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Conserved domains on  [gi|11466429|ref|NP_038435|]
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septum-site determining protein (chloroplast) [Mesostigma viride]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
minD CHL00175
septum-site determining protein; Validated
 3-283 0e+00

septum-site determining protein; Validated


:

Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 503.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    3 EQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGE 82
Cdd:CHL00175   1 EQITTEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   83 CCLDQALIRDKRWSNLALLAISKTRQRYHLTRRNMEMLVDSIRLRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEI 162
Cdd:CHL00175  81 CRLDQALIRDKRWKNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  163 TSIRDADRVAGLLEASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTL 242
Cdd:CHL00175 161 TAIRDADRVAGLLEANGIYNVKLLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 11466429  243 SGISFENAARRLVGRKEYLVNLETGNKGLLKRVQQFLTGSE 283
Cdd:CHL00175 241 SGIAFENAARRLVGKQDYFIDLDSPSKGPLKRLQKFFLGSS 281
 
Name Accession Description Interval E-value
minD CHL00175
septum-site determining protein; Validated
 3-283 0e+00

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 503.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    3 EQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGE 82
Cdd:CHL00175   1 EQITTEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   83 CCLDQALIRDKRWSNLALLAISKTRQRYHLTRRNMEMLVDSIRLRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEI 162
Cdd:CHL00175  81 CRLDQALIRDKRWKNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  163 TSIRDADRVAGLLEASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTL 242
Cdd:CHL00175 161 TAIRDADRVAGLLEANGIYNVKLLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 11466429  243 SGISFENAARRLVGRKEYLVNLETGNKGLLKRVQQFLTGSE 283
Cdd:CHL00175 241 SGIAFENAARRLVGKQDYFIDLDSPSKGPLKRLQKFFLGSS 281
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 18-279 1.22e-130

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: 370.90  E-value: 1.22e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWSN 97
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    98 LALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEA 177
Cdd:TIGR01968  82 LYLLPASQTRDKDAVTPEQMKKLVNELK-EEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   178 SGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKlTLSGISFENAARRLVGR 257
Cdd:TIGR01968 161 KGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDK-SRAGKAFENIARRILGE 239

                         250       260
                  ....*....|....*....|..
gi 11466429   258 KEYLVNLETGNKGLLKRVQQFL 279
Cdd:TIGR01968 240 EVPFEDLTTQKKGFFARIKRFF 261
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 17-275 8.26e-122

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 348.59  E-value: 8.26e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  17 TRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWS 96
Cdd:COG2894   2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRFE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  97 NLALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLE 176
Cdd:COG2894  82 NLYLLPASQTRDKDALTPEQMKKLVEELK-EEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLLE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 177 ASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKlTLSGISFENAARRLVG 256
Cdd:COG2894 161 AKGIRKPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEK-SKAGQAYRNIARRLLG 239

                       250
                ....*....|....*....
gi 11466429 257 RKEYLVNLETGNKGLLKRV 275
Cdd:COG2894 240 EEVPLRDLEEEKKGFFSRL 258
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 18-254 4.69e-121

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: 345.73  E-value: 4.69e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWSN 97
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  98 LALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEA 177
Cdd:cd02036  81 LYLLPASQTRDKDALTPEKLEELVKELK-DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11466429 178 SGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTLSGISFENAARRL 254
Cdd:cd02036 160 KGIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 20-234 1.58e-39

