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Conserved domains on  [gi|517487917|ref|WP_018658494|]
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ParA family protein [Actinomadura flavalba]

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
ParA_partition super family cl49513
ParA family partition ATPase;
9-203 2.36e-17

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 76.82  E-value: 2.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWARLAGDALPVTVVRHTYDDIADEIGRQAQAHdvv 88
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-QGSALDWAAAREDERPFPVVGLARPTLHRELPSLARDY--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  89 VVDVGGGAPHLLEAAAS---VSDVLLMPLAPAAADARRVAATLASAERgAARNRRGLLAYVVIVRADGRSAEPARWREQM 165
Cdd:NF041546  77 DFVVIDGPPRAEDLARSaikAADLVLIPVQPSPYDLWASADTVDLIKE-AREYTPGLKAAFVLNRAIARTALGREVAEAL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 517487917 166 QRDGHPLVETTIGARVLY--SRAYGTAPSDVG-------EYEALLAE 203
Cdd:NF041546 156 AEYGLPVLKTRIGQRVAFaeSAAEGLTVFEAEpdgkaarEIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
9-203 2.36e-17

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 76.82  E-value: 2.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWARLAGDALPVTVVRHTYDDIADEIGRQAQAHdvv 88
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-QGSALDWAAAREDERPFPVVGLARPTLHRELPSLARDY--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  89 VVDVGGGAPHLLEAAAS---VSDVLLMPLAPAAADARRVAATLASAERgAARNRRGLLAYVVIVRADGRSAEPARWREQM 165
Cdd:NF041546  77 DFVVIDGPPRAEDLARSaikAADLVLIPVQPSPYDLWASADTVDLIKE-AREYTPGLKAAFVLNRAIARTALGREVAEAL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 517487917 166 QRDGHPLVETTIGARVLY--SRAYGTAPSDVG-------EYEALLAE 203
Cdd:NF041546 156 AEYGLPVLKTRIGQRVAFaeSAAEGLTVFEAEpdgkaarEIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 9-166 8.51e-14

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: 8.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWArlagdalpvtvvrhtYDDI-ADeigrqaqahdv 87
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL---------------YDYIlID----------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  88 vvvdvggGAPH---LLEAAASVSDVLLMPLAPAAADARRVAATLASAER-GAARNRRGLLAYVVIVRADGRSAEPARWRE 163
Cdd:cd02042   55 -------TPPSlglLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEElKKQLNPPLLILGILLTRVDPRTKLAREVLE 127


                 ...
gi 517487917 164 QMQ 166
Cdd:cd02042  128 ELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 7-209 1.12e-10

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: 59.10  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   7 PIVITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADP--------------TSQSAHDWarLAGDALPVTVVRHTY- 71
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPqgnltsglgldpddLDPTLYDL--LLDDAPLEDAIVPTEi 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  72 ------------DDIADEIGRQAQAHDVVVVDVGGGAPH--------------LLEAAASVSDVLLMPLAPAAADARRVA 125
Cdd:COG1192   79 pgldlipanidlAGAEIELVSRPGRELRLKRALAPLADDydyilidcppslglLTLNALAAADSVLIPVQPEYLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917 126 ATLASAERGAARNRRGL-LAYVVIVRADGRSAEPARWREQMQRD-GHPLVETTIGARVLYSRAYGT-------APSDVG- 195
Cdd:COG1192  159 QLLETIEEVREDLNPKLeILGILLTMVDPRTRLSREVLEELREEfGDKVLDTVIPRSVALAEAPSAgkpvfeyDPKSKGa 238

                        250
                 ....*....|....*
gi 517487917 196 -EYEALLAEVEQDLA 209
Cdd:COG1192  239 kAYRALAEELLERLE 253
PHA02518 PHA02518
ParA-like protein; Provisional
 9-113 3.49e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 49.08  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWARLAGDALPVTVVRHTYDDIADEIGRQAQAHDVV 88
Cdd:PHA02518   2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDP-QGSSTDWAEAREEGEPLIPVVRMGKSIRADLPKVASGYDYV 80

                         90       100
                 ....*....|....*....|....*
gi 517487917  89 VVDVGGGAPHLLEAAASVSDVLLMP 113
Cdd:PHA02518  81 VVDGAPQDSELARAALRIADMVLIP 105
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 9-46 6.80e-06

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: 44.88  E-value: 6.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 517487917    9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADP 46
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP 40
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 6-45 5.24e-05

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: 42.71  E-value: 5.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 517487917    6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:TIGR01968   2 RVIVITSG--KGGVGKTTTTANLGTALARLGKKVVLIDAD 39
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 18-59 8.00e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.43  E-value: 8.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 517487917    18 GSGKTTSAMFIALRYARSGRRVVVLDADPTSQSAHDWARLAG 59
Cdd:smart00382  12 GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII 53
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
9-203 2.36e-17

