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Conserved domains on  [gi|746466169|ref|WP_039505235|]
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MULTISPECIES: ParA family protein [Enterobacteriaceae]

Protein Classification

ParA family protein( domain architecture ID 11439703)

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-196 6.34e-19

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: 81.83  E-value: 6.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   1 MIPYSVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDIAKA-----------NGSPLPFLVVKS---- 65
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDdldptlydlllDDAPLEDAIVPTeipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169  66 ---------LSEIN--------------------RDEIDAVVFDHSPGVNPGGQLAPI----VIVPTILDAAS-HSI--- 108
Cdd:COG1192   81 ldlipanidLAGAEielvsrpgrelrlkralaplADDYDYILIDCPPSLGLLTLNALAaadsVLIPVQPEYLSlEGLaql 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169 109 --TIKSVHElDGTDKLCI--VIPNRVELQNREHKDLLEM---QF-ENV--PYMKKRVSYSRAYGMGVTIY-----SEGtg 173
Cdd:COG1192  161 leTIEEVRE-DLNPKLEIlgILLTMVDPRTRLSREVLEElreEFgDKVldTVIPRSVALAEAPSAGKPVFeydpkSKG-- 237

                        250       260
                 ....*....|....*....|...
gi 746466169 174 lpnlgitRQEFDGVAKYIHKRIE 196
Cdd:COG1192  238 -------AKAYRALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-196 6.34e-19

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: 81.83  E-value: 6.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   1 MIPYSVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDIAKA-----------NGSPLPFLVVKS---- 65
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDdldptlydlllDDAPLEDAIVPTeipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169  66 ---------LSEIN--------------------RDEIDAVVFDHSPGVNPGGQLAPI----VIVPTILDAAS-HSI--- 108
Cdd:COG1192   81 ldlipanidLAGAEielvsrpgrelrlkralaplADDYDYILIDCPPSLGLLTLNALAaadsVLIPVQPEYLSlEGLaql 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169 109 --TIKSVHElDGTDKLCI--VIPNRVELQNREHKDLLEM---QF-ENV--PYMKKRVSYSRAYGMGVTIY-----SEGtg 173
Cdd:COG1192  161 leTIEEVRE-DLNPKLEIlgILLTMVDPRTRLSREVLEElreEFgDKVldTVIPRSVALAEAPSAGKPVFeydpkSKG-- 237

                        250       260
                 ....*....|....*....|...
gi 746466169 174 lpnlgitRQEFDGVAKYIHKRIE 196
Cdd:COG1192  238 -------AKAYRALAEELLERLE 253
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 4-143 2.76e-17

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: 74.50  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   4 YSVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSdiakangsplpflvvkslseinrdeIDAVVFDHSP 83
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-------------------------YDYILIDTPP 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746466169  84 GVNPGGQLA----PIVIVPTILDAAS-HSI-----TIKSVHELDGTDKLCI-VIPNRVELQNREHKDLLEM 143
Cdd:cd02042   58 SLGLLTRNAlaaaDLVLIPVQPSPFDlDGLaklldTLEELKKQLNPPLLILgILLTRVDPRTKLAREVLEE 128
ParA_partition NF041546
ParA family partition ATPase;
5-189 4.69e-14

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 67.58  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAticSDIAKANGSPLPFLVVKSLSEINRDEI-------DAV 77
Cdd:NF041546   3 AVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA---LDWAAAREDERPFPVVGLARPTLHRELpslardyDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169  78 VFDHSPGVN----PGGQLAPIVIVP---TILDAASHSITIKSVHE----LDGTdKLCIVIpNRVELQNREHKDLLE-MQF 145
Cdd:NF041546  80 VIDGPPRAEdlarSAIKAADLVLIPvqpSPYDLWASADTVDLIKEareyTPGL-KAAFVL-NRAIARTALGREVAEaLAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 746466169 146 ENVPYMK----KRVSYSRAYGMGVTIYSEGTGlpnlGITRQEFDGVAK 189
Cdd:NF041546 158 YGLPVLKtrigQRVAFAESAAEGLTVFEAEPD----GKAAREIRALAK 201
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 5-55 1.39e-11

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: 60.68  E-value: 1.39e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 746466169    5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDIAKANG 55
Cdd:pfam13614   5 AIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNV 55
PHA02518 PHA02518
ParA-like protein; Provisional
 5-99 2.04e-11

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 60.63  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDiAKANGSPLpFLVVKSLSEINRD------EIDAVV 78
Cdd:PHA02518   4 AVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAE-AREEGEPL-IPVVRMGKSIRADlpkvasGYDYVV 81

                         90       100
                 ....*....|....*....|....*
gi 746466169  79 FDHSPGVN----PGGQLAPIVIVPT 99
Cdd:PHA02518  82 VDGAPQDSelarAALRIADMVLIPV 106
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 5-41 3.25e-08