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 137.86  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVI--YTAMEVFEGECCLDQALIRDKRWS- 96
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPalQALAEGLKGRVNLDPILLKEKSDEg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    97 NLALL----AISKTRQRYHLTRRNmEMLVDSIRL--RNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADR 170
Cdd:pfam01656  81 GLDLIpgniDLEKFEKELLGPRKE-ERLREALEAlkEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11466429   171 VAGLLEASGIYEVKL-------LVNRVRPDMIQKNDMLSVRdvQEMLGIPLLGAIPEDTNVIVSTNRGQPL 234
Cdd:pfam01656 160 LGGVIAALVGGYALLglkiigvVLNKVDGDNHGKLLKEALE--ELLRGLPVLGVIPRDEAVAEAPARGLPV 228
ParA_partition NF041546
ParA family partition ATPase;
19-217 2.78e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 64.11  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   19 TIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADvglrnldlllglenrviytamevfegecclDQALIRDkrWSNL 98
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD------------------------------PQGSALD--WAAA 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   99 ----ALLAISKtrqryhLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGL 174
Cdd:NF041546  49 redeRPFPVVG------LARPTLHRELPSLA-RDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDL 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 11466429  175 LEASGIY----EVKLLVNRVRPdmiqkNDMLSvRDVQEML---GIPLLGA 217
Cdd:NF041546 122 IKEAREYtpglKAAFVLNRAIA-----RTALG-REVAEALaeyGLPVLKT 165
 
Name Accession Description Interval E-value
minD CHL00175
septum-site determining protein; Validated
 3-283 0e+00

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 503.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    3 EQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGE 82
Cdd:CHL00175   1 EQITTEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   83 CCLDQALIRDKRWSNLALLAISKTRQRYHLTRRNMEMLVDSIRLRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEI 162
Cdd:CHL00175  81 CRLDQALIRDKRWKNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  163 TSIRDADRVAGLLEASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTL 242
Cdd:CHL00175 161 TAIRDADRVAGLLEANGIYNVKLLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 11466429  243 SGISFENAARRLVGRKEYLVNLETGNKGLLKRVQQFLTGSE 283
Cdd:CHL00175 241 SGIAFENAARRLVGKQDYFIDLDSPSKGPLKRLQKFFLGSS 281
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 18-279 1.22e-130

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: 370.90  E-value: 1.22e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWSN 97
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    98 LALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEA 177
Cdd:TIGR01968  82 LYLLPASQTRDKDAVTPEQMKKLVNELK-EEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   178 SGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKlTLSGISFENAARRLVGR 257
Cdd:TIGR01968 161 KGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDK-SRAGKAFENIARRILGE 239

                         250       260
                  ....*....|....*....|..
gi 11466429   258 KEYLVNLETGNKGLLKRVQQFL 279
Cdd:TIGR01968 240 EVPFEDLTTQKKGFFARIKRFF 261
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 17-275 8.26e-122

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 348.59  E-value: 8.26e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  17 TRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWS 96
Cdd:COG2894   2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRFE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  97 NLALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLE 176
Cdd:COG2894  82 NLYLLPASQTRDKDALTPEQMKKLVEELK-EEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLLE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 177 ASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKlTLSGISFENAARRLVG 256
Cdd:COG2894 161 AKGIRKPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEK-SKAGQAYRNIARRLLG 239

                       250
                ....*....|....*....
gi 11466429 257 RKEYLVNLETGNKGLLKRV 275
Cdd:COG2894 240 EEVPLRDLEEEKKGFFSRL 258
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 18-254 4.69e-121

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: 345.73  E-value: 4.69e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWSN 97
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  98 LALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEA 177
Cdd:cd02036  81 LYLLPASQTRDKDALTPEKLEELVKELK-DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11466429 178 SGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTLSGISFENAARRL 254
Cdd:cd02036 160 KGIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIARRL 236
PRK10818 PRK10818
septum site-determining protein MinD;
18-275 6.69e-66

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 207.10  E-value: 6.69e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWSN 97
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTEN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   98 LALLAISKTRQRYHLTRRNMEMLVDSIRLRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEA 177
Cdd:PRK10818  83 LYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  178 ------SGIYEVK--LLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKlTLSGISFEN 249
Cdd:PRK10818 163 ksrraeNGEEPIKehLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIE-ADAGKAYAD 241

                        250       260
                 ....*....|....*....|....*.
gi 11466429  250 AARRLVGRKEYLVNLETGNKGLLKRV 275
Cdd:PRK10818 242 TVDRLLGEERPFRFIEEEKKGFLKRL 267
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 20-234 1.58e-39

