR----LGGVIAALVGGYALLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGV-IPRDEAVAEAPARGL 226


                  ..
gi 1584016544 359 TL 360
Cdd:pfam01656 227 PV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 119-332 2.20e-22

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: 91.83  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSalhgfqpeldrnpslydairydderksiadvilptnf 198
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 199 pgldivpanlelqeyeydtplamqagadgkrfftrlgksleevDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQM 278
Cdd:cd02042    45 -------------------------------------------SWLYDYILIDTPPSLGLLTRNALAAADLVLIPVQPSP 81

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1584016544 279 LDLMSMSQFLLMLGNITKTIKKaganvRMDWLRYLITRFEPTDVPQVQMLGFMQ 332
Cdd:cd02042    82 FDLDGLAKLLDTLEELKKQLNP-----PLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
119-256 2.36e-16

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 76.82  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHgfqpeldrnpslydAIRYDDerksiadvilptnf 198
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWA--------------AAREDE-------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 199 PGLDIVpanlelqeyeydtplamqaGADGKrfftRLGKSLEEVDIRYDVVVVDCPPQL 256
Cdd:NF041546   53 RPFPVV-------------------GLARP----TLHRELPSLARDYDFVVIDGPPRA 87
 
Name Accession Description Interval E-value
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 13-397 0e+00

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: 643.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  13 DDKILMQGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTPITMSGNRRYYTAEQMLEL 92
Cdd:TIGR03453   1 DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPETLSNGRRSYTLEQINEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  93 RFFLDRTGKtEAKRYVPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELD- 171
Cdd:TIGR03453  81 RRHLAQRGR-EARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 172 -RNPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTPLAMQAGADGKR-FFTRLGKSLEEVDIRYDVVV 249
Cdd:TIGR03453 160 gENETLYGAIRYDDERRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRALSRGQGGDTiFFARVGEALAEVEDDYDVVV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 250 VDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRMDWLRYLITRFEPTDVPQVQMLG 329
Cdd:TIGR03453 240 IDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMVA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 330 FMQSMFAEEILKSPMVKTTAISDAGLTKRTLYELDRSNFTRETYDRAIECMDAVNFEIQGLIHRAWGR 397
Cdd:TIGR03453 320 FLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR 387
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 7-397 6.74e-162

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 460.68  E-value: 6.74e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544   7 LPSFefDDKILMQGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTPITMSGNRRYYTA 86
Cdd:PRK13869   12 RPSV--DVTIGEHAEQLSSQLQAMSEALFPPTSHKSLRKFTSGEAARLMKISDSTLRKMTLAGEGPQPELASNGRRFYTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  87 EQMLELRFFLDRTGK-TEAKRYVPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHG 165
Cdd:PRK13869   90 GQINEIRQMLAGSTRgRESIDFVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 166 FQPELD--RNPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTPLAMQAGADGKR-FFTRLGKSLEEVD 242
Cdd:PRK13869  170 VLPETDvgANETLYAAIRYDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGlFFTRVAQAFDEVA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 243 IRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRMDWLRYLITRFEPTDV 322
Cdd:PRK13869  250 DDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFIRYLLTRYEPQDA 329

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1584016544 323 PQVQMLGFMQSMFAEEILKSPMVKTTAISDAGLTKRTLYELDRSNFTRETYDRAIECMDAVNFEIQGLIHRAWGR 397
Cdd:PRK13869  330 PQTKVAALLRNMFEDHVLTNPMVKSAAVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEALIKMAWGR 404
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 118-378 6.83e-70

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: 220.50  E-value: 6.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPElDRNPSLYDAIRyddERKSIADVILPTN 197
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD-DLDPTLYDLLL---DDAPLEDAIVPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 198 FPGLDIVPANLELQEYEYDtpLAMQAGADgkrffTRLGKSLEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQ 277
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIE--LVSRPGRE-----LRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 278 MLDLMSMSQFLLMLGNITKTIkkagaNVRMDWLRYLITRFEPTDVPQVQMLGFMQSMFAEEILKSPMVKTTAISDAGLTK 357
Cdd:COG1192   151 YLSLEGLAQLLETIEEVREDL-----NPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAG 225