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: 52.67  E-value: 3.25e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 746466169    5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQ 41
Cdd:TIGR03453 108 AVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQ 144
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-196 6.34e-19

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: 81.83  E-value: 6.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   1 MIPYSVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDIAKA-----------NGSPLPFLVVKS---- 65
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDdldptlydlllDDAPLEDAIVPTeipg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169  66 ---------LSEIN--------------------RDEIDAVVFDHSPGVNPGGQLAPI----VIVPTILDAAS-HSI--- 108
Cdd:COG1192   81 ldlipanidLAGAEielvsrpgrelrlkralaplADDYDYILIDCPPSLGLLTLNALAaadsVLIPVQPEYLSlEGLaql 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169 109 --TIKSVHElDGTDKLCI--VIPNRVELQNREHKDLLEM---QF-ENV--PYMKKRVSYSRAYGMGVTIY-----SEGtg 173
Cdd:COG1192  161 leTIEEVRE-DLNPKLEIlgILLTMVDPRTRLSREVLEElreEFgDKVldTVIPRSVALAEAPSAGKPVFeydpkSKG-- 237

                        250       260
                 ....*....|....*....|...
gi 746466169 174 lpnlgitRQEFDGVAKYIHKRIE 196
Cdd:COG1192  238 -------AKAYRALAEELLERLE 253
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 4-143 2.76e-17

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: 74.50  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   4 YSVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSdiakangsplpflvvkslseinrdeIDAVVFDHSP 83
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-------------------------YDYILIDTPP 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746466169  84 GVNPGGQLA----PIVIVPTILDAAS-HSI-----TIKSVHELDGTDKLCI-VIPNRVELQNREHKDLLEM 143
Cdd:cd02042   58 SLGLLTRNAlaaaDLVLIPVQPSPFDlDGLaklldTLEELKKQLNPPLLILgILLTRVDPRTKLAREVLEE 128
ParA_partition NF041546
ParA family partition ATPase;
5-189 4.69e-14

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 67.58  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAticSDIAKANGSPLPFLVVKSLSEINRDEI-------DAV 77
Cdd:NF041546   3 AVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA---LDWAAAREDERPFPVVGLARPTLHRELpslardyDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169  78 VFDHSPGVN----PGGQLAPIVIVP---TILDAASHSITIKSVHE----LDGTdKLCIVIpNRVELQNREHKDLLE-MQF 145
Cdd:NF041546  80 VIDGPPRAEdlarSAIKAADLVLIPvqpSPYDLWASADTVDLIKEareyTPGL-KAAFVL-NRAIARTALGREVAEaLAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 746466169 146 ENVPYMK----KRVSYSRAYGMGVTIYSEGTGlpnlGITRQEFDGVAK 189
Cdd:NF041546 158 YGLPVLKtrigQRVAFAESAAEGLTVFEAEPD----GKAAREIRALAK 201
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 5-55 1.39e-11

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: 60.68  E-value: 1.39e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 746466169    5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDIAKANG 55
Cdd:pfam13614   5 AIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNV 55
PHA02518 PHA02518
ParA-like protein; Provisional
 5-99 2.04e-11

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 60.63  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDiAKANGSPLpFLVVKSLSEINRD------EIDAVV 78
Cdd:PHA02518   4 AVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAE-AREEGEPL-IPVVRMGKSIRADlpkvasGYDYVV 81

                         90       100
                 ....*....|....*....|....*
gi 746466169  79 FDHSPGVN----PGGQLAPIVIVPT 99
Cdd:PHA02518  82 VDGAPQDSelarAALRIADMVLIPV 106
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 5-41 3.25e-08

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: 52.67  E-value: 3.25e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 746466169    5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQ 41
Cdd:TIGR03453 108 AVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQ 144
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 8-41 6.16e-08

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: 51.19  E-value: 6.16e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 746466169    8 NFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQ 41
Cdd:pfam01656   5 GTKGGVGKTTLAANLARALARRGLRVLLIDLDPQ 38
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-41 2.25e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 50.06  E-value: 2.25e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 746466169   5 SVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQ 41
Cdd:PRK13869 125 AVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQ 161
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 3-76 5.83e-07

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: 48.93  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169    3 PYSVWNFKGGVGKTHTSLTLSGHLASQGKRVALVDYDPQN------GATICSDIAKANGSPlpflvvkSLSEINRDEIDA 76
Cdd:TIGR04291   4 PYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASnvgqvfGQTIGNKITAIAGVP-------GLFALEIDPQAA 76
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 10-39 1.34e-06

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 47.36  E-value: 1.34e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:COG2894   11 KGGVGKTTTTANLGTALALLGKKVVLIDAD 40
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 10-74 1.11e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 44.77  E-value: 1.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDP-QNgaticsdIAKANGSPLPFLVVKSLSEInRDEI 74
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPnAN-------LAEALGLEVEADLIKPLGEM-RELI 65
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
10-40 2.15e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 44.04  E-value: 2.15e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDP 40
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDP 41
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 10-39 3.05e-05