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 137.86  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVI--YTAMEVFEGECCLDQALIRDKRWS- 96
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPalQALAEGLKGRVNLDPILLKEKSDEg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    97 NLALL----AISKTRQRYHLTRRNmEMLVDSIRL--RNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADR 170
Cdd:pfam01656  81 GLDLIpgniDLEKFEKELLGPRKE-ERLREALEAlkEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11466429   171 VAGLLEASGIYEVKL-------LVNRVRPDMIQKNDMLSVRdvQEMLGIPLLGAIPEDTNVIVSTNRGQPL 234
Cdd:pfam01656 160 LGGVIAALVGGYALLglkiigvVLNKVDGDNHGKLLKEALE--ELLRGLPVLGVIPRDEAVAEAPARGLPV 228
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 18-258 1.91e-38

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: 135.63  E-value: 1.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIyTAMEVFEGECCLDQALIRDKRWSN 97
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPV-TLHDVLAGEADIKDAIYEGPFGVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    98 LALLAISKTrqryHLTRRNMEMLVDSIR--LRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLL 175
Cdd:TIGR01969  80 VIPAGVSLE----GLRKADPDKLEDVLKeiIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKTKIVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   176 EASGIYEVKLLVNRVRPDmiqKNDMlSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTLSGISFENAARRLV 255
Cdd:TIGR01969 156 EKLGTAILGVVLNRVTRD---KTEL-GREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELAAELA 231


                  ...
gi 11466429   256 GRK 258
Cdd:TIGR01969 232 GIE 234
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 1-275 3.62e-35

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: 129.85  E-value: 3.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   1 MIEQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARL-GYKVALIDADVGLRNLDLLLGLENRviYTAMEVF 79
Cdd:COG4963  86 LRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPR--RGLADAL 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  80 EGECCLDQALIRD---KRWSNLALLAISKTRQR-YHLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAV 155
Cdd:COG4963 164 RNPDRLDETLLDRaltRHSSGLSVLAAPADLERaEEVSPEAVERLLDLLR-RHFDYVVVDLPRGLNPWTLAALEAADEVV 242

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 156 VVTTPEITSIRDADRVAGLLEASGIYE--VKLLVNRVrpdmiQKNDMLSVRDVQEMLGIPLLGAIPEDT-NVIVSTNRGQ 232
Cdd:COG4963 243 LVTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLNRV-----PKRGEISAKDIEEALGLPVAAVLPNDPkAVAEAANQGR 317

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 11466429 233 PLVLNKKLTLSGISFENAARRLVGRKEylVNLETGNKGLLKRV 275
Cdd:COG4963 318 PLAEVAPKSPLAKAIRKLAARLTGRPA--AAAAKAGGKLLKRL 358
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 33-258 3.91e-34

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: 123.85  E-value: 3.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  33 TTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRviYTAMEVFEGECCLDQALIRDKrwSNLALL-AISKTRQRYH 111
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK--ATLADVLAGEADLEDAIVQGP--GGLDVLpGGSGPAELAE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 112 LTRrnMEMLVDSIRL--RNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLE-ASGIYEVKLLVN 188
Cdd:COG0455  77 LDP--EERLIRVLEEleRFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRrRLGVRRAGVVVN 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11466429 189 RVRP--DMIQKNDMLSvRDVQEMLGI--PLLGAIPEDTNVIVSTNRGQPLVLNKKLTLSGISFENAARRLVGRK 258
Cdd:COG0455 155 RVRSeaEARDVFERLE-QVAERFLGVrlRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWP 227
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 18-239 5.13e-33

