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Conserved domains on  [gi|31711804|gb|AAP68258|]
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At5g24020 [Arabidopsis thaliana]

Protein Classification

septum site-determining protein MinD( domain architecture ID 10114125)

septum site-determining protein MinD, one of the three protein products of the min operon, is a membrane ATPase required for proper placement of the cell division site at the midcell position through the activation and regulation of MinC and MinE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 59-300 1.98e-120

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: 1.98e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 139 FELLCISKPRSKlpMGFGGKALEWLVDALKtrpeGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:cd02036  81 LYLLPASQTRDK--DALTPEKLEELVKELK----DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVI 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 219 GLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAW 298
Cdd:cd02036 155 GLLESKGIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIAR 234


                ..
gi 31711804 299 RL 300
Cdd:cd02036 235 RL 236
 
Name Accession Description Interval E-value
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 59-300 1.98e-120

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: 1.98e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 139 FELLCISKPRSKlpMGFGGKALEWLVDALKtrpeGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:cd02036  81 LYLLPASQTRDK--DALTPEKLEELVKELK----DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVI 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 219 GLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAW 298
Cdd:cd02036 155 GLLESKGIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIAR 234


                ..
gi 31711804 299 RL 300
Cdd:cd02036 235 RL 236
minD CHL00175
septum-site determining protein; Validated
 57-303 8.78e-117

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 338.28  E-value: 8.78e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   57 TPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRW 136
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRDKRW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  137 SNFELLCISKPRSKLPMGfgGKALEWLVDALKTRpegSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADR 216
Cdd:CHL00175  94 KNLSLLAISKNRQRYNVT--RKNMNMLVDSLKNR---GYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADR 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  217 VTGLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQA 296
Cdd:CHL00175 169 VAGLLEANGIYNVKLLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFENA 248


                 ....*..
gi 31711804  297 AWRLVEQ 303
Cdd:CHL00175 249 ARRLVGK 255
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 59-324 2.34e-98

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 290.81  E-value: 2.34e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:COG2894   3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRFEN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 139 FELLCISKPRSKlpmgfggKAL-----EWLVDALKTRPegspDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRD 213
Cdd:COG2894  83 LYLLPASQTRDK-------DALtpeqmKKLVEELKEEF----DYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 214 ADRVTGLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNkPPTLAGLAF 293
Cdd:COG2894 152 ADRIIGLLEAKGIRKPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLD-EKSKAGQAY 230

                       250       260       270
                ....*....|....*....|....*....|.
gi 31711804 294 EQAAWRLVEQDSmkaVMVEEEPKKRGFFSFF 324
Cdd:COG2894 231 RNIARRLLGEEV---PLRDLEEEKKGFFSRL 258
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 59-322 8.69e-98

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: 289.24  E-value: 8.69e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   139 FELLCISKPRSKLPMGfgGKALEWLVDALKTRPegspDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:TIGR01968  82 LYLLPASQTRDKDAVT--PEQMKKLVNELKEEF----DYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   219 GLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKpPTLAGLAFEQAAW 298
Cdd:TIGR01968 156 GLLEAKGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLND-KSRAGKAFENIAR 234

                         250       260
                  ....*....|....*....|....
gi 31711804   299 RLVEQDsmkAVMVEEEPKKRGFFS 322
Cdd:TIGR01968 235 RILGEE---VPFEDLTTQKKGFFA 255
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 61-280 1.19e-32

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: 120.91  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    61 VVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVN--YTCVEVINGDCRLDQALVRDK--RW 136
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPalQALAEGLKGRVNLDPILLKEKsdEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   137 SNFELLC---ISKPRSKLPMGFGGKALEWLVDALKtrpeGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRD 213
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALEALK----EDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVED 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31711804   214 ADRVTGLLE-------CDGIRDIKMIVNRVRTDMIKGEDMMSVLdvQEMLGLSLLGVIPEDSEVIRSTNRGFPL 280
Cdd:pfam01656 157 AKRLGGVIAalvggyaLLGLKIIGVVLNKVDGDNHGKLLKEALE--ELLRGLPVLGVIPRDEAVAEAPARGLPV 228
ParA_partition NF041546
ParA family partition ATPase;
60-95 8.95e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 45.62  E-value: 8.95e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 31711804   60 IVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDA 95
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDA 36
 
Name Accession Description Interval E-value
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 59-300 1.98e-120

