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Conserved domains on  [gi|493358314|ref|WP_006314831|]
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MULTISPECIES: septum site-determining protein MinD [Agrobacterium]

Protein Classification

septum site-determining protein MinD( domain architecture ID 11458413)

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 COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
1-265 8.80e-162

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


:

Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 449.12  E-value: 8.80e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRL 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLD 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 161 SKTLKaergermEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAYFD 240
Cdd:COG2894  161 AKGIR-------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVL-DEKSKAGQAYRN 232
                        250       260
                 ....*....|....*....|....*.
gi 493358314 241 AARRLSGEDIPVVIPG-EKRGIFSKI 265
Cdd:COG2894  233 IARRLLGEEVPLRDLEeEKKGFFSRL 258
 
Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
1-265 8.80e-162

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 449.12  E-value: 8.80e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRL 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLD 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 161 SKTLKaergermEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAYFD 240
Cdd:COG2894  161 AKGIR-------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVL-DEKSKAGQAYRN 232
                        250       260
                 ....*....|....*....|....*.
gi 493358314 241 AARRLSGEDIPVVIPG-EKRGIFSKI 265
Cdd:COG2894  233 IARRLLGEEVPLRDLEeEKKGFFSRL 258
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
2-266 5.42e-122

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: 348.56  E-value: 5.42e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    2 GKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRLE 81
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   82 TLFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLDS 161
Cdd:TIGR01968  81 NLYLLPASQTRDKDAVTPEQMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  162 KtlkaergERMEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAYFDA 241
Cdd:TIGR01968 161 K-------GIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVL-NDKSRAGKAFENI 232
                         250       260
                  ....*....|....*....|....*.
gi 493358314  242 ARRLSGEDIP-VVIPGEKRGIFSKIF 266
Cdd:TIGR01968 233 ARRILGEEVPfEDLTTQKKGFFARIK 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-266 4.29e-119

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 341.53  E-value: 4.29e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRL 80
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTRDKDNLTPEGVEWVIAELKKH-FDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLL 159
Cdd:PRK10818  81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMdFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 160 DSKTLKAERGER-MEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAY 238
Cdd:PRK10818 161 ASKSRRAENGEEpIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVIL-DIEADAGKAY 239
                        250       260
                 ....*....|....*....|....*....
gi 493358314 239 FDAARRLSGEDIPV-VIPGEKRGIFSKIF 266
Cdd:PRK10818 240 ADTVDRLLGEERPFrFIEEEKKGFLKRLF 268
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
3-245 7.92e-114

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: 326.85  E-value: 7.92e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRLET 82
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  83 LFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLDSK 162
Cdd:cd02036   81 LYLLPASQTRDKDALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLESK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 163 TLKaergermEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLADARCAPAMAYFDAA 242
Cdd:cd02036  161 GIV-------NIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIA 233

                 ...
gi 493358314 243 RRL 245
Cdd:cd02036  234 RRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-225 1.94e-36

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: 129.00  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    5 VVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNL--DLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRLET 82
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   83 -LFLLPASQTRDKDNLTPEG------VEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRI 155
Cdd:pfam01656  81 gLDLIPGNIDLEKFEKELLGprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493358314  156 IGLLDSKTLKAERGERMEKHLLLTRYDSvraERGDMLKVDDVLEIL-SIPLLGIIPESTDVLRASNVGAPV 225
Cdd:pfam01656 161 GGVIAALVGGYALLGLKIIGVVLNKVDG---DNHGKLLKEALEELLrGLPVLGVIPRDEAVAEAPARGLPV 228
ParA_partition NF041546
ParA family partition ATPase;
4-144 2.71e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 49.86  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   4 VVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVglrnldlvmgaerrvvydlvnviQGDAKLTQALIRDKRletl 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-----------------------QGSALDWAAAREDER---- 53
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493358314  84 fLLPASqtrdkdNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNP 144
Cdd:NF041546  54 -PFPVV------GLARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQP 107
 
Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
1-265 8.80e-162

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 449.12  E-value: 8.80e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRL 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLD 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 161 SKTLKaergermEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAYFD 240
Cdd:COG2894  161 AKGIR-------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVL-DEKSKAGQAYRN 232
                        250       260
                 ....*....|....*....|....*.
gi 493358314 241 AARRLSGEDIPVVIPG-EKRGIFSKI 265
Cdd:COG2894  233 IARRLLGEEVPLRDLEeEKKGFFSRL 258
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
2-266 5.42e-122

