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Conserved domains on  [gi|2320367072|ref|WP_263728240|]
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ParA family protein [Campylobacter sp. RKI_CA19_01116]

Protein Classification

ParA family protein( domain architecture ID 10114212)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division, and to BcsQ, an essential component of the cellulose biosynthesis apparatus

CATH:  3.40.50.300
Gene Ontology:  GO:0005524
PubMed:  28373206|22672910|17161598|2149583
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-158 5.47e-36

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: 123.42  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRstevfidirNSSNLkqnfkhsfdinllnnnfnnelnRYD 80
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG---------SLTSW----------------------LYD 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  81 AIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKN--IILLILINRVSPNPFLIKELNNLI 158
Cdd:cd02042    50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLAREVLEEL 129
 
Name Accession Description Interval E-value
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-158 5.47e-36

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: 123.42  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRstevfidirNSSNLkqnfkhsfdinllnnnfnnelnRYD 80
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG---------SLTSW----------------------LYD 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  81 AIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKN--IILLILINRVSPNPFLIKELNNLI 158
Cdd:cd02042    50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLAREVLEEL 129
ParA_partition NF041546
ParA family partition ATPase;
2-216 6.54e-32

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 115.34  E-value: 6.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQ---------RSTEVFIDIRNSS--NLKQNFKhsfdinllnn 70
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQgsaldwaaaREDERPFPVVGLArpTLHRELP---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  71 nfnNELNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKNIILLILINRVSPNPFL 150
Cdd:NF041546   71 ---SLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320367072 151 IKELNN-LIDYihekketyclnDVFLLESVLYERQAYKRAVIEGKSICEFcDKNDKALMDFEKFYQE 216
Cdd:NF041546  148 GREVAEaLAEY-----------GLPVLKTRIGQRVAFAESAAEGLTVFEA-EPDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-221 1.74e-31

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 114.56  E-value: 1.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRSTEVFIDIRNS-SNLKQNFKHSFDInllNNNFNNELNRY 79
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEgEPLIPVVRMGKSI---RADLPKVASGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  80 DAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKNI-ILLILINRVSPNPFLIKELNNLI 158
Cdd:PHA02518   78 DYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLpKFAFIISRAIKNTQLYREARKAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2320367072 159 DYihekketYCLNdvfLLESVLYERQAYKRAVIEGKSICEFCDKnDKALMDFEKFYQEALQTI 221
Cdd:PHA02518  158 AG-------YGLP---ILRNGTTQRVAYADAAEAGGSVLELPED-DKAAEEIIQLVKELFRGI 209
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-222 2.11e-27

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: 104.94  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRST----------------EVFIDIRNSSNL--KQNFKH- 61
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLtsglgldpddldptlyDLLLDDAPLEDAivPTEIPGl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  62 ----------SFDINLLNNNFNNE---------LNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHML 122
Cdd:COG1192    82 dlipanidlaGAEIELVSRPGRELrlkralaplADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072 123 NVYKEVK-SINKNI-ILLILINRVSPNPFLIKE-LNNLIDYIHEKketyclndvfLLESVLYERQAYKRAVIEGKSICEF 199
Cdd:COG1192   162 ETIEEVReDLNPKLeILGILLTMVDPRTRLSREvLEELREEFGDK----------VLDTVIPRSVALAEAPSAGKPVFEY 231

                         250       260
                  ....*....|....*....|...
gi 2320367072 200 cDKNDKALMDFEKFYQEALQTIK 222
Cdd:COG1192   232 -DPKSKGAKAYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-196 4.72e-17