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: 1.98e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 139 FELLCISKPRSKlpMGFGGKALEWLVDALKtrpeGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:cd02036  81 LYLLPASQTRDK--DALTPEKLEELVKELK----DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVI 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 219 GLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAW 298
Cdd:cd02036 155 GLLESKGIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIAR 234


                ..
gi 31711804 299 RL 300
Cdd:cd02036 235 RL 236
minD CHL00175
septum-site determining protein; Validated
 57-303 8.78e-117

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 338.28  E-value: 8.78e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   57 TPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRW 136
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRDKRW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  137 SNFELLCISKPRSKLPMGfgGKALEWLVDALKTRpegSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADR 216
Cdd:CHL00175  94 KNLSLLAISKNRQRYNVT--RKNMNMLVDSLKNR---GYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADR 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  217 VTGLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQA 296
Cdd:CHL00175 169 VAGLLEANGIYNVKLLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFENA 248


                 ....*..
gi 31711804  297 AWRLVEQ 303
Cdd:CHL00175 249 ARRLVGK 255
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 59-324 2.34e-98

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 290.81  E-value: 2.34e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:COG2894   3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRFEN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 139 FELLCISKPRSKlpmgfggKAL-----EWLVDALKTRPegspDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRD 213
Cdd:COG2894  83 LYLLPASQTRDK-------DALtpeqmKKLVEELKEEF----DYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 214 ADRVTGLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNkPPTLAGLAF 293
Cdd:COG2894 152 ADRIIGLLEAKGIRKPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLD-EKSKAGQAY 230

                       250       260       270
                ....*....|....*....|....*....|.
gi 31711804 294 EQAAWRLVEQDSmkaVMVEEEPKKRGFFSFF 324
Cdd:COG2894 231 RNIARRLLGEEV---PLRDLEEEKKGFFSRL 258
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 59-322 8.69e-98

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: 289.24  E-value: 8.69e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   139 FELLCISKPRSKLPMGfgGKALEWLVDALKTRPegspDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:TIGR01968  82 LYLLPASQTRDKDAVT--PEQMKKLVNELKEEF----DYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   219 GLLECDGIRDIKMIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKpPTLAGLAFEQAAW 298
Cdd:TIGR01968 156 GLLEAKGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLND-KSRAGKAFENIAR 234

                         250       260
                  ....*....|....*....|....
gi 31711804   299 RLVEQDsmkAVMVEEEPKKRGFFS 322
Cdd:TIGR01968 235 RILGEE---VPFEDLTTQKKGFFA 255
PRK10818 PRK10818
septum site-determining protein MinD;
59-326 2.65e-51

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 170.89  E-value: 2.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRWSN 138
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTEN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  139 FELLCISKPRSKLPMGFGGkaLEWLVDALKtrpEGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:PRK10818  83 LYILPASQTRDKDALTREG--VAKVLDDLK---AMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  219 GLLEC------DGIRDIK--MIVNRVRTDMIKGEDMMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTlAG 290
Cdd:PRK10818 158 GILASksrraeNGEEPIKehLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEAD-AG 236

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 31711804  291 LAFEQAAWRLV-EQDSMKavMVEEEpkKRGFFS-FFGG 326
Cdd:PRK10818 237 KAYADTVDRLLgEERPFR--FIEEE--KKGFLKrLFGG 270
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 59-322 1.37e-37

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: 134.47  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENrVNYTCVEVINGDCRLDQALVRDKrwsn 138
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMED-KPVTLHDVLAGEADIKDAIYEGP---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   139 FELLCIskPRSKLPMGFGGKALEWLVDALKTRPEgSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:TIGR01969  76 FGVKVI--PAGVSLEGLRKADPDKLEDVLKEIID-DTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKTK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   219 GLLECDGIRDIKMIVNRVRTDmiKGEdmMSVLDVQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAW 298
Cdd:TIGR01969 153 IVAEKLGTAILGVVLNRVTRD--KTE--LGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELAA 228

                         250       260
                  ....*....|....*....|....
gi 31711804   299 RLVeqdsmKAVMVEEEPKKRGFFS 322
Cdd:TIGR01969 229 ELA-----GIEYEPKEPKKEGFIA 247
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 61-280 1.19e-32