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: 348.56  E-value: 5.42e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    2 GKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRLE 81
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   82 TLFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLDS 161
Cdd:TIGR01968  81 NLYLLPASQTRDKDAVTPEQMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  162 KtlkaergERMEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAYFDA 241
Cdd:TIGR01968 161 K-------GIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVL-NDKSRAGKAFENI 232
                         250       260
                  ....*....|....*....|....*.
gi 493358314  242 ARRLSGEDIP-VVIPGEKRGIFSKIF 266
Cdd:TIGR01968 233 ARRILGEEVPfEDLTTQKKGFFARIK 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-266 4.29e-119

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 341.53  E-value: 4.29e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRL 80
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTRDKDNLTPEGVEWVIAELKKH-FDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLL 159
Cdd:PRK10818  81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMdFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 160 DSKTLKAERGER-MEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLaDARCAPAMAY 238
Cdd:PRK10818 161 ASKSRRAENGEEpIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVIL-DIEADAGKAY 239
                        250       260
                 ....*....|....*....|....*....
gi 493358314 239 FDAARRLSGEDIPV-VIPGEKRGIFSKIF 266
Cdd:PRK10818 240 ADTVDRLLGEERPFrFIEEEKKGFLKRLF 268
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
3-245 7.92e-114

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: 326.85  E-value: 7.92e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRLET 82
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  83 LFLLPASQTRDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLDSK 162
Cdd:cd02036   81 LYLLPASQTRDKDALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLESK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 163 TLKaergermEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLADARCAPAMAYFDAA 242
Cdd:cd02036  161 GIV-------NIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIA 233

                 ...
gi 493358314 243 RRL 245
Cdd:cd02036  234 RRL 236
minD CHL00175
septum-site determining protein; Validated
1-266 4.64e-80

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 242.75  E-value: 4.64e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRL 80
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRDKRW 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTRDKDNLTPEGVEWVIAELKKH-FDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLL 159
Cdd:CHL00175  94 KNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRgYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADRVAGLL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 160 DSKTLKaergermEKHLLLTRYDSVRAERGDMLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLADARCAPAMAYF 239
Cdd:CHL00175 174 EANGIY-------NVKLLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFE 246
                        250       260
                 ....*....|....*....|....*...
gi 493358314 240 DAARRLSGEDIPVV-IPGEKRGIFSKIF 266
Cdd:CHL00175 247 NAARRLVGKQDYFIdLDSPSKGPLKRLQ 274
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
3-266 1.66e-39

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: 137.94  E-value: 1.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVVyDLVNVIQGDAKLTQALIRDKrlET 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPV-TLHDVLAGEADIKDAIYEGP--FG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   83 LFLLPASQTRDK-DNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIgllds 161
Cdd:TIGR01969  78 VKVIPAGVSLEGlRKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKTK----- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  162 ktLKAERGERMEKHLLLTRYDSVRAErgdmLKVDDVLEILSIPLLGIIPESTDVLRASNVGAPVTLADARCAPAMAYFDA 241
Cdd:TIGR01969 153 --IVAEKLGTAILGVVLNRVTRDKTE----LGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMEL 226
                         250       260
                  ....*....|....*....|....*
gi 493358314  242 ARRLSGEDIPVVIPgEKRGIFSKIF 266
Cdd:TIGR01969 227 AAELAGIEYEPKEP-KKEGFIAKVI 250
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-225 1.94e-36

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: 129.00  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    5 VVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNL--DLVMGAERRVVYDLVNVIQGDAKLTQALIRDKRLET 82
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   83 -LFLLPASQTRDKDNLTPEG------VEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRI 155
Cdd:pfam01656  81 gLDLIPGNIDLEKFEKELLGprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493358314  156 IGLLDSKTLKAERGERMEKHLLLTRYDSvraERGDMLKVDDVLEIL-SIPLLGIIPESTDVLRASNVGAPV 225
Cdd:pfam01656 161 GGVIAALVGGYALLGLKIIGVVLNKVDG---DNHGKLLKEALEELLrGLPVLGVIPRDEAVAEAPARGLPV 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
18-251 8.55e-35