                         250       260
                  ....*....|....*....|.
gi 1584016544 358 RTLYELDRSNFTRETYDRAIE 378
Cdd:COG1192   226 KPVFEYDPKSKGAKAYRALAE 246
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 120-360 8.03e-51

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: 170.22  E-value: 8.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 120 VAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELDRNP-SLYDAIRYDDERKSIADVIlPTNF 198
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqALAEGLKGRVNLDPILLKE-KSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 199 PGLDIVPANLELQEYEYDTPlamqagadGKRFFTRLGKSLEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQM 278
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKELL--------GPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 279 LDLMSMSQfllmLGNITKTIKKAGANVRMDWLRYLITRFEPTDVPQVQMLGFMQSMFAEEILKSpMVKTTAISDAGLTKR 358
Cdd:pfam01656 152 ILVEDAKR----LGGVIAALVGGYALLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGV-IPRDEAVAEAPARGL 226


                  ..
gi 1584016544 359 TL 360
Cdd:pfam01656 227 PV 228
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 19-395 4.41e-38

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 141.30  E-value: 4.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  19 QGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTP-ITMSG---NRRYYTAEQMLELRf 94
Cdd:PHA02519   13 RGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPdFETRGrveRRAGYTIDQISHMR- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  95 flDRTGKteakryvPHRKPGDKLQVV-AVVNFKGGSGKTTTTAHLAQHLALTGHRVLAID-LDPQASLSALHGFQPELDR 172
Cdd:PHA02519   92 --DHFGN-------PNQRPDDKNPVVlAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLHI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 173 NPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTplaMQAGADGKRFFT---RLGKSLEEVDIRYDVVV 249
Cdd:PHA02519  163 HADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDL---MQYHDAGKLPHPphlMLRAAIESVWDNYDIIV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 250 VDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRmdwLRYLITRFEPTDVPQVQ-ML 328
Cdd:PHA02519  240 IDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPV---VRLLLTKYSLTVGNQSRwME 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584016544 329 GFMQSMFAEEILKSPMVKTTAISDAGLTKRTLYEldRSNFTRET---YDRAIECMDAVNFEI-QGLIHRAW 395
Cdd:PHA02519  317 EQIRNTWGSMVLRQVVRVTDEVGKGQIKMRTVFE--QAANQRSTlnaWRNAVAIWEPVCAEIfNDLIKPRW 385
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 118-300 4.92e-36

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: 130.01  E-value: 4.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPElDRNPSLYDAIRyddERKSIADVILPTN 197
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKN-NVEKTIYELLI---GECNIEEAIIKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 198 FPGLDIVPANLELQEYEYDTplamqAGADGKRFftRLGKSLEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQ 277
Cdd:pfam13614  78 IENLDLIPSNIDLAGAEIEL-----IGIENREN--ILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150

                         170       180
                  ....*....|....*....|...
gi 1584016544 278 MLDLMSMSQFLLMLGNITKTIKK 300
Cdd:pfam13614 151 YYALEGLSQLLNTIKLVKKRLNP 173
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 14-362 2.92e-35

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 133.56  E-value: 2.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  14 DKILMQGAEISRKLDQLRLENFPPNAKKNLRQFSLAEVAHYLGVTPSNLKRLYLDGKGPTPIT-MSG---NRRYYTAEQM 89
Cdd:PRK13705    8 NQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMeMRGrveQRVGYTIEQI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  90 LELR-FFLDRtgkteakryvPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAID-LDPQASLSALHGFQ 167
Cdd:PRK13705   88 NHMRdVFGTR----------LRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 168 PELDRNPSLYDAIRYDDERKSIADVILPTNFPGLDIVPANLELQEYEYDTPLAMQAGADGKRFFTRLGKSLEEVDIRYDV 247
Cdd:PRK13705  158 PDLHIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 248 VVVDCPPQLGYLTLTALTAATSVLITVHPQMLDLMSMSQFLLMLGNITKTIKKAG--ANVRMdwlryLITRFEPTDVPQV 325
Cdd:PRK13705  238 IVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGfePDVRI-----LLTKYSNSNGSQS 312

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1584016544 326 Q-MLGFMQSMFAEEILKSPMVKTTAISDAGLTKRTLYE 362
Cdd:PRK13705  313 PwMEEQIRDAWGSMVLKNVVRETDEVGKGQIRMRTVFE 350
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 119-332 2.20e-22