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: 120.75  E-value: 5.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRviYTAMEVFEGECCLDQALIRDKrwSN 97
Cdd:cd02038   1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK--KTLGDVLKGRVSLEDIIVEGP--EG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  98 LALL-AISKTRQRYHLTRRNMEMLVDSIR--LRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGL 174
Cdd:cd02038  77 LDIIpGGSGMEELANLDPEQKAKLIEELSslESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 175 LEASGI-YEVKLLVNRVR--PDMIQKNDMLSvRDVQEMLGIPL--LGAIPEDTNVIVSTNRGQPLVLNKK 239
Cdd:cd02038 157 LSRRGGkKNFRLIVNMARspKEGRATFERLK-KVAKRFLDINLdfVGFIPYDQSVRRAVRSQKPFVLLFP 225
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 17-257 3.02e-28

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: 108.79  E-value: 3.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  17 TRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD--------VGlrnldlllGLENRVIYTAMEVFEGECCLDQA 88
Cdd:COG1192   1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDpqgnltsgLG--------LDPDDLDPTLYDLLLDDAPLEDA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  89 lIRDKRWSNLALLA-----------ISKTRQRYHLTRRNMEMLVDsirlrNYNFILIDCPAGIDVGFVNAVAPAEEAVVV 157
Cdd:COG1192  73 -IVPTEIPGLDLIPanidlagaeieLVSRPGRELRLKRALAPLAD-----DYDYILIDCPPSLGLLTLNALAAADSVLIP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 158 TTPEITSIRDADRVAGLLEA------SGIYEVKLLVNRVRPDMIQKNDMlsVRDVQEMLGIPLLGA-IPEDTNVIVSTNR 230
Cdd:COG1192 147 VQPEYLSLEGLAQLLETIEEvredlnPKLEILGILLTMVDPRTRLSREV--LEELREEFGDKVLDTvIPRSVALAEAPSA 224

                       250       260
                ....*....|....*....|....*..
gi 11466429 231 GQPLVLNKKLTLSGISFENAARRLVGR 257
Cdd:COG1192 225 GKPVFEYDPKSKGAKAYRALAEELLER 251
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 8-193 5.51e-25

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: 101.03  E-value: 5.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   8 DGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRViyTAMEVFEGECCLDQ 87
Cdd:COG0489  83 LLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP--GLSDVLAGEASLED 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  88 ALIRDKRwSNLALLAISKTRQRY--HLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAP-AEEAVVVTTPEITS 164
Cdd:COG0489 161 VIQPTEV-EGLDVLPAGPLPPNPseLLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASlVDGVLLVVRPGKTA 238

                       170       180       190
                ....*....|....*....|....*....|..
gi 11466429 165 IRDADRVAGLLEASGiyeVKLL---VNRVRPD 193
Cdd:COG0489 239 LDDVRKALEMLEKAG---VPVLgvvLNMVCPK 267
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 18-236 3.25e-21

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: 89.64  E-value: 3.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIA-RLGYKVALIDADVGLRNLDLLLGLENRviYTAMEVFEGECCLDQALIRD---K 93
Cdd:cd03111   1 RVVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDLPFGDLGLYLNLRPD--YDLADVIQNLDRLDRTLLDSavtR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  94 RWSNLALLAiskTRQRYHLTRRNMEMLVDSI--RLRN-YNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADR 170
Cdd:cd03111  79 HSSGLSLLP---APQELEDLEALGAEQVDKLlqVLRAfYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARR 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11466429 171 VAGLLEASGIYE--VKLLVNRVRpdmiqKNDMLSVRDVQEMLGIPLLGAIPEDTN-VIVSTNRGQPLVL 236
Cdd:cd03111 156 LLDSLRELEGSSdrLRLVLNRYD-----KKSEISPKDIEEALGLEVFATLPNDYKaVSESANTGRPLVE 219
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 17-255 3.38e-18