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: 76.62  E-value: 4.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   3 ISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRS------TEVFID---------IRNSSNLKQ------NFKH 61
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssvegLEGDIApalqalaegLKGRVNLDPillkekSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  62 SFDINLLNNNFNNELN--------------------RYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHM 121
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKellgprkeerlrealealkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2320367072 122 LNVYKEVKSINKNIILLI---LINRVSPNpfliKELNNLIDYIhekkETYCLNDVFLleSVLYERQAYKRAVIEGKSI 196
Cdd:pfam01656 161 GGVIAALVGGYALLGLKIigvVLNKVDGD----NHGKLLKEAL----EELLRGLPVL--GVIPRDEAVAEAPARGLPV 228
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 2-42 7.15e-07

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: 49.21  E-value: 7.15e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRS 42
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQAS 146
 
Name Accession Description Interval E-value
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-158 5.47e-36

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: 123.42  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRstevfidirNSSNLkqnfkhsfdinllnnnfnnelnRYD 80
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG---------SLTSW----------------------LYD 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  81 AIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKN--IILLILINRVSPNPFLIKELNNLI 158
Cdd:cd02042    50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLAREVLEEL 129
ParA_partition NF041546
ParA family partition ATPase;
2-216 6.54e-32

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 115.34  E-value: 6.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQ---------RSTEVFIDIRNSS--NLKQNFKhsfdinllnn 70
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQgsaldwaaaREDERPFPVVGLArpTLHRELP---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  71 nfnNELNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKNIILLILINRVSPNPFL 150
Cdd:NF041546   71 ---SLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320367072 151 IKELNN-LIDYihekketyclnDVFLLESVLYERQAYKRAVIEGKSICEFcDKNDKALMDFEKFYQE 216
Cdd:NF041546  148 GREVAEaLAEY-----------GLPVLKTRIGQRVAFAESAAEGLTVFEA-EPDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-221 1.74e-31

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 114.56  E-value: 1.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRSTEVFIDIRNS-SNLKQNFKHSFDInllNNNFNNELNRY 79
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEgEPLIPVVRMGKSI---RADLPKVASGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  80 DAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLNVYKEVKSINKNI-ILLILINRVSPNPFLIKELNNLI 158
Cdd:PHA02518   78 DYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLpKFAFIISRAIKNTQLYREARKAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2320367072 159 DYihekketYCLNdvfLLESVLYERQAYKRAVIEGKSICEFCDKnDKALMDFEKFYQEALQTI 221
Cdd:PHA02518  158 AG-------YGLP---ILRNGTTQRVAYADAAEAGGSVLELPED-DKAAEEIIQLVKELFRGI 209
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-222 2.11e-27

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: 104.94  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRST----------------EVFIDIRNSSNL--KQNFKH- 61
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLtsglgldpddldptlyDLLLDDAPLEDAivPTEIPGl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  62 ----------SFDINLLNNNFNNE---------LNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHML 122
Cdd:COG1192    82 dlipanidlaGAEIELVSRPGRELrlkralaplADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072 123 NVYKEVK-SINKNI-ILLILINRVSPNPFLIKE-LNNLIDYIHEKketyclndvfLLESVLYERQAYKRAVIEGKSICEF 199
Cdd:COG1192   162 ETIEEVReDLNPKLeILGILLTMVDPRTRLSREvLEELREEFGDK----------VLDTVIPRSVALAEAPSAGKPVFEY 231

                         250       260
                  ....*....|....*....|...
gi 2320367072 200 cDKNDKALMDFEKFYQEALQTIK 222
Cdd:COG1192   232 -DPKSKGAKAYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-196 4.72e-17

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: 76.62  E-value: 4.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   3 ISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRS------TEVFID---------IRNSSNLKQ------NFKH 61
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssvegLEGDIApalqalaegLKGRVNLDPillkekSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  62 SFDINLLNNNFNNELN--------------------RYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHM 121
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKellgprkeerlrealealkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2320367072 122 LNVYKEVKSINKNIILLI---LINRVSPNpfliKELNNLIDYIhekkETYCLNDVFLleSVLYERQAYKRAVIEGKSI 196
Cdd:pfam01656 161 GGVIAALVGGYALLGLKIigvVLNKVDGD----NHGKLLKEAL----EELLRGLPVL--GVIPRDEAVAEAPARGLPV 228
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-118 1.24e-09