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: 91.83  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSalhgfqpeldrnpslydairydderksiadvilptnf 198
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 199 pgldivpanlelqeyeydtplamqagadgkrfftrlgksleevDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQM 278
Cdd:cd02042    45 -------------------------------------------SWLYDYILIDTPPSLGLLTRNALAAADLVLIPVQPSP 81

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1584016544 279 LDLMSMSQFLLMLGNITKTIKKaganvRMDWLRYLITRFEPTDVPQVQMLGFMQ 332
Cdd:cd02042    82 FDLDGLAKLLDTLEELKKQLNP-----PLLILGILLTRVDPRTKLAREVLEELK 130
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 89-257 7.82e-21

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: 91.79  E-value: 7.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544  89 MLELRFFLDRTGKTEAKRYVPHRKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDP-QASLSALHGfq 167
Cdd:COG0489    64 LLLLGLLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLG-- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 168 peLDRNPSLYDAIRyddERKSIADVILPTNFPGLDIVPANLELQeyEYDTPLAMQAgadgkrfFTRLgksLEEVDIRYDV 247
Cdd:COG0489   142 --LENRPGLSDVLA---GEASLEDVIQPTEVEGLDVLPAGPLPP--NPSELLASKR-------LKQL---LEELRGRYDY 204

                         170
                  ....*....|
gi 1584016544 248 VVVDCPPQLG 257
Cdd:COG0489   205 VIIDTPPGLG 214
ParA_partition NF041546
ParA family partition ATPase;
119-256 2.36e-16

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 76.82  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHgfqpeldrnpslydAIRYDDerksiadvilptnf 198
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWA--------------AAREDE-------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 199 PGLDIVpanlelqeyeydtplamqaGADGKrfftRLGKSLEEVDIRYDVVVVDCPPQL 256
Cdd:NF041546   53 RPFPVV-------------------GLARP----TLHRELPSLARDYDFVVIDGPPRA 87
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 126-252 3.56e-15

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 74.43  E-value: 3.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELDRNPSLYDAIRYDDERKSIADV-ILPTNFPGLDIv 204
Cdd:COG3640     8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLIKPLGEMRELIKERTGAPGGgMFKLNPKVDDI- 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1584016544 205 panleLQEYEYDTP----LAM---QAGADG---------KRFFTRLgksleeVDIRYDVVVVDC 252
Cdd:COG3640    87 -----PEEYLVEGDgvdlLVMgtiEEGGSGcycpenallRALLNHL------VLGNYEYVVVDM 139
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 133-254 1.01e-14

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: 73.00  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 133 TTTAHLAQHLALTGHRVLAIDLDPQ-ASLSALHGFQPEldrnPSLYDAIRyddERKSIADVILPTNfPGLDIVPANLELQ 211
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPK----ATLADVLA---GEADLEDAIVQGP-GGLDVLPGGSGPA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1584016544 212 EYEYDTPLAmqagadgkrfftRLGKSLEEVDIRYDVVVVDCPP 254
Cdd:COG0455    73 ELAELDPEE------------RLIRVLEELERFYDVVLVDTGA 103
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 119-278 7.99e-14

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: 70.92  E-value: 7.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD-PQASLSALHGFQpelDRNPSLYDAIRyddERKSIADVILPTN 197
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGME---DKPVTLHDVLA---GEADIKDAIYEGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 198 FpGLDIVPANLELQEYeydtplaMQAGADgkrfftRLGKSLEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITVHPQ 277
Cdd:TIGR01969  76 F-GVKVIPAGVSLEGL-------RKADPD------KLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE 141


                  .
gi 1584016544 278 M 278
Cdd:TIGR01969 142 I 142
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 118-254 9.75e-14

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: 69.91  E-value: 9.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD-PQASLSALHGFQPELDrnpsLYDAIRyddERKSIADVILPT 196
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPKKT----LGDVLK---GRVSLEDIIVEG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 197 NfPGLDIVPANLELQEYeYDTPLAMQAgadgkrfftRLGKSLEEVDIRYDVVVVDCPP 254
Cdd:cd02038    74 P-EGLDIIPGGSGMEEL-ANLDPEQKA---------KLIEELSSLESNYDYLLIDTGA 120
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 111-254 1.10e-13