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: 81.73  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    17 TRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADvglrnldlllglenrvIY-----TAMEVfEGEccldQALIR 91
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD----------------IYgpsipRMLGL-EGE----RPEQS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    92 DKRW---SNLALLAISktrqryhltrrnMEMLVDS---------------IR--LRNYN-----FILIDCPAGI-DV--G 143
Cdd:pfam10609  62 DGGIipvEAHGIKVMS------------IGFLLPDeddaviwrgpmksgaIKqfLTDVDwgeldYLIIDLPPGTgDEqlT 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   144 FVNAVaPAEEAVVVTTPEITSIRDADR-----------VAGLLE-ASGIyevkllvnrVRPDMIQKNDMLS---VRDVQE 208
Cdd:pfam10609 130 LAQLL-PLTGAVIVTTPQDVALLDVRKaidmfkkvnvpVLGVVEnMSYF---------VCPHCGEETYIFGkggGEKLAE 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 11466429   209 MLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTLSGISFENAARRLV 255
Cdd:pfam10609 200 ELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 19-235 1.65e-17

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 79.83  E-value: 1.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  19 TIVITsGKGGVGKTTTTANLGMSIARLGYKVALIDAD--------VGLRNLDLLLG--------LENRVIYTAMEVFE-- 80
Cdd:COG3640   2 KIAVA-GKGGVGKTTLSALLARYLAEKGKPVLAVDADpnanlaeaLGLEVEADLIKplgemrelIKERTGAPGGGMFKln 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  81 --GECCLDQALIRDKrwsNLALLAISKTRQR------YH--LTRRnmemLVDSIRLRNYNFILIDCPAGID------VGF 144
Cdd:COG3640  81 pkVDDIPEEYLVEGD---GVDLLVMGTIEEGgsgcycPEnaLLRA----LLNHLVLGNYEYVVVDMEAGIEhlgrgtAEG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 145 VNAVapaeeaVVVTTPEITSIRDADRVAGLLEASGIYEVKLLVNRVRPDMiqkndmlSVRDVQEMLGIPLLGAIPEDTNV 224
Cdd:COG3640 154 VDLL------LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEE-------DEEFLRELLGLELLGFIPYDEEV 220

                       250
                ....*....|.
gi 11466429 225 IVSTNRGQPLV 235
Cdd:COG3640 221 READLEGKPLL 231
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 18-180 1.05e-16

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: 76.07  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRViyTAMEVFEGECCLDQALIRDKRwSN 97
Cdd:cd05387  20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEP--GLSEVLSGQASLEDVIQSTNI-PN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  98 LALLA---ISKTRQRYhLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVV-VTTPEITSIRDADRVAG 173
Cdd:cd05387  97 LDVLPagtVPPNPSEL-LSSPRFAELLEELK-EQYDYVIIDTPPVLAVADALILAPLVDGVLlVVRAGKTRRREVKEALE 174


                ....*..
gi 11466429 174 LLEASGI 180
Cdd:cd05387 175 RLEQAGA 181
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 18-201 1.94e-15

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: 71.03  E-value: 1.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADvglrnldlllglenrviytamevfegecclDQAlirdkrwsN 97
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD------------------------------PQG--------S 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  98 LALLAisktrqryhltrrnmemlvdsirlrnYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEA 177
Cdd:cd02042  43 LTSWL--------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEE 96

                       170       180       190
                ....*....|....*....|....*....|
gi 11466429 178 SGIY------EVKLLVNRVRPDMIQKNDML 201
Cdd:cd02042  97 LKKQlnppllILGILLTRVDPRTKLAREVL 126
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 17-166 6.24e-15

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: 71.08  E-value: 6.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    17 TRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKrWS 96
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTV-IE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    97 NLALLA------------ISKTRQRYHLTRrnmemLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITS 164
Cdd:pfam13614  80 NLDLIPsnidlagaeielIGIENRENILKE-----ALEPVK-DNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153


                  ..
gi 11466429   165 IR 166
Cdd:pfam13614 154 LE 155
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 18-221 8.44e-14