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: 125.00  E-value: 8.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  18 TSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRvvYDLVNVIQGDAKLTQALIRDKrlETLFLLPASQ-TRDKDN 96
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK--ATLADVLAGEADLEDAIVQGP--GGLDVLPGGSgPAELAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  97 LTP-EGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIglldsKTLKAERGERmEKH 175
Cdd:COG0455   77 LDPeERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALL-----KLLRRRLGVR-RAG 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493358314 176 LLLTRYDSVRAERGDMLKVDDVLE---ILSIPLLGIIPESTDVLRASNVGAPVTLADARCAPAMAYFDAARRLSGEDIP 251
Cdd:COG0455  151 VVVNRVRSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWPVP 229
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
2-248 3.98e-33

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: 123.69  E-value: 3.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   2 GKVVVVTSGKGGVGKTTSTAALGAALAQN-KEKVVVVDFDVGLRNLDLVMGAERRvvYDLVNVIQGDAKLTQALIRD--- 77
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPR--RGLADALRNPDRLDETLLDRalt 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  78 KRLETLFLLPASQTRDK-DNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRII 156
Cdd:COG4963  180 RHSSGLSVLAAPADLERaEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLL 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 157 glldsKTLKAERGERMEKHLLLTRYDsvraeRGDMLKVDDVLEILSIPLLGIIP-ESTDVLRASNVGAPVTLADARCAPA 235
Cdd:COG4963  260 -----DLLRELGLPDDKVRLVLNRVP-----KRGEISAKDIEEALGLPVAAVLPnDPKAVAEAANQGRPLAEVAPKSPLA 329
                        250
                 ....*....|...
gi 493358314 236 MAYFDAARRLSGE 248
Cdd:COG4963  330 KAIRKLAARLTGR 342
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
3-245 7.97e-31

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: 115.34  E-value: 7.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDV-GlrNLDLVMGAERRVV-YDLVNVIQGDAKLTQAlIRDKRL 80
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPqG--NLTSGLGLDPDDLdPTLYDLLLDDAPLEDA-IVPTEI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQ---TRDKDNLTPEGVEWV----IAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSD 153
Cdd:COG1192   79 PGLDLIPANIdlaGAEIELVSRPGRELRlkraLAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 154 RIIGLLDSktLKAERGERMEK-HLLLTRYDSVRAERGDMlkVDDVLEILSIPLLG-IIPESTDVLRASNVGAPVTLADAR 231
Cdd:COG1192  159 QLLETIEE--VREDLNPKLEIlGILLTMVDPRTRLSREV--LEELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYDPK 234
                        250
                 ....*....|....
gi 493358314 232 CAPAMAYFDAARRL 245
Cdd:COG1192  235 SKGAKAYRALAEEL 248
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
3-235 2.06e-25

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: 100.34  E-value: 2.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRvvYDLVNVIQGDAKLTQALIRDKrlET 82
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK--KTLGDVLKGRVSLEDIIVEGP--EG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  83 LFLLPASQ-TRDKDNLTPEGVEWVIAELKK---HFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIgl 158
Cdd:cd02038   77 LDIIPGGSgMEELANLDPEQKAKLIEELSSlesNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALI-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 159 ldsKTLKAERGERmEKHLLLTRYDSVRAERGDMLKVDDVLE-ILSIPL--LGIIPESTDVLRASNVGAPVTLADARCAPA 235
Cdd:cd02038  155 ---KVLSRRGGKK-NFRLIVNMARSPKEGRATFERLKKVAKrFLDINLdfVGFIPYDQSVRRAVRSQKPFVLLFPNSKAS 230
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
4-161 1.40e-21

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 91.40  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   4 VVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERRVvyDLVNVIQGDAKLTQALIRDkRLETL 83
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP--GLSDVLAGEASLEDVIQPT-EVEGL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  84 FLLPASQTRDKDN--LTPEGVEWVIAELKKHFDWVICDSPAGIE-RGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLD 160
Cdd:COG0489  171 DVLPAGPLPPNPSelLASKRLKQLLEELRGRYDYVIIDTPPGLGvADATLLASLVDGVLLVVRPGKTALDDVRKALEMLE 250

                 .
gi 493358314 161 S 161
Cdd:COG0489  251 K 251
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
3-225 3.97e-20

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: 86.18  E-value: 3.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQ-NKEKVVVVDFDVGLRNLDLVMGAERRvvYDLVNVIQGDAKLTQALIRD---K 78
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPFGDLGLYLNLRPD--YDLADVIQNLDRLDRTLLDSavtR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  79 RLETLFLLPASQTRDK-DNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIg 157
Cdd:cd03111   79 HSSGLSLLPAPQELEDlEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLL- 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493358314 158 lldsKTLKAERGERMEKHLLLTRYDSvRAErgdmLKVDDVLEILSIPLLGIIPESTDVLRAS-NVGAPV 225
Cdd:cd03111  158 ----DSLRELEGSSDRLRLVLNRYDK-KSE----ISPKDIEEALGLEVFATLPNDYKAVSESaNTGRPL 217
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
3-162 4.67e-17