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: 69.14  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 111 RKPGDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPqaslsalhgfqpeldRNPSLYDAIRYDDER---- 186
Cdd:cd05387    13 AGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADL---------------RRPSLHRLLGLPNEPglse 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1584016544 187 -----KSIADVILPTNFPGLDIVPANlelqeyeydtplamQAGADGKRFFT--RLGKSLEEVDIRYDVVVVDCPP 254
Cdd:cd05387    78 vlsgqASLEDVIQSTNIPNLDVLPAG--------------TVPPNPSELLSspRFAELLEELKEQYDYVIIDTPP 138
PHA02518 PHA02518
ParA-like protein; Provisional
 119-286 2.87e-13

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 68.34  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASlsalhgfqpeldrnpslydAIRYDDERKSiadvilptnf 198
Cdd:PHA02518    2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGS-------------------STDWAEAREE---------- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 199 pGLDIVPAnlelqeyeydtplamqagadgkrffTRLGKS----LEEVDIRYDVVVVDCPPQLGYLTLTALTAATSVLITV 274
Cdd:PHA02518   53 -GEPLIPV-------------------------VRMGKSiradLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPV 106

                         170
                  ....*....|..
gi 1584016544 275 HPQMLDLMSMSQ 286
Cdd:PHA02518  107 QPSPFDIWAAPD 118
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 118-256 2.50e-12

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: 67.45  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLA-LTGHRVLAIDLDPQASLSALHgFQpeLDRNPSLYDAIRyDDER--KSIADVIL 194
Cdd:COG4963   103 RVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALY-LD--LEPRRGLADALR-NPDRldETLLDRAL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1584016544 195 PTNFPGLDIVPANLELQEYEYDTPlamqagadgkRFFTRLgksLEEVDIRYDVVVVDCPPQL 256
Cdd:COG4963   179 TRHSSGLSVLAAPADLERAEEVSP----------EAVERL---LDLLRRHFDYVVVDLPRGL 227
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 119-353 3.26e-11

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: 63.13  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSaLHgFQPELDRNPSLYDAIRYDDERKSIADVILptnf 198
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLR-LH-FGMDWSVRDGWARALLNGADWAAAAYRSP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 199 PGLDIVPANlELQEYEYDTPLAMQAGAdgkrfftrLGKSLEEVDIR-YDVVVVDCPPQLGYLTLTALTAATSVL------ 271
Cdd:TIGR03371  77 DGVLFLPYG-DLSADEREAYQAHDAGW--------LARLLQQLDLAaRDWVLIDLPRGPSPITRQALAAADLVLvvvnad 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 272 ----ITVHPQMLDLMSMSQfllmlGNITktikkaganvrmdwLRYLITRFEPTDVPQVQMLGFMQSMFAEEILKSPMVKT 347
Cdd:TIGR03371 148 aacyATLHQLALALFAGSG-----PRDG--------------PRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRD 208


                  ....*.
gi 1584016544 348 TAISDA 353
Cdd:TIGR03371 209 EAVSEA 214
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 119-253 2.09e-10

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: 60.93  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDP-QASLSalhgfqpeldrnpslydaiRYDDERKSIADVI---L 194
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFH-------------------RYFENRSATADRTglsL 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1584016544 195 PTnfPGLDIVPANLELQEYEYDTPLamqagadgkrfFTRLGKSLEEVDIRYDVVVVDCP 253
Cdd:pfam09140  63 PT--PEHLNLPDNDVAEVPDGENID-----------DARLEEAFADLEARCDFIVIDTP 108
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 118-180 2.15e-10

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: 57.44  E-value: 2.15e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD--------PQASLSALHGFQPELDRNPSLYDAI 180
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDdyvlidggGGLETGLLLGTIVALLALKKADEVI 71
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 119-253 5.40e-10

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: 59.14  E-value: 5.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD-PQASLSALHGFQpeldrNPSLYDAIRYDDERKSIADVILPT- 196
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLE-----NRIVYTLVDVLEGECRLEQALIKDk 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1584016544 197 NFPGLDIVPANLELQEYEYDtplamqagadgKRFFTRLGKSLEEvdiRYDVVVVDCP 253
Cdd:cd02036    77 RWENLYLLPASQTRDKDALT-----------PEKLEELVKELKD---SFDFILIDSP 119
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 114-254 6.25e-10