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 56.69  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDP-QRSTEVFIDIRNSS--------------NLKQNFKH----- 61
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATadrtglslptpehlNLPDNDVAevpdg 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2320367072  62 -SFDINLLNNNFNNELNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVL 118
Cdd:pfam09140  82 eNIDDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLL 139
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-150 1.29e-09

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: 57.05  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGD-SVLLFDSDPQRST------------------------EVFID---IRNSS 53
Cdd:COG4963   104 VIAVVGAKGGVGATTLAVNLAWALARESGrRVLLVDLDLQFGDvalyldleprrgladalrnpdrldETLLDralTRHSS 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  54 NLK-----QNFKHSFDINLLNNNFNNELNR--YDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIAsqyDVSVLDHMLNVYK 126
Cdd:COG4963   184 GLSvlaapADLERAEEVSPEAVERLLDLLRrhFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP---DLPSLRNAKRLLD 260

                         170       180
                  ....*....|....*....|....*
gi 2320367072 127 EVKSINKNII-LLILINRVSPNPFL 150
Cdd:COG4963   261 LLRELGLPDDkVRLVLNRVPKRGEI 285
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-135 1.70e-09

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: 55.28  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQ--RSTEVFID-----------IRNSSNLKQNFKH------- 61
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgnATSGLGIDknnvektiyelLIGECNIEEAIIKtvienld 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  62 ---------SFDINLLNNNFNNE---------LNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDVSVLDHMLN 123
Cdd:pfam13614  83 lipsnidlaGAEIELIGIENRENilkealepvKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLN 162

                         170
                  ....*....|...
gi 2320367072 124 VYKEVK-SINKNI 135
Cdd:pfam13614 163 TIKLVKkRLNPSL 175
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-38 1.08e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 48.58  E-value: 1.08e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2320367072   1 MIISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-39 6.48e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 48.62  E-value: 6.48e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2320367072   1 MIISICNeKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDP 39
Cdd:COG3640     1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 2-42 7.15e-07

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: 49.21  E-value: 7.15e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRS 42
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQAS 146
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-144 2.90e-06

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: 46.50  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAED-GDSVLLFDSDPQRST-EVFIDIRNSSNLK---QN-------------FKHS- 62
Cdd:cd03111     2 VVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDlGLYLNLRPDYDLAdviQNldrldrtlldsavTRHSs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  63 --------------FDINLLNNNFNNELNR--YDAIIIDTGGRDSKEMRKAMLLSDVIIIPTiasQYDVSVLDHMLNVYK 126
Cdd:cd03111    82 glsllpapqeledlEALGAEQVDKLLQVLRafYDHIIVDLGHFLDEVTLAVLEAADEILLVT---QQDLPSLRNARRLLD 158

                         170       180
                  ....*....|....*....|
gi 2320367072 127 EVKS--INKNIILLILiNRV 144
Cdd:cd03111   159 SLREleGSSDRLRLVL-NRY 177
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-38 2.92e-06

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: 46.34  E-value: 2.92e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:cd02037     2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 9-38 2.98e-06

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: 47.10  E-value: 2.98e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:COG0489   101 KGGEGKSTVAANLALALAQSGKRVLLIDAD 130
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-38 4.67e-06

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: 46.02  E-value: 4.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:cd02038     2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-38 7.36e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 45.80  E-value: 7.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-38 8.61e-06

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: 45.14  E-value: 8.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 2-58 1.29e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 45.44  E-value: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRSTEVFIDIRNSSNLKQN 58
Cdd:PRK13869  123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDVGAN 179
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 2-40 2.08e-05

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: 44.26  E-value: 2.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQ 40
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 9-39 2.57e-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: 44.04  E-value: 2.57e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDP 39
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 2-186 2.82e-05