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: 43.34  E-value: 3.05e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:cd02036    9 KGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 4-85 3.29e-05

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: 43.56  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   4 YSVWNFKGGVGKThtslTLSGHLA-----SQGKRVALVDYDPQNG-ATICSDIAKANGsplpFL-VVKSLSEINRDEIDA 76
Cdd:COG4963  105 IAVVGAKGGVGAT----TLAVNLAwalarESGRRVLLVDLDLQFGdVALYLDLEPRRG----LAdALRNPDRLDETLLDR 176


                 ....*....
gi 746466169  77 VVFDHSPGV 85
Cdd:COG4963  177 ALTRHSSGL 185
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 4-86 5.47e-05

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: 42.65  E-value: 5.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746466169   4 YSVWNFKGGVGKTHTSLTLSGHLASQGK-RVALVDYDPQNGaticsDIA-KANGSPL--PFLVVKSLSEINRDEIDAVVF 79
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPFG-----DLGlYLNLRPDydLADVIQNLDRLDRTLLDSAVT 77


                 ....*..
gi 746466169  80 DHSPGVN 86
Cdd:cd03111   78 RHSSGLS 84
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 10-40 9.07e-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: 42.11  E-value: 9.07e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDP 40
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 10-39 1.26e-04

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: 41.55  E-value: 1.26e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 746466169   10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:TIGR01968  10 KGGVGKTTTTANLGTALARLGKKVVLIDAD 39
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 10-39 1.36e-04

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: 41.33  E-value: 1.36e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:cd02037    9 KGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
10-85 2.18e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 40.89  E-value: 2.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746466169   10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGATICSDIAKANGSPLPFLVVKSLSEinRDEIDAVVFDHSPGV 85
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVE--DVEVEDVVYKGYGGV 81
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 10-39 2.35e-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: 40.63  E-value: 2.35e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:cd02038    9 KGGVGKTNVSANLALALSKLGKRVLLLDAD 38
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
9-39 2.93e-04

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 40.60  E-value: 2.93e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 746466169   9 FKGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:PRK13849   9 FKGGAGKTTALMGLCAALASDGKRVALFEAD 39
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 10-37 3.66e-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: 40.56  E-value: 3.66e-04
                         10        20
                 ....*....|....*....|....*...
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVD 37
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLID 128
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 9-39 4.49e-04

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: 38.18  E-value: 4.49e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 746466169   9 FKGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:cd01983    8 GKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 8-39 5.82e-04

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: 39.48  E-value: 5.82e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 746466169    8 NFKGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:pfam07015   8 SFKGGAGKTTALMGLCSALASDGKRVALFEAD 39
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 10-39 6.97e-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: 39.36  E-value: 6.97e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 746466169   10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 10-76 1.82e-03

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 38.48  E-value: 1.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746466169   10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPqngATICSDIAKANGSPLPFLVVKSLSEInrdEIDA 76
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDP---AHSLSDSFNQKFGHEPTKVKENLSAM---EIDP 69
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 10-45 2.13e-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: 38.27  E-value: 2.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAT 45
Cdd:cd02033   39 KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTT 74
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 10-45 2.68e-03

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 36.93  E-value: 2.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAT 45
Cdd:cd05386    9 KGGVGKSVIASLLAQYLIDKGQPVSCIDTDPVNKTF 44
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 10-54 4.06e-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: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 746466169   10 KGGVGKTHTSLTLSGHLASQGKRVALVDydpqngaticSDIAKAN 54
Cdd:TIGR01969   9 KGGTGKTTITANLGVALAKLGKKVLALD----------ADITMAN 43
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
10-39 4.98e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 36.94  E-value: 4.98e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:PRK11670 116 KGGVGKSSTAVNLALALAAEGAKVGILDAD 145
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 10-40 4.98e-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: 36.72  E-value: 4.98e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDP 40
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
minD CHL00175
septum-site determining protein; Validated
 10-39 5.25e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 37.06  E-value: 5.25e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:CHL00175  24 KGGVGKTTTTANLGMSIARLGYRVALIDAD 53
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 10-45 6.02e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 36.48  E-value: 6.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAT 45
Cdd:PRK13185  10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
PRK10818 PRK10818
septum site-determining protein MinD;
10-39 6.41e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 36.46  E-value: 6.41e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYD 39
Cdd:PRK10818  11 KGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 10-45 6.55e-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: 6.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAT 45
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 10-42 8.07e-03

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: 36.17  E-value: 8.07e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 746466169   10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQN 42
Cdd:TIGR03371  10 RGGVGKTTLTANLASALKLLGEPVLAIDLDPQN 42
chlL CHL00072
photochlorophyllide reductase subunit L
 10-45 8.73e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 36.25  E-value: 8.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 746466169  10 KGGVGKTHTSLTLSGHLASQGKRVALVDYDPQNGAT 45
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDST 43
 
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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