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: 58.60  E-value: 6.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 114 GDKLQVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLsaLHGFQPELDRNPSLYDAIrydDERKSIADVI 193
Cdd:TIGR01007  14 GAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSV--MSGTFKSQNKITGLTNFL---SGTTDLSDAI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1584016544 194 LPTNFPGLDI-----VPANlelqeyeydtPLAMQAGADgkrfFTRLgksLEEVDIRYDVVVVDCPP 254
Cdd:TIGR01007  89 CDTNIENLDVitagpVPPN----------PTELLQSSN----FKTL---IETLRKRFDYIIIDTPP 137
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 118-256 6.60e-09

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: 56.13  E-value: 6.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLA-LTGHRVLAIDLD-PQASLSALHGFQPELDRNPSLYDAIRYDdeRKSIADVILP 195
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDlPFGDLGLYLNLRPDYDLADVIQNLDRLD--RTLLDSAVTR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584016544 196 TNfPGLDIVPANLELQEYEydtplAMQAGaDGKRFFTRLGKSleevdirYDVVVVDCPPQL 256
Cdd:cd03111    79 HS-SGLSLLPAPQELEDLE-----ALGAE-QVDKLLQVLRAF-------YDHIIVDLGHFL 125
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
126-350 8.18e-09

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 56.37  E-value: 8.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALhgFQPELDRNPslydairydderKSIADvilptnfPGLDIVp 205
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDV--LGTELGNEP------------TEVAV-------PNLYAL- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 206 anlelqeyEYDTPLAMQA-----GADGKRFFTRLGK--------------SLEEV-----DIRYDVVVVDCPPqlgyltl 261
Cdd:COG0003    69 --------EIDPEAELEEywervRAPLRGLLPSAGVdelaeslpgteelaALDELlelleEGEYDVIVVDTAP------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 262 taltaatsvliTVHpqMLDLMSMSQFLL-MLGNITKTIKKAganvrMDWLRYLITRFEPTDVPQVQMLGFMQSMFAE--E 338
Cdd:COG0003   134 -----------TGH--TLRLLSLPELLGwWLDRLLKLRRKA-----SGLGRPLAGILGLPDDPVLEGLEELRERLERlrE 195

                         250
                  ....*....|..
gi 1584016544 339 ILKSPmvKTTAI 350
Cdd:COG0003   196 LLRDP--ERTSF 205
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 126-254 3.66e-08

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: 54.05  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLS-----ALHGFQP----------------ELDRNPS-----LYDA 179
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSdafgqKLGGETPvkgapnlwameidpeeALEEYWEevkelLAQY 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1584016544 180 IRYDDERKSIADVILptNFPGLDivpanlELqeyeydtpLAMQAgadgkrfFTRLGKSLEevdirYDVVVVDCPP 254
Cdd:cd02035    88 LRLPGLDEVYAEELL--SLPGMD------EA--------AAFDE-------LREYVESGE-----YDVIVFDTAP 134
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 126-251 1.54e-07

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: 51.93  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSALHGFQPELDRNPSLYDAIRYDDERKSIADVILPTNFPGLDIVP 205
Cdd:cd02034     8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKTIGDIRERTGAKKGEPPEGMSLNPYVDDII 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1584016544 206 ANLELQEYEYDTpLAM---QAGADG-----KRFFTRLGKSLeeVDIRYDVVVVD 251
Cdd:cd02034    88 KEIIVEPDGIDL-LVMgrpEGGGSGcycpvNALLRELLRHL--ALKNYEYVVID 138
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 126-155 3.76e-07

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 50.83  E-value: 3.76e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLD 155
Cdd:COG2894    11 KGGVGKTTTTANLGTALALLGKKVVLIDAD 40
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 119-155 2.86e-06