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: 120.91  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    61 VVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVN--YTCVEVINGDCRLDQALVRDK--RW 136
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPalQALAEGLKGRVNLDPILLKEKsdEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   137 SNFELLC---ISKPRSKLPMGFGGKALEWLVDALKtrpeGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRD 213
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALEALK----EDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVED 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31711804   214 ADRVTGLLE-------CDGIRDIKMIVNRVRTDMIKGEDMMSVLdvQEMLGLSLLGVIPEDSEVIRSTNRGFPL 280
Cdd:pfam01656 157 AKRLGGVIAalvggyaLLGLKIIGVVLNKVDGDNHGKLLKEALE--ELLRGLPVLGVIPRDEAVAEAPARGLPV 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 74-307 1.38e-30

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: 115.37  E-value: 1.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  74 TTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRvnYTCVEVINGDCRLDQALVRDKrwSNFELL-CISKPRSKLP 152
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK--ATLADVLAGEADLEDAIVQGP--GGLDVLpGGSGPAELAE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 153 MgfggKALEWLVDALKtRPEGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVTGLLECD-GIRDIKM 231
Cdd:COG0455  77 L----DPEERLIRVLE-ELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRlGVRRAGV 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 232 IVNRVRTDmikgEDMMSVLD-----VQEMLGLSL--LGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAWRLVEQD 304
Cdd:COG0455 152 VVNRVRSE----AEARDVFErleqvAERFLGVRLrvLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWP 227


                ...
gi 31711804 305 SMK 307
Cdd:COG0455 228 VPE 230
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 35-318 1.46e-29

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: 115.60  E-value: 1.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  35 PSRRSPIRSVLQFNRKPElAGETPRIVVITSGKGGVGKTTTTANVGLSLAR-YGFSVVAIDADLGLRNLDLLLGLENRvn 113
Cdd:COG4963  80 PLSPDELRAALARLLDPG-AARRGRVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLDLEPR-- 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 114 YTCVEVINGDCRLDQALVRD---KRWSNFELLCISKPRSKLPMgFGGKALEWLVDALKTRPegspDFIIIDCPAGIDAGF 190
Cdd:COG4963 157 RGLADALRNPDRLDETLLDRaltRHSSGLSVLAAPADLERAEE-VSPEAVERLLDLLRRHF----DYVVVDLPRGLNPWT 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 191 ITAITPANEAVLVTTPDITALRDADRVTGLLECDGIRD--IKMIVNRVRTDMikgedMMSVLDVQEMLGLSLLGVIPEDS 268
Cdd:COG4963 232 LAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLNRVPKRG-----EISAKDIEEALGLPVAAVLPNDP 306

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 31711804 269 -EVIRSTNRGFPLVLNKPPTLAGLAFEQAAWRLVEQDSMKAVMVEEEPKKR 318
Cdd:COG4963 307 kAVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKAGGKLLKR 357
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 59-298 1.75e-28

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: 110.06  E-value: 1.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARY-GFSVVAIDADLGLRNLDLLLGLENRvnYTCVEVINGDCRLDQALVRD---K 134
Cdd:cd03111   1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPD--YDLADVIQNLDRLDRTLLDSavtR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 135 RWSNFELLCISKPRSKLpMGFGGKALEWLVDALKtrpeGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDA 214
Cdd:cd03111  79 HSSGLSLLPAPQELEDL-EALGAEQVDKLLQVLR----AFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 215 DRVTGLLECDGIRD--IKMIVNRVRTdmiKGEdmMSVLDVQEMLGLSLLGVIPEDSE-VIRSTNRGFPLVLNKPPTLAGL 291
Cdd:cd03111 154 RRLLDSLRELEGSSdrLRLVLNRYDK---KSE--ISPKDIEEALGLEVFATLPNDYKaVSESANTGRPLVEVAPRSALVR 228


                ....*..
gi 31711804 292 AFEQAAW 298
Cdd:cd03111 229 ALQDLAA 235
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 59-289 1.53e-26

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: 104.57  E-value: 1.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRnldlllgleN-------RVNYTCVEVINGDCRLDQALV 131
Cdd:cd02038   1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLA---------NldillglAPKKTLGDVLKGRVSLEDIIV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 132 RDKrwsnfELLCIskprskLPMGFGGKALEWLVDALKTR-------PEGSPDFIIIDCPAGIDAGFITAITPANEAVLVT 204
Cdd:cd02038  72 EGP-----EGLDI------IPGGSGMEELANLDPEQKAKlieelssLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVT 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 205 TPDITALRDADRVTGLLECDGIR-DIKMIVNRVRtDMIKGEDMM-SVLDVQEM---LGLSLLGVIPEDSEVIRSTNRGFP 279
Cdd:cd02038 141 TPEPTSITDAYALIKVLSRRGGKkNFRLIVNMAR-SPKEGRATFeRLKKVAKRfldINLDFVGFIPYDQSVRRAVRSQKP 219