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 76.82  E-value: 2.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWARLAGDALPVTVVRHTYDDIADEIGRQAQAHdvv 88
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-QGSALDWAAAREDERPFPVVGLARPTLHRELPSLARDY--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  89 VVDVGGGAPHLLEAAAS---VSDVLLMPLAPAAADARRVAATLASAERgAARNRRGLLAYVVIVRADGRSAEPARWREQM 165
Cdd:NF041546  77 DFVVIDGPPRAEDLARSaikAADLVLIPVQPSPYDLWASADTVDLIKE-AREYTPGLKAAFVLNRAIARTALGREVAEAL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 517487917 166 QRDGHPLVETTIGARVLY--SRAYGTAPSDVG-------EYEALLAE 203
Cdd:NF041546 156 AEYGLPVLKTRIGQRVAFaeSAAEGLTVFEAEpdgkaarEIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 9-166 8.51e-14

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: 8.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWArlagdalpvtvvrhtYDDI-ADeigrqaqahdv 87
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL---------------YDYIlID----------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  88 vvvdvggGAPH---LLEAAASVSDVLLMPLAPAAADARRVAATLASAER-GAARNRRGLLAYVVIVRADGRSAEPARWRE 163
Cdd:cd02042   55 -------TPPSlglLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEElKKQLNPPLLILGILLTRVDPRTKLAREVLE 127


                 ...
gi 517487917 164 QMQ 166
Cdd:cd02042  128 ELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 7-209 1.12e-10

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: 59.10  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   7 PIVITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADP--------------TSQSAHDWarLAGDALPVTVVRHTY- 71
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPqgnltsglgldpddLDPTLYDL--LLDDAPLEDAIVPTEi 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917  72 ------------DDIADEIGRQAQAHDVVVVDVGGGAPH--------------LLEAAASVSDVLLMPLAPAAADARRVA 125
Cdd:COG1192   79 pgldlipanidlAGAEIELVSRPGRELRLKRALAPLADDydyilidcppslglLTLNALAAADSVLIPVQPEYLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917 126 ATLASAERGAARNRRGL-LAYVVIVRADGRSAEPARWREQMQRD-GHPLVETTIGARVLYSRAYGT-------APSDVG- 195
Cdd:COG1192  159 QLLETIEEVREDLNPKLeILGILLTMVDPRTRLSREVLEELREEfGDKVLDTVIPRSVALAEAPSAgkpvfeyDPKSKGa 238

                        250
                 ....*....|....*
gi 517487917 196 -EYEALLAEVEQDLA 209
Cdd:COG1192  239 kAYRALAEELLERLE 253
PHA02518 PHA02518
ParA-like protein; Provisional
 9-113 3.49e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 49.08  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPtSQSAHDWARLAGDALPVTVVRHTYDDIADEIGRQAQAHDVV 88
Cdd:PHA02518   2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDP-QGSSTDWAEAREEGEPLIPVVRMGKSIRADLPKVASGYDYV 80

                         90       100
                 ....*....|....*....|....*
gi 517487917  89 VVDVGGGAPHLLEAAASVSDVLLMP 113
Cdd:PHA02518  81 VVDGAPQDSELARAALRIADMVLIP 105
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 16-46 3.39e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 46.31  E-value: 3.39e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 517487917  16 KGGSGKTT-SAMFIALrYARSGRRVVVLDADP 46
Cdd:COG3640    8 KGGVGKTTlSALLARY-LAEKGKPVLAVDADP 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 8-52 5.59e-06

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: 45.58  E-value: 5.59e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 517487917   8 IVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDADPtsqsAH 52
Cdd:cd02035    2 IIFFGG--KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP----AH 40
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 9-46 6.80e-06

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: 44.88  E-value: 6.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 517487917    9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADP 46
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP 40
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 6-45 7.35e-06

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: 45.27  E-value: 7.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 517487917   6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:cd02036    1 RVIVITSG--KGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 8-45 2.42e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 43.89  E-value: 2.42e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 517487917   8 IVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:COG2894    5 IVVTSG--KGGVGKTTTTANLGTALALLGKKVVLIDAD 40
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 9-84 4.26e-05

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: 43.21  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517487917    9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPTSQSAH-------DWARLAGDALPVTVVRHTYDDIADEIGRQ 81
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHryfenrsATADRTGLSLPTPEHLNLPDNDVAEVPDG 81


                  ...
gi 517487917   82 AQA 84
Cdd:pfam09140  82 ENI 84
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 6-45 5.24e-05