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: 68.68  E-value: 8.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVF-----EGECCL------- 85
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIvpvevGGIKVMsigfllp 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  86 -DQALIrdkrWSNLALLAISKtrqryhltrrnmEMLVDSIrLRNYNFILIDCPAG---IDVGFVNAVAPAeEAVVVTTPE 161
Cdd:cd02037  81 eDDAVI----WRGPMKSGAIK------------QFLKDVD-WGELDYLIIDLPPGtgdEHLSLVQLIPID-GAVVVTTPQ 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11466429 162 ITSIRDADRVAGLLEASGIYEVKLLVN---RVRPDMIQKNDMLSVRDVQEM---LGIPLLGAIPED 221
Cdd:cd02037 143 EVSLIDVRKAIDMCKKLNIPVLGIVENmsgFVCPHCGKKIYIFGKGGGEKLaeeLGVPFLGKIPLD 208
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 20-219 1.32e-13

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 68.95  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  20 IVITSGKGGVGKTTTTANLgmsiARLGYKVALIDADVGL------RNLDLLLGLENRVIYTA------------------ 75
Cdd:cd03110   2 IAVLSGKGGTGKTTITANL----AVLLYNVILVDCDVDApnlhllLGPEPEEEEDFVGGKKAfidqekcircgncervck 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  76 ----------MEVFEGEC---------CLDQALIRDKRWSNLALLAISK----TRQRYHLTRRNMEMLVDSIR------L 126
Cdd:cd03110  78 fgaileffqkLIVDESLCegcgacviiCPRGAIYLKDRDTGKIFISSSDggplVHGRLNIGEENSGKLVTELRkkalerS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 127 RNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEASGIyEVKLLVNRvrpDMIQKNDMLSVRDV 206
Cdd:cd03110 158 KECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAIELAKHFGI-PTGIVINR---YDINDEISEEIEDF 233

                       250
                ....*....|...
gi 11466429 207 QEMLGIPLLGAIP 219
Cdd:cd03110 234 ADEEGIPLLGKIP 246
ParA_partition NF041546
ParA family partition ATPase;
19-217 2.78e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 64.11  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   19 TIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADvglrnldlllglenrviytamevfegecclDQALIRDkrWSNL 98
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD------------------------------PQGSALD--WAAA 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   99 ----ALLAISKtrqryhLTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGL 174
Cdd:NF041546  49 redeRPFPVVG------LARPTLHRELPSLA-RDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDL 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 11466429  175 LEASGIY----EVKLLVNRVRPdmiqkNDMLSvRDVQEML---GIPLLGA 217
Cdd:NF041546 122 IKEAREYtpglKAAFVLNRAIA-----RTALG-REVAEALaeyGLPVLKT 165
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 20-236 6.78e-11

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: 61.17  E-value: 6.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  20 IVITsGKGGVGKTTTTANLGMSIARLGYKVALIDAD-------------VGLRNLDLLLGLENRV---IYTAMEVFEG-- 81
Cdd:cd02034   3 IAVA-GKGGVGKTTIAALLIRYLAKKGGKVLAVDADpnsnlaetlgvevEKLPLIKTIGDIRERTgakKGEPPEGMSLnp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  82 --ECCLDQALIRDKrwsNLALLAISKTRQRY--------HLTRRnmemLVDSIRLRNYNFILIDCPAGIDV---GFVNAV 148
Cdd:cd02034  82 yvDDIIKEIIVEPD---GIDLLVMGRPEGGGsgcycpvnALLRE----LLRHLALKNYEYVVIDMEAGIEHlsrGTIRAV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 149 apaEEAVVVTTPEITSIRDADRVAGLLEASGIYEVKLLVNRVR-PDMIQKNDmlsvrdvQEMLGIPLLGAIPEDTNVIVS 227
Cdd:cd02034 155 ---DLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRnEEEQELIE-------ELLIKLKLIGVIPYDEEIMEA 224


                ....*....
gi 11466429 228 TNRGQPLVL 236
Cdd:cd02034 225 DLKGKPLFD 233
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 16-179 2.99e-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: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    16 DTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRvIYTAMEVFEGECCLDQAlIRDKRW 95
Cdd:TIGR01007  16 EIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNK-ITGLTNFLSGTTDLSDA-ICDTNI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    96 SNLALLAISKT--RQRYHLTRRNMEMLVDSIRLRnYNFILIDCPAgidvgfVNAVAPA-------EEAVVVTTPEITSIR 166
Cdd:TIGR01007  94 ENLDVITAGPVppNPTELLQSSNFKTLIETLRKR-FDYIIIDTPP------IGTVTDAaiiaracDASILVTDAGKIKKR 166