                       250
                ....*....|
gi 31711804 280 LVLNKPPTLA 289
Cdd:cd02038 220 FVLLFPNSKA 229
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 58-303 2.14e-22

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: 94.15  E-value: 2.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  58 PRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQAlVRDKRWS 137
Cdd:COG1192   1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDA-IVPTEIP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 138 NFELLCISKPRSKLPMGFGGKA--LEWLVDALKTRpEGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDAD 215
Cdd:COG1192  80 GLDLIPANIDLAGAEIELVSRPgrELRLKRALAPL-ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 216 RVTGLLEcdGIRD--------IKMIVNRVRTDMIKGEDMMSvlDVQEMLGLSLLG-VIPEDSEVIRSTNRGFPLVLNKPP 286
Cdd:COG1192 159 QLLETIE--EVREdlnpkleiLGILLTMVDPRTRLSREVLE--ELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYDPK 234

                       250
                ....*....|....*..
gi 31711804 287 TLAGLAFEQAAWRLVEQ 303
Cdd:COG1192 235 SKGAKAYRALAEELLER 251
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 52-239 1.75e-19

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: 86.78  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  52 ELAGETPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVnyTCVEVINGDCRLDQALV 131
Cdd:COG0489  86 LLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP--GLSDVLAGEASLEDVIQ 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 132 RDKRwSNFELLCISkPRSKLPMG-FGGKALEWLVDALKTRpegsPDFIIIDCPAGIDAGFITAITP-ANEAVLVTTPDIT 209
Cdd:COG0489 164 PTEV-EGLDVLPAG-PLPPNPSElLASKRLKQLLEELRGR----YDYVIIDTPPGLGVADATLLASlVDGVLLVVRPGKT 237

                       170       180       190
                ....*....|....*....|....*....|
gi 31711804 210 ALRDADRVTGLLECDGIRDIKMIVNRVRTD 239
Cdd:COG0489 238 ALDDVRKALEMLEKAGVPVLGVVLNMVCPK 267
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 59-292 2.31e-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: 2.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVitSGKGGVGKTTTTANVGLSLARYGFSVVAIDA----------------DLGLRNLDLLLGLENRVNYTCVEVIN- 121
Cdd:COG3640   2 KIAV--AGKGGVGKTTLSALLARYLAEKGKPVLAVDAdpnanlaealgleveaDLIKPLGEMRELIKERTGAPGGGMFKl 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 122 ---GDCRLDQALVRDKrwsNFELLCISKPRSklpMGFG-----GKALEWLVDALKTRPEgspDFIIIDCPAGIDA---GF 190
Cdd:COG3640  80 npkVDDIPEEYLVEGD---GVDLLVMGTIEE---GGSGcycpeNALLRALLNHLVLGNY---EYVVVDMEAGIEHlgrGT 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 191 ITAItpaNEAVLVTTPDITALRDADRVTGLLECDGIRDIKMIVNRVRTDMIKGEdmmsvldVQEMLGLSLLGVIPEDSEV 270
Cdd:COG3640 151 AEGV---DLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEF-------LRELLGLELLGFIPYDEEV 220

                       250       260
                ....*....|....*....|...
gi 31711804 271 IRSTNRGFPLV-LNKPPTLAGLA 292
Cdd:COG3640 221 READLEGKPLLdLPDSPAVAAVE 243
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 59-212 1.13e-12

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: 65.30  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNYTCVEVINGDCRLDQALVRDKRwSN 138
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVI-EN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31711804   139 FELLCISKPRSKLPMGFGGK-----ALEWLVDALKTRpegsPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALR 212
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIenrenILKEALEPVKDN----YDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALE 155
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 65-286 1.59e-12