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: 76.84  E-value: 4.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDvgLRN--LDLVMGAERRVvyDLVNVIQGDAKLTQALIRDkRL 80
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD--LRRpsLHRLLGLPNEP--GLSEVLSGQASLEDVIQST-NI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  81 ETLFLLPASQTrdKDN----LTPEGVEWVIAELKKHFDWVICDSPA-GIERGATLAMRHADVAVVVTNPEVSSVRDSDRI 155
Cdd:cd05387   95 PNLDVLPAGTV--PPNpselLSSPRFAELLEELKEQYDYVIIDTPPvLAVADALILAPLVDGVLLVVRAGKTRRREVKEA 172

                 ....*..
gi 493358314 156 IGLLDSK 162
Cdd:cd05387  173 LERLEQA 179
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
3-194 6.01e-15

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: 72.38  E-value: 6.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDvGLRNLDLVMGAERRVVYDLVNVIQGDAKLTQALIRDkrLET 82
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLD-PQNLLRLHFGMDWSVRDGWARALLNGADWAAAAYRS--PDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   83 LFLLP--ASQTRDKDNLTPEGVEWVIAELKK----HFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRdsdRII 156
Cdd:TIGR03371  79 VLFLPygDLSADEREAYQAHDAGWLARLLQQldlaARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYA---TLH 155
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 493358314  157 GLLDSktLKAERGERMEKHLLLTRYDSVRAERGDMLKV 194
Cdd:TIGR03371 156 QLALA--LFAGSGPRDGPRFLINQFDPARQLSRDVRAV 191
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
3-237 3.05e-14

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 70.20  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVvtSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLrNLDLVMGAErrVVYDLVNVIqGDAKltqALIRDKR--- 79
Cdd:COG3640    2 KIAV--AGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNA-NLAEALGLE--VEADLIKPL-GEMR---ELIKERTgap 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  80 -----LETLFL--LPASQTRDKDNL------TPEG------------VEWVIAEL-KKHFDWVICDSPAGIE---RGATl 130
Cdd:COG3640   73 gggmfKLNPKVddIPEEYLVEGDGVdllvmgTIEEggsgcycpenalLRALLNHLvLGNYEYVVVDMEAGIEhlgRGTA- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 131 amRHADVAVVVTNPEVSSVRDSDRIIGLldSKTLKAERgermeKHLLLTRydsVRAERgdmlKVDDVLEILSIPLLGIIP 210
Cdd:COG3640  152 --EGVDLLLVVSEPSRRSIETARRIKEL--AEELGIKK-----IYLVGNK---VREEE----DEEFLRELLGLELLGFIP 215
                        250       260
                 ....*....|....*....|....*...
gi 493358314 211 ESTDVLRASNVGAPV-TLADARCAPAMA 237
Cdd:COG3640  216 YDEEVREADLEGKPLlDLPDSPAVAAVE 243
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-193 2.15e-13

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: 65.25  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDvglrnldlvmgaerrvvydlvnvIQGDAklTQALirdkrlet 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD-----------------------PQGSL--TSWL-------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  83 lfllpasqtrdkdnltpegvewviaelkkhFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLDsK 162
Cdd:cd02042   48 ------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLE-E 96
                        170       180       190
                 ....*....|....*....|....*....|.
gi 493358314 163 TLKAERGERMEKHLLLTRYDSVRAERGDMLK 193
Cdd:cd02042   97 LKKQLNPPLLILGILLTRVDPRTKLAREVLE 127
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-121 1.34e-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: 64.53  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    2 GKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLrNLDLVMGAERRVVY-DLVNVIQGDAKLTQALIRDKrL 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG-NATSGLGIDKNNVEkTIYELLIGECNIEEAIIKTV-I 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 493358314   81 ETLFLLPAS-----------QTRDKDNLTPEGVEWViaelKKHFDWVICDSP 121
Cdd:pfam13614  79 ENLDLIPSNidlagaeieliGIENRENILKEALEPV----KDNYDYIIIDCP 126
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
5-210 1.30e-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: 62.79  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   5 VVVTSGKGGVGKTTSTAALGAALaqnkEKVVVVDFDVGLRNLDLVMGAERRVVYDLVN-------------------VIQ 65
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGgkkafidqekcircgncerVCK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  66 GDA--KLTQALIRDKRL-------------ETLFLLP-------------ASQTRDKDNLTPEGVEWVIAELKKH----- 112
Cdd:cd03110   78 FGAilEFFQKLIVDESLcegcgacviicprGAIYLKDrdtgkifisssdgGPLVHGRLNIGEENSGKLVTELRKKalers 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 113 --FDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLdsKTLKAERGermekhLLLTRYD--SVRAEr 188
Cdd:cd03110  158 keCDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAIELA--KHFGIPTG------IVINRYDinDEISE- 228
                        250       260
                 ....*....|....*....|..
gi 493358314 189 gdmlKVDDVLEILSIPLLGIIP 210
Cdd:cd03110  229 ----EIEDFADEEGIPLLGKIP 246
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
3-148 3.36e-11