                         170
                  ....*....|...
gi 11466429   167 DADRVAGLLEASG 179
Cdd:TIGR01007 167 EVKKAKEQLEQAG 179
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 18-55 1.02e-09

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: 54.74  E-value: 1.02e-09
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 11466429  18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:cd01983   1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 19-235 3.34e-09

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: 56.20  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    19 TIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD------------------------VGLRNLDLLLGLENRVIYT 74
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDpqnllrlhfgmdwsvrdgwarallNGADWAAAAYRSPDGVLFL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    75 AmevfEGECCLDQALIR---DKRWSNlALLAISktrqryhltRRNMEMLVdsirlrnynfiLIDCPAGIDVGFVNAVAPA 151
Cdd:TIGR03371  83 P----YGDLSADEREAYqahDAGWLA-RLLQQL---------DLAARDWV-----------LIDLPRGPSPITRQALAAA 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   152 EEAVVVTTPEITS-IRDADRVAGLLEASGI-YEVKLLVNRVRPDMIQKNDMLSVrdVQEMLGIPLL-GAIPEDTNVIVST 228
Cdd:TIGR03371 138 DLVLVVVNADAACyATLHQLALALFAGSGPrDGPRFLINQFDPARQLSRDVRAV--LRQTLGSRLLpFVIHRDEAVSEAL 215


                  ....*..
gi 11466429   229 NRGQPLV 235
Cdd:TIGR03371 216 ARGTPVL 222
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 20-208 4.19e-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: 52.90  E-value: 4.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALI---------DA-DVGLRNLDLLLGLENrviYTAMEvfegeccLDQAL 89
Cdd:cd02035   2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVstdpahslsDAfGQKLGGETPVKGAPN---LWAME-------IDPEE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  90 IRDKRWSNLALLAISKTRQRyHLTRRNMEML---------------VDSIRLRNYNFILIDC-PAG-----IDVGFVNAV 148
Cdd:cd02035  72 ALEEYWEEVKELLAQYLRLP-GLDEVYAEELlslpgmdeaaafdelREYVESGEYDVIVFDTaPTGhtlrlLSLPLEQVR 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11466429 149 A----PAE-EAVVVTTPEITSIRDADRVAGLLEASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQE 208
Cdd:cd02035 151 EllrdPERtTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFFLRRRRQQQ 215
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
20-56 4.88e-08

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 53.51  E-value: 4.88e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 11466429   20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADV 56
Cdd:PRK11670 110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 15-159 6.91e-07

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: 50.49  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    15 TDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRViyTAMEVFEGECCLDQALIRDKR 94
Cdd:TIGR01005 551 AENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKP--GLLDLLAGEASIEAGIHRDQR 628

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    95 wSNLALLAISKTRQRYH-----LTRRNMEMLVDSIRlRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTT 159
Cdd:TIGR01005 629 -PGLAFIAAGGASHFPHnpnelLANPAMAELIDNAR-NAFDLVLVDLAALAAVADAAAFAALADGILFVT 696
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
16-52 5.07e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 47.12  E-value: 5.07e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 11466429  16 DTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALI 52
Cdd:COG0003   1 DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLV 37
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 18-259 1.03e-05