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: 66.18  E-value: 1.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  65 SGKGGVGKTTTTANVGLSLARYGFSVVAIDA-------------DLGLRNLDLLLGLENRVN---YTCVEVINGDCRLD- 127
Cdd:cd02034   6 AGKGGVGKTTIAALLIRYLAKKGGKVLAVDAdpnsnlaetlgveVEKLPLIKTIGDIRERTGakkGEPPEGMSLNPYVDd 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 128 ---QALVRDKrwsNFELLCISKPRSKLP--MGFGGKALEWLVDALKTRPEgspDFIIIDCPAGIDAgFITAITPANEA-V 201
Cdd:cd02034  86 iikEIIVEPD---GIDLLVMGRPEGGGSgcYCPVNALLRELLRHLALKNY---EYVVIDMEAGIEH-LSRGTIRAVDLlI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 202 LVTTPDITALRDADRVTGLLECDGIRDIKMIVNRVRTDMIKGEdmmsvLDvQEMLGLSLLGVIPEDSEVIRSTNRGFPLV 281
Cdd:cd02034 159 IVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQEL-----IE-ELLIKLKLIGVIPYDEEIMEADLKGKPLF 232


                ....*
gi 31711804 282 LNKPP 286
Cdd:cd02034 233 DLDSA 237
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 59-301 7.55e-12

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: 64.40  E-value: 7.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADlglrnldlllglenrvnytcvevING-------DCRLDQALV 131
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD-----------------------IYGpsiprmlGLEGERPEQ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   132 RDKRW---SNFELLCISkprsklpMGF----GGKALEW------------LVDALktrpEGSPDFIIIDCPAGI-DAgfi 191
Cdd:pfam10609  61 SDGGIipvEAHGIKVMS-------IGFllpdEDDAVIWrgpmksgaikqfLTDVD----WGELDYLIIDLPPGTgDE--- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   192 tAIT-----PANEAVLVTTPDITALRDADR-----------VTGLLE---------CDGIRDIkmivnrVRTDmiKGEDM 246
Cdd:pfam10609 127 -QLTlaqllPLTGAVIVTTPQDVALLDVRKaidmfkkvnvpVLGVVEnmsyfvcphCGEETYI------FGKG--GGEKL 197

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 31711804   247 msvldvQEMLGLSLLGVIPEDSEVIRSTNRGFPLVLNKPPTLAGLAFEQAAWRLV 301
Cdd:pfam10609 198 ------AEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 60-265 2.86e-11

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: 62.40  E-value: 2.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  60 IVVITSGKGGVGKTTTTANVGLSLARygfsVVAIDADLGLRNLDLLLGLENRVNY-------------------TCVEVi 120
Cdd:cd03110   1 IIAVLSGKGGTGKTTITANLAVLLYN----VILVDCDVDAPNLHLLLGPEPEEEEdfvggkkafidqekcircgNCERV- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 121 ngdCRLDQALVRDKRWSNFELLC---------------ISKPRS----------KLPMGFG---------GKalewLVDA 166
Cdd:cd03110  76 ---CKFGAILEFFQKLIVDESLCegcgacviicprgaiYLKDRDtgkifisssdGGPLVHGrlnigeensGK----LVTE 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 167 LK---TRPEGSPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVTGLLECDGIrDIKMIVNRvrtDMIKG 243
Cdd:cd03110 149 LRkkaLERSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAIELAKHFGI-PTGIVINR---YDIND 224

                       250       260
                ....*....|....*....|..
gi 31711804 244 EDMMSVLDVQEMLGLSLLGVIP 265
Cdd:cd03110 225 EISEEIEDFADEEGIPLLGKIP 246
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 59-250 5.73e-11

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: 59.48  E-value: 5.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDAdlglrnldlllglenrvnytcvevingdcrldqalvrDKRWSn 138
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-------------------------------------DPQGS- 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 139 fellciskprsklpmgfggkALEWLvdalktrpegsPDFIIIDCPAGIDAGFITAITPANEAVLVTTPDITALRDADRVT 218
Cdd:cd02042  43 --------------------LTSWL-----------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 31711804 219 GLLE------CDGIRDIKMIVNRVRTDMIKGEDMMSVL 250
Cdd:cd02042  92 DTLEelkkqlNPPLLILGILLTRVDPRTKLAREVLEEL 129
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 41-235 7.78e-11