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


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 61.62  E-value: 3.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDF--DVGLR---NLDLvmgaERRvvydlvnviQG--DAKLTQALI 75
Cdd:pfam06564   2 KILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLspDNLLRlhfNVPF----EHR---------QGwaRAELDGADW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   76 RDKRLET---LFLLPASQTRDKDNLTPEGV-----EWVIA--ELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPE 145
Cdd:pfam06564  69 RDAALEYtpgLDLLPFGRLSVEEQENLQQLqpdpgAWCRRlqQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD 148

                  ...
gi 493358314  146 VSS 148
Cdd:pfam06564 149 ANC 151
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
3-160 3.70e-11

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: 60.91  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314    3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDvgLRNldLVMGA---ERRVVYDLVNVIQGDAKLTQAlIRDKR 79
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD--MRN--SVMSGtfkSQNKITGLTNFLSGTTDLSDA-ICDTN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   80 LETLFLLPASQTRDKDN--LTPEGVEWVIAELKKHFDWVICDS-PAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRII 156
Cdd:TIGR01007  93 IENLDVITAGPVPPNPTelLQSSNFKTLIETLRKRFDYIIIDTpPIGTVTDAAIIARACDASILVTDAGKIKKREVKKAK 172

                  ....
gi 493358314  157 GLLD 160
Cdd:TIGR01007 173 EQLE 176
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
9-236 4.19e-10

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: 58.48  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   9 SGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLrNLDLVMGaerrvvydlVNVIQGDAKLTQALIRDKRLE------T 82
Cdd:cd02034    6 AGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS-NLAETLG---------VEVEKLPLIKTIGDIRERTGAkkgeppE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  83 LFLL-------PASQTRDKDNL------TPEGV-------------EWVIAELKKHFDWVICDSPAGIE---RGATlamR 133
Cdd:cd02034   76 GMSLnpyvddiIKEIIVEPDGIdllvmgRPEGGgsgcycpvnallrELLRHLALKNYEYVVIDMEAGIEhlsRGTI---R 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 134 HADVAVVVTNPEVSSVRDSDRIIGLLDSKTLKaergermEKHLLLTRydsVRAErgdmLKVDDVLEILS-IPLLGIIPES 212
Cdd:cd02034  153 AVDLLIIVIEPSKRSIQTAKRIKELAEELGIK-------KIYLIVNK---VRNE----EEQELIEELLIkLKLIGVIPYD 218
                        250       260
                 ....*....|....*....|....
gi 493358314 213 TDVLRASNVGAPVTLADARCAPAM 236
Cdd:cd02034  219 EEIMEADLKGKPLFDLDSAAVKAI 242
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
3-40 3.91e-08

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: 50.51  E-value: 3.91e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFD 40
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
3-41 1.92e-07

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: 50.91  E-value: 1.92e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 493358314    3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDV 41
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADI 42
ParA_partition NF041546
ParA family partition ATPase;
4-144 2.71e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 49.86  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   4 VVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVglrnldlvmgaerrvvydlvnviQGDAKLTQALIRDKRletl 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-----------------------QGSALDWAAAREDER---- 53
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493358314  84 fLLPASqtrdkdNLTPEGVEWVIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNP 144
Cdd:NF041546  54 -PFPVV------GLARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQP 107
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
3-41 6.38e-07

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


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 49.04  E-value: 6.38e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDV 41
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADI 39
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
5-40 1.32e-06