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: 45.82  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  18 RTIVITsGKGGVGKTTTTANLGMSIARLGYKVALIDADvgLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRD--KRW 95
Cdd:cd02117   1 ESIVVY-GKGGIGKSTTASNLSAALAEGGKKVLHVGCD--PKHDSTLLLTGGKVPPTIDEMLTEDGTAEELRREDllFSG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429  96 SN---------------LALLAISKTRQryhLTRRNMEMLVDsirlrnYNFILIDCPAgiDV---GFvnaVAP-----AE 152
Cdd:cd02117  78 FNgvdcveaggpepgvgCGGRGIGTMLE---LLEEHGLLDDD------YDVVIFDVLG--DVvcgGF---AAPlrrgfAQ 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429 153 EAVVVTTPEITSIRDADRVAGLLEA---SGIYEVKLLVNRVRPDmiqknDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTN 229
Cdd:cd02117 144 KVVIVVSEELMSLYAANNIVKAVENyskNGVRLAGLVANLRDPA-----GTEEIQAFAAAVGTKILAVIPRDPAVRRAEL 218

                       250       260       270
                ....*....|....*....|....*....|
gi 11466429 230 RGQPLVLNKKLTLSGISFENAARRLVGRKE 259
Cdd:cd02117 219 ARVTVFEHDPVSPAASEFARLAAKIADAVP 248
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-165 1.03e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 46.21  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    3 EQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLD------LLLGLENRVIYTAM 76
Cdd:PRK13869 107 ESIDFVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSAllgvlpETDVGANETLYAAI 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429   77 EVFEGECCLDQaLIRDKRWSNLALL---------------AISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAGID 141
Cdd:PRK13869 187 RYDDTRRPLRD-VIRPTYFDGLHLVpgnlelmefehttpkALSDKGTRDGLFFTRVAQAFDEVA-DDYDVVVIDCPPQLG 264

                        170       180
                 ....*....|....*....|....
gi 11466429  142 VGFVNAVAPAEEAVVVTTPEITSI 165
Cdd:PRK13869 265 FLTLSGLCAATSMVITVHPQMLDI 288
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 19-55 4.29e-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: 44.26  E-value: 4.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 11466429    19 TIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:pfam02374   2 RWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 25-55 4.47e-05

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: 43.83  E-value: 4.47e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 11466429  25 GKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:cd02032   7 GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCD 37
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 1-55 4.62e-05

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: 44.69  E-value: 4.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11466429     1 MIEQINKDGEKknstdtrtIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:TIGR04291 312 LIDEIAKSEKG--------LIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 25-55 1.43e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.26  E-value: 1.43e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 11466429   25 GKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCD 39
PHA02518 PHA02518
ParA-like protein; Provisional
 20-55 4.26e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.60  E-value: 4.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 11466429   20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD 38
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 25-55 9.35e-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: 39.80  E-value: 9.35e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 11466429  25 GKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:cd02040   7 GKGGIGKSTTASNLSAALAEMGKKVLHVGCD 37
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 18-139 9.87e-04

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: 39.74  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11466429    18 RTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADvgLRNLDLLLGLENRVIY---TAMEVFEGECcldqalirdkr 94
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLD--LRQRTFHRYFENRSATadrTGLSLPTPEH----------- 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 11466429    95 wSNLALLAISKTRQRYHLTRRNMEMLVDSIRlRNYNFILIDCPAG 139
Cdd:pfam09140  68 -LNLPDNDVAEVPDGENIDDARLEEAFADLE-ARCDFIVIDTPGS 110
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 20-55 1.05e-03

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: 39.96  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 11466429    20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLD 142
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
25-55 1.15e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 39.73  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 11466429    25 GKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCD 37
chlL CHL00072
photochlorophyllide reductase subunit L
 25-55 2.32e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.95  E-value: 2.32e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 11466429   25 GKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCD 37
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 14-55 5.34e-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: 37.89  E-value: 5.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 11466429  14 STDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDAD 55
Cdd:cd02033  27 PTKETQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCD 68
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 20-56 9.04e-03

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 36.58  E-value: 9.04e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 11466429  20 IVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADV 56
Cdd:cd03115   2 VILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADT 38
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 1-56 9.41e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 37.11  E-value: 9.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 11466429    1 MIEQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADV 56
Cdd:PRK00771  78 LVKLLGEETEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADT 133
 
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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