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: 42.71  E-value: 5.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 517487917    6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:TIGR01968   2 RVIVITSG--KGGVGKTTTTANLGTALARLGKKVVLIDAD 39
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
6-66 5.96e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 42.88  E-value: 5.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517487917   6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDADPtsqsAHdwaRLaGDALPVTV 66
Cdd:COG0003    3 TRIIFFTG--KGGVGKTTVAAATALALAERGKRTLLVSTDP----AH---SL-GDVLGTEL 53
minD CHL00175
septum-site determining protein; Validated
 6-45 1.02e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 42.06  E-value: 1.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 517487917   6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:CHL00175  16 RIIVITSG--KGGVGKTTTTANLGMSIARLGYRVALIDAD 53
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 16-61 1.47e-04

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: 41.71  E-value: 1.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 517487917  16 KGGSGKTTSAMFIALRYARSGRRVVVLDADPTSQSAHDWARLAGDA 61
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP 146
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 9-46 2.14e-04

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 41.50  E-value: 2.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 517487917    9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADP 46
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDP 143
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 16-46 2.55e-04

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: 40.79  E-value: 2.55e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 517487917   16 KGGSGKTTSA--MFIALryARSGRRVVVLDADP 46
Cdd:pfam01656   7 KGGVGKTTLAanLARAL--ARRGLRVLLIDLDP 37
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 18-59 3.28e-04

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 41.09  E-value: 3.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 517487917  18 GSGKTTSAMFIALRYARSGRRVVVLDADptsQSAHDWARLAG 59
Cdd:COG3451  214 GSGKSFLLKLLLLQLLRYGARIVIFDPG---GSYEILVRALG 252
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 16-48 3.94e-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: 40.37  E-value: 3.94e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517487917  16 KGGSGKTT-SAMFIALrYARSGRRVVVLDADPTS 48
Cdd:cd02034    8 KGGVGKTTiAALLIRY-LAKKGGKVLAVDADPNS 40
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 16-45 4.97e-04

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: 39.74  E-value: 4.97e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 517487917   16 KGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 6-45 5.97e-04

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: 39.47  E-value: 5.97e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 517487917   6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:cd02038    1 RIIAVTSG--KGGVGKTNVSANLALALSKLGKRVLLLDAD 38
PRK10818 PRK10818
septum site-determining protein MinD;
6-45 6.19e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 39.54  E-value: 6.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 517487917   6 RPIVITLGmlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:PRK10818   3 RIIVVTSG--KGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 16-48 6.36e-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: 40.07  E-value: 6.36e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 517487917   16 KGGSGKTTSAMFIALRYARSGRRVVVLDADPTS 48
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPAS 43
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 16-52 8.94e-04

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 39.26  E-value: 8.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 517487917   16 KGGSGKTTSAMFIALRYARSGRRVVVLDADPtsqsAH 52
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDP----AH 41
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
9-54 2.68e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 37.51  E-value: 2.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADpTSQSAHDW 54
Cdd:PRK13849   3 LLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEAD-ENRPLTRW 47
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 16-45 2.81e-03

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: 37.48  E-value: 2.81e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 517487917  16 KGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:cd02037    9 KGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 18-70 3.39e-03

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: 37.16  E-value: 3.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517487917  18 GSGKTTSAMFIALRYARSGRRVVVLDADPTSQSAH------------DWarLAGDALPVTVVRHT 70
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHrllglpnepglsEV--LSGQASLEDVIQST 92
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 9-48 3.86e-03

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 37.73  E-value: 3.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 517487917   9 VITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPTS 48
Cdd:PRK13869 123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQA 162
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 8-47 5.18e-03

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: 37.02  E-value: 5.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 517487917    8 IVITLGMLKGGSGKTTSAMFIALRYARSGRRVVVLDADPT 47
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADIT 40
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 7-45 6.06e-03

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: 35.10  E-value: 6.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 517487917   7 PIVITLGMlKGGSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:cd01983    1 RVIAVTGG-KGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 5-45 6.09e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 37.11  E-value: 6.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 517487917   5 HRPIVItlgMLKG--GSGKTTSAMFIALRYARSGRRVVVLDAD 45
Cdd:PRK00771  93 LKPQTI---MLVGlqGSGKTTTAAKLARYFKKKGLKVGLVAAD 132
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 18-46 6.78e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 36.08  E-value: 6.78e-03
                          10        20
                  ....*....|....*....|....*....
gi 517487917   18 GSGKTTSAMFIALRYARSGRRVVVLDADP 46
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDV 32
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 18-59 8.00e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.43  E-value: 8.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 517487917    18 GSGKTTSAMFIALRYARSGRRVVVLDADPTSQSAHDWARLAG 59
Cdd:smart00382  12 GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII 53
 
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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