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: 48.49  E-value: 2.86e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD 155
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 119-253 3.57e-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: 47.76  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPqASLSALHGFQP----------ELDRNPSLYDAIRYdderks 188
Cdd:pfam06564   3 ILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSP-DNLLRLHFNVPfehrqgwaraELDGADWRDAALEY------ 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1584016544 189 iadvilptnFPGLDIVP-ANLELQEYEYDTPLAMQAGAdGKRFFTRLGKsleevdiRYDVVVVDCP 253
Cdd:pfam06564  76 ---------TPGLDLLPfGRLSVEEQENLQQLQPDPGA-WCRRLQQLKG-------RYDWVLFDLP 124
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 122-206 7.66e-06

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: 46.97  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 122 VVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQA--SLSALHGFQP----ELDRNPSLYDAIRYDDerksiadvILP 195
Cdd:cd02117     4 VVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHdsTLLLTGGKVPptidEMLTEDGTAEELRRED--------LLF 75

                          90
                  ....*....|.
gi 1584016544 196 TNFPGLDIVPA 206
Cdd:cd02117    76 SGFNGVDCVEA 86
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 119-155 3.17e-05

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: 44.80  E-value: 3.17e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD 155
Cdd:cd02037     2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
minD CHL00175
septum-site determining protein; Validated
 118-253 8.52e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 43.99  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD-PQASLSALHGFQpeldrNPSLYDAIR-YDDERKSIADVILP 195
Cdd:CHL00175   16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLE-----NRVLYTAMDvLEGECRLDQALIRD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 196 TNFPGLDIVPANLELQEYEYdTPLAMQagadgkrfftRLGKSLEEVDirYDVVVVDCP 253
Cdd:CHL00175   91 KRWKNLSLLAISKNRQRYNV-TRKNMN----------MLVDSLKNRG--YDYILIDCP 135
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 126-254 1.12e-04

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: 43.49  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSalHGFQPELDRNPSLYDairydderksiadvilpTNFPGLDIVP 205
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLS--DSFNQKFGHEPTKVK-----------------ENLSAMEIDP 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584016544 206 aNLELQEY-----EYDTP----------LAMQA----GADGKRFFTRLGKSLEEVDirYDVVVVDCPP 254
Cdd:pfam02374  70 -NMELEEYwqevqKYMNAllglrmlegiLAEELaslpGIDEAASFDEFKKYMDEGE--YDVVVFDTAP 134
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 126-193 1.16e-04

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: 43.27  E-value: 1.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQA-SLSALHGFQPEldrnPSLYDAIRYDDERKSIADVI 193
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKAdSTRLLLGGKAI----PTVLDTLREKGEVEELEDVI 72
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
126-206 1.50e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 43.20  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSA--LHGFQpeldrNPSLYDAIRyddERKSIADV----ILPTNFP 199
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRllLGGKL-----QPTVLDTAR---EKGYVEDVevedVVYKGYG 79


                  ....*..
gi 1584016544 200 GLDIVPA 206
Cdd:pfam00142  80 GVKCVES 86
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 118-256 1.71e-04

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 43.94  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQAslSALHG-FQPelDRNPSLYDAIRYDderKSIADVILPT 196
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRK--GGLHQmFGK--APKPGLLDLLAGE---ASIEAGIHRD 626

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584016544 197 NFPGLDIVPA-NLELQEYEYDTPLAMqagadgkrffTRLGKSLEEVDIRYDVVVVDCPPQL 256
Cdd:TIGR01005 627 QRPGLAFIAAgGASHFPHNPNELLAN----------PAMAELIDNARNAFDLVLVDLAALA 677
MerR_1 pfam13411
MerR HTH family regulatory protein;
46-94 2.35e-04