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


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 43.71  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRSTEVFidiRNSSNLKQNFKHSFDINLLNNN-------FNN 74
Cdd:pfam07015   3 LITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKW---RENALRKGTWDPACEIFNADELplleqayEHA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  75 ELNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDvsvLDHMLNVYKEVKSI----NKNIILLILINRVSPNpfl 150
Cdd:pfam07015  80 EGSGFDYALADTHGGSSELNNTIIASSDLLLIPTMLTPLD---IDEALATYRYVIELllteNLAIPTAILRQRVPVG--- 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2320367072 151 ikELNNLIDYIHEKKETYCLNDvflleSVLYERQAY 186
Cdd:pfam07015 154 --RLTSSQRFCSDMLEQLPVFD-----CPMHERDAF 182
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
2-144 3.20e-05

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 43.68  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQR-----------------STEVFIdIRNSSNLKQNFKHSfd 64
Cdd:PRK13849    3 LLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRpltrwkenalrsntwdpACEVYA-ADELPLLEAAYEDA-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  65 inllnnnfnnELNRYDAIIIDTGGRDSKEMRKAMLLSDVIIIPTIASQYDvsvLDHMLNVYKEVKSI----NKNIILLIL 140
Cdd:PRK13849   80 ----------ELQGFDYALADTHGGSSELNNTIIASSNLLLIPTMLTPLD---IDEALSTYRYVIELllseNLAIPTAIL 146


                  ....
gi 2320367072 141 INRV 144
Cdd:PRK13849  147 RQRV 150
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 16-146 7.27e-05

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: 42.57  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  16 TLAVNLSLRLAEDGDSVLLFDSDPQRST-EVFIDIRNSSNLK-------------QNFKHSFDI---------------- 65
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANlDVLLGLEPKATLAdvlageadledaiVQGPGGLDVlpggsgpaelaeldpe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320367072  66 NLLNNNFNNELNRYDAIIIDTGGRDSKEMRKAMLLSDVIII---PTIASQYDVSVLDHMLNVYKEVKSINkniillILIN 142
Cdd:COG0455    81 ERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVvttPEPTSITDAYALLKLLRRRLGVRRAG------VVVN 154


                  ....
gi 2320367072 143 RVSP 146
Cdd:COG0455   155 RVRS 158
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
9-42 1.92e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.34  E-value: 1.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRS 42
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHS 44
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-48 2.72e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 41.61  E-value: 2.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRSTEVFID 48
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLT 368
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 9-39 2.84e-04

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: 40.81  E-value: 2.84e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDP 39
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDP 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
9-47 4.18e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 40.50  E-value: 4.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRSTEVFI 47
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLL 46
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-39 4.86e-04

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: 39.99  E-value: 4.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2320367072   1 MIISICNeKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDP 39
Cdd:cd02034     1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-38 5.07e-04

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: 39.88  E-value: 5.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSD 38
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-43 8.11e-04

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: 39.09  E-value: 8.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRST 43
Cdd:cd05387    21 VIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPS 62
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 2-43 9.45e-04

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: 38.96  E-value: 9.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2320367072   2 IISICNEKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRST 43
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSV 60
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-59 1.42e-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: 39.30  E-value: 1.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPqrstevfidirnSSNLKQNF 59
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDP------------ASNVGQVF 49
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 9-43 2.11e-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: 38.26  E-value: 2.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2320367072   9 KGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQR-ST 43
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKAdST 43
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 2-43 2.86e-03

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


Pssm-ID: 349753  Cd Length: 329  Bit Score: 37.89  E-value: 2.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2320367072   2 IISICNeKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQRST 43
Cdd:cd02033    33 IIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDT 73
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-40 8.69e-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: 36.51  E-value: 8.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2320367072   1 MIISICNeKGGSGKSTLAVNLSLRLAEDGDSVLLFDSDPQ 40
Cdd:cd02032     1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPK 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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