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: 60.28  E-value: 7.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  41 IRSVLQFNrkpeLAGETPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVnyTCVEVI 120
Cdd:cd05387   6 LRTNLLFA----GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEP--GLSEVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 121 NGDCRLDQALVRDKRwSNFELLcISKPRSKLPMG-FGGKALEWLVDALKtrpeGSPDFIIIDCP---AGIDAgfiTAITP 196
Cdd:cd05387  80 SGQASLEDVIQSTNI-PNLDVL-PAGTVPPNPSElLSSPRFAELLEELK----EQYDYVIIDTPpvlAVADA---LILAP 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 31711804 197 ANEAV-LVTTPDITALRDADRVTGLLECDGIRDIKMIVNR 235
Cdd:cd05387 151 LVDGVlLVVRAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 41-239 2.69e-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: 58.99  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    41 IRSVLQFnrkpelAGETPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADLGLRNLDLLLGLENRVNyTCVEVI 120
Cdd:TIGR01007   6 IRTNIQF------SGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKIT-GLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   121 NGDCRLDQALvRDKRWSNFELLCiSKPRSKLPMGF-GGKALEWLVDALKTRpegsPDFIIIDCP---AGIDAGFITAITP 196
Cdd:TIGR01007  79 SGTTDLSDAI-CDTNIENLDVIT-AGPVPPNPTELlQSSNFKTLIETLRKR----FDYIIIDTPpigTVTDAAIIARACD 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 31711804   197 AneAVLVTTPDITALRDADRVTGLLECDGIRDIKMIVNRVRTD 239
Cdd:TIGR01007 153 A--SILVTDAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDIS 193
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 60-286 4.32e-10

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: 59.28  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    60 IVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDAdlglrnldlllGLEN--RVNYTC-VEVINGdcrLDQALVRDKRW 136
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDL-----------DPQNllRLHFGMdWSVRDG---WARALLNGADW 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   137 SNFELLCISKPRSkLPMG---------FGGKALEWLVDAL-KTRPEGSpDFIIIDCPAGIDAGFITAITPANEAVLVTTP 206
Cdd:TIGR03371  69 AAAAYRSPDGVLF-LPYGdlsadereaYQAHDAGWLARLLqQLDLAAR-DWVLIDLPRGPSPITRQALAAADLVLVVVNA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804   207 DITA-LRDADRVTGLLECDGIRD-IKMIVNRVRTDMIKGEDMMSVLdvQEMLGLSLL-GVIPEDSEVIRSTNRGFPlVLN 283
Cdd:TIGR03371 147 DAACyATLHQLALALFAGSGPRDgPRFLINQFDPARQLSRDVRAVL--RQTLGSRLLpFVIHRDEAVSEALARGTP-VLN 223


                  ...
gi 31711804   284 KPP 286
Cdd:TIGR03371 224 YAP 226
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 59-270 1.25e-08

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: 54.43  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDADlglrnldlllglenrvnytcvevING-------DCRLDQALV 131
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD-----------------------IYGpsiprllGVEGKPLHQ 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 132 RDKRWS---NFELLCISkprsklpMGF--------------GGKALE-------WlvdalktrpeGSPDFIIIDCPAGI- 186
Cdd:cd02037  58 SEEGIVpveVGGIKVMS-------IGFllpeddaviwrgpmKSGAIKqflkdvdW----------GELDYLIIDLPPGTg 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 187 DAGF-ITAITPANEAVLVTTPDITALRDADRVTGLLECDGIRDIKMIVNrvrtdM-------------IKGEDmmSVLDV 252
Cdd:cd02037 121 DEHLsLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKLNIPVLGIVEN-----MsgfvcphcgkkiyIFGKG--GGEKL 193

                       250
                ....*....|....*...
gi 31711804 253 QEMLGLSLLGVIPEDSEV 270
Cdd:cd02037 194 AEELGVPFLGKIPLDPEL 211
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 59-325 3.46e-07

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 50.83  E-value: 3.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804  59 RIVVItsGKGGVGKTTTTANVGLSLARYGFSVVAI------DADLGLRNLdlllglenRVNYTCVEVINGDCRLDQALVR 132
Cdd:cd02117   2 SIVVY--GKGGIGKSTTASNLSAALAEGGKKVLHVgcdpkhDSTLLLTGG--------KVPPTIDEMLTEDGTAEELRRE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 133 DKRWSNFE-LLCISKPRSKLPMGFGGKALEWLVDALKT--RPEGSPDFIIID------CpagidAGFITAI--TPANEAV 201
Cdd:cd02117  72 DLLFSGFNgVDCVEAGGPEPGVGCGGRGIGTMLELLEEhgLLDDDYDVVIFDvlgdvvC-----GGFAAPLrrGFAQKVV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804 202 LVTTPDITALRDADRVTGLLEC---DGIRDIKMIVNRVRTDmikGEDMmsVLDVQEMLGLSLLGVIPEDSEVIRSTNRGF 278
Cdd:cd02117 147 IVVSEELMSLYAANNIVKAVENyskNGVRLAGLVANLRDPA---GTEE--IQAFAAAVGTKILAVIPRDPAVRRAELARV 221