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 39.08  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1584016544  46 FSLAEVAHYLGVTPSNLKrlYLDGKGP-TPITMSGNRRYYTAEQMLELRF 94
Cdd:pfam13411   1 YTISELARLLGVTPRTLR--YWEREGLlPPPRTERGRRYYTDEDVERLRL 48
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 126-157 3.92e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 41.87  E-value: 3.92e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQ 157
Cdd:PRK13185   10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 126-170 4.44e-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: 4.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLS-ALHGFQPEL 170
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSvTLTGSLNNL 374
PRK10818 PRK10818
septum site-determining protein MinD;
118-345 4.44e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 41.85  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 118 QVVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLD-PQASLSALHGFQPELdrnpsLYDAIRYDDERKSIAD-VILP 195
Cdd:PRK10818    3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRV-----VYDFVNVIQGDATLNQaLIKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 196 TNFPGLDIVPANlelQEYEYDTplamqagadgkrfFTRLG--KSLEEVD-IRYDVVVVDCPPQLGYLTLTALTAATSVLI 272
Cdd:PRK10818   78 KRTENLYILPAS---QTRDKDA-------------LTREGvaKVLDDLKaMDFEFIVCDSPAGIETGALMALYFADEAII 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1584016544 273 TVHPQMLDLMSMSQFLLMLGNITKTIKKAGANVRMdwlRYLITRFEPTDVPQVQMLGfMQSMFaeEILKSPMV 345
Cdd:PRK10818  142 TTNPEVSSVRDSDRILGILASKSRRAENGEEPIKE---HLLLTRYNPGRVSRGDMLS-MEDVL--EILRIKLV 208
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 119-254 1.23e-03

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: 40.13  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDpqaslsaLHGF-QPEL----DRNPslydaiRYDDERksiadvI 193
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD-------IYGPsIPRMlgleGERP------EQSDGG------I 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1584016544 194 LPTNFPGLDIVPANLeLQEYEyDTPLA----MQAGAdgkrfftrLGKSLEEVDIRY-DVVVVDCPP 254
Cdd:pfam10609  66 IPVEAHGIKVMSIGF-LLPDE-DDAVIwrgpMKSGA--------IKQFLTDVDWGElDYLIIDLPP 121
HTH_MerR-SF cd04761
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 46-94 1.25e-03

Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


Pssm-ID: 133389 [Multi-domain]  Cd Length: 49  Bit Score: 36.42  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1584016544  46 FSLAEVAHYLGVTPSNLkRLYLDGKGPTPITMSGNRRYYTAEQMLELRF 94
Cdd:cd04761     1 YTIGELAKLTGVSPSTL-RYYERIGLLSPARTEGGYRLYSDADLERLRL 48
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 103-163 1.28e-03

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: 40.59  E-value: 1.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584016544 103 EAKRYVPHRKPGDKLQVVAVVNfKGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQASLSAL 163
Cdd:cd02033    17 EPSLEIPTGPPTKETQIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSL 76
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 126-157 1.63e-03

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: 39.97  E-value: 1.63e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQ 157
Cdd:cd02032     8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPK 39
AlpA COG3311
DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];
47-87 1.74e-03

DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];


Pssm-ID: 442540 [Multi-domain]  Cd Length: 64  Bit Score: 36.45  E-value: 1.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1584016544  47 SLAEVAHYLGVTPSNLKRLYLDGKGPTPITMSGNRRYYTAE 87
Cdd:COG3311    10 RLKEVAELLGVSRSTIYRLIKKGEFPKPVKLGGRSVRWRES 50
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
 119-156 2.84e-03

helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.


Pssm-ID: 274798 [Multi-domain]  Cd Length: 322  Bit Score: 39.24  E-value: 2.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1584016544 119 VVAVVNFKGGSGKTTTTAHLAQHLALTGHRVLAIDLDP 156
Cdd:TIGR03815  95 VVAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADP 132
Ffh COG0541
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ...
 128-157 4.16e-03

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


Pssm-ID: 440307 [Multi-domain]  Cd Length: 423  Bit Score: 39.23  E-value: 4.16e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1584016544 128 GSGKTTTTAHLAQHLALTGHRVLAIDLDPQ 157
Cdd:COG0541   110 GSGKTTTAAKLAKYLKKKGKKPLLVAADVY 139
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
 109-150 5.56e-03

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 38.54  E-value: 5.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1584016544 109 PHRKPGDKLQVVAV--VNfkgGSGKTTTTAHLAQHLALTGHRVL 150
Cdd:PRK10416  106 PLNIEEKKPFVILVvgVN---GVGKTTTIGKLAHKYKAQGKKVL 146
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 126-193 9.98e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 37.44  E-value: 9.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584016544 126 KGGSGKTTTTAHLAQHLALTGHRVLAIDLDPQA-SLSALHGfqpelDRNPSLYDAIRYDD-ERKSIADVI 193
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKAdCTRNLVG-----EKIPTVLDVLREKGiDNLGLEDII 73
 
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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