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: 48.50  E-value: 1.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 493358314    5 VVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFD 40
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-40 1.90e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 48.28  E-value: 1.90e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 493358314   1 MGKVVVVTsGKGGVGKTTSTAALGAALAQNKEKVVVVDFD 40
Cdd:COG0003    2 MTRIIFFT-GKGGVGKTTVAAATALALAERGKRTLLVSTD 40
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
2-161 4.56e-06

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


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 46.38  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   2 GKVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDvGLRNLDLVMGAERR-----VVYDLVNVIQGDAKLTQALIR 76
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-RLQSTDVFFGASGRylmsdHLYTLKSRKANLADKLESCVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  77 DKRLETLFLLPASQTRDKDNLTPEGVEWVIAELKK--HFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDR 154
Cdd:cd17869   82 QHESGVYYFSPFKSALDILEIKKDDILHMITKLVEahAYDYIIMDLSFEFSSTVCKLLQASHNNVVIALQDANSSYKLNK 161

                 ....*..
gi 493358314 155 IIGLLDS 161
Cdd:cd17869  162 FLRALED 168
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
3-37 1.90e-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: 44.81  E-value: 1.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 493358314   3 KVVVVTsGKGGVGKTTSTAALGAALAQNKEKVVVV 37
Cdd:cd02035    1 RIIFFG-GKGGVGKTTIAAATAVRLAEQGKRVLLV 34
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-41 7.47e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.49  E-value: 7.47e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 493358314   4 VVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDV 41
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
PHA02518 PHA02518
ParA-like protein; Provisional
3-247 3.03e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.99  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDfdvglrnldlvmgaerrvvydlvnviqGDAKLTQALIRDKRLET 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVD---------------------------LDPQGSSTDWAEAREEG 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314  83 LFLLPASqtRDKDNLTPEgvewvIAELKKHFDWVICDSPAGIERGATLAMRHADVAVVVTNPEVSSVRDSDRIIGLLDSK 162
Cdd:PHA02518  54 EPLIPVV--RMGKSIRAD-----LPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKAR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314 163 TlkaERGERMEKHLLLTRYDSVRAERGDmlKVDDVLEILSIPLL-GIIPESTDVLRASNVGAPVTLAD----ARCAPAMA 237
Cdd:PHA02518 127 Q---EVTDGLPKFAFIISRAIKNTQLYR--EARKALAGYGLPILrNGTTQRVAYADAAEAGGSVLELPeddkAAEEIIQL 201
                        250
                 ....*....|
gi 493358314 238 YFDAARRLSG 247
Cdd:PHA02518 202 VKELFRGISG 211
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
10-40 9.83e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 39.75  E-value: 9.83e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 493358314  10 GKGGVGKTTSTAALGAALAQNKEKVVVVDFD 40
Cdd:PRK13230   8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCD 38
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
4-151 2.47e-03

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 38.98  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   4 VVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFDVGLRNLDLVMGAERrvVYDLVNVIQGDAKLTQAlIRDKRLETL 83
Cdd:PRK11519 528 VLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNN--VNGLSDILIGQGDITTA-AKPTSIANF 604
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493358314  84 FLLPASQT--RDKDNLTPEGVEWVIAELKKHFDWVICDSPAGIE-RGATLAMRHADVAVVVTNPEVSSVRD 151
Cdd:PRK11519 605 DLIPRGQVppNPSELLMSERFAELVNWASKNYDLVLIDTPPILAvTDAAIVGRHVGTTLMVARYAVNTLKE 675
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
3-40 2.67e-03

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 38.89  E-value: 2.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 493358314   3 KVVVVTSGKGGVGKTTSTAALGAALAQNKEKVVVVDFD 40
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLD 159
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
2-34 3.67e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 38.53  E-value: 3.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 493358314    2 GKVVVVTSGKGGVGKTTSTAALGAALAQNKEKV 34
Cdd:TIGR04291 320 EKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDV 352
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
10-37 6.97e-03

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: 37.11  E-value: 6.97e-03
                         10        20
                 ....*....|....*....|....*...
gi 493358314  10 GKGGVGKTTSTAALGAALAQNKEKVVVV 37
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMGKKVLHV 34
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
5-58 9.77e-03

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 37.01  E-value: 9.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493358314   5 VVVTSGKGGVGKTTSTAALGAALAQNKEKVVVvdFDVGL----------------RNLDLVMGAERRVVY 58
Cdd:COG1797    6 LVIAAPHSGSGKTTVTLGLLAALRRRGLKVQP--FKVGPdyidpgyhtlatgrpsRNLDPFLMGEEGVRE 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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