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 31711804 279 PLVLNKPPTLAGLAFEQAAWRLveQDSMKAVMVEEEPKKRGFFSFFG 325
Cdd:cd02117 222 TVFEHDPVSPAASEFARLAAKI--ADAVPPVPGPRPLSDRELFALLG 266
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 59-94 1.19e-06

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 46.66  E-value: 1.19e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 31711804  59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAID 94
Cdd:cd01983   1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLID 36
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
60-95 6.13e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 47.34  E-value: 6.13e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 31711804   60 IVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDA 95
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDA 144
ParA_partition NF041546
ParA family partition ATPase;
60-95 8.95e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 45.62  E-value: 8.95e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 31711804   60 IVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDA 95
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDA 36
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
56-94 2.24e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 45.20  E-value: 2.24e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 31711804  56 ETPRIVVITsGKGGVGKTTTTANVGLSLARYGFSV--VAID 94
Cdd:COG0003   1 DMTRIIFFT-GKGGVGKTTVAAATALALAERGKRTllVSTD 40
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 61-90 7.12e-05

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: 43.65  E-value: 7.12e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 31711804  61 VVITSGKGGVGKTTTTANVGLSLARYGFSV 90
Cdd:cd02035   2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRV 31
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 59-200 2.14e-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: 42.06  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711804    59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDadLGLRNLDLLLGLENRVnytcvevingdcrldqALVRDKRWSN 138
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAID--LDLRQRTFHRYFENRS----------------ATADRTGLSL 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31711804   139 FELLCISKPRSKLPMGFGGKALEWL-VDALKTRPEGSPDFIIIDCPaGIDAGFI--------TAITPANEA 200
Cdd:pfam09140  63 PTPEHLNLPDNDVAEVPDGENIDDArLEEAFADLEARCDFIVIDTP-GSDSPLSrlahsradTLVTPLNDS 132
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 42-94 4.50e-04

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 41.58  E-value: 4.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 31711804   42 RSVLQF--NRKPelaGETPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAID 94
Cdd:PRK13869 106 RESIDFvpHRRG---SEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVD 157
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 54-94 7.71e-04

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: 40.73  E-value: 7.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 31711804    54 AGETPRIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAID 94
Cdd:TIGR03453 100 GGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAID 140
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 61-90 1.43e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.07  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 31711804    61 VVITSGKGGVGKTTTTANVGLSLARYGFSV 90
Cdd:TIGR04291 323 LIMTMGKGGVGKTTVAAAIAVRLANKGLDV 352
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 66-93 1.66e-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: 39.59  E-value: 1.66e-03
                        10        20
                ....*....|....*....|....*...
gi 31711804  66 GKGGVGKTTTTANVGLSLARYGFSVVAI 93
Cdd:cd02032   7 GKGGIGKSTTSSNLSAAFAKRGKKVLQI 34
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 61-93 5.20e-03

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 38.10  E-value: 5.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 31711804    61 VVITSGKGGVGKTTTTANVGLSLARYGFSVVAI 93
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLI 35
PHA02518 PHA02518
ParA-like protein; Provisional
 59-95 5.55e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 37.52  E-value: 5.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 31711804   59 RIVVITSGKGGVGKTTTTANVGLSLARYGFSVVAIDA 95
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDL 37
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 66-93 8.86e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 37.25  E-value: 8.86e-03
                         10        20
                 ....*....|....*....|....*...
gi 31711804   66 GKGGVGKTTTTANVGLSLARYGFSVVAI 93
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQI 36
chlL CHL00072
photochlorophyllide reductase subunit L
 66-93 9.42e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 37.41  E-value: 9.42e-03
                         10        20
                 ....*....|....*....|....*...
gi 31711804   66 GKGGVGKTTTTANVGLSLARYGFSVVAI 93
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQI 34
 
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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