NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2473272039|ref|WP_277595684|]
View 

ParA family protein [Staphylococcus equorum]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 10-231 7.90e-24

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: 96.47  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSQVMDV--YDQEGTVANILEGSGEVK---IHNINDNVD 84
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALA-RRGKRVLLIDLDPQGNLTSGLGLdpDDLDPTLYDLLLDDAPLEdaiVPTEIPGLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  85 LIAGFNRLDDVQEAMVTSERKTMMLYmwlednyEALN--INQYDFVIIDTHNDFGTATKNAMAVSHVTFSPIVPVAFS-D 161
Cdd:COG1192    83 LIPANIDLAGAEIELVSRPGRELRLK-------RALAplADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSlE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473272039 162 AVT-MQERLDEFRADvIDFKTRESYIttdlklIANMVKHNTTNSREFEEHIANNddyiakFPfKEIFNTSI 231
Cdd:COG1192   156 GLAqLLETIEEVRED-LNPKLEILGI------LLTMVDPRTRLSREVLEELREE------FG-DKVLDTVI 212
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 10-231 7.90e-24

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: 96.47  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSQVMDV--YDQEGTVANILEGSGEVK---IHNINDNVD 84
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALA-RRGKRVLLIDLDPQGNLTSGLGLdpDDLDPTLYDLLLDDAPLEdaiVPTEIPGLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  85 LIAGFNRLDDVQEAMVTSERKTMMLYmwlednyEALN--INQYDFVIIDTHNDFGTATKNAMAVSHVTFSPIVPVAFS-D 161
Cdd:COG1192    83 LIPANIDLAGAEIELVSRPGRELRLK-------RALAplADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSlE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473272039 162 AVT-MQERLDEFRADvIDFKTRESYIttdlklIANMVKHNTTNSREFEEHIANNddyiakFPfKEIFNTSI 231
Cdd:COG1192   156 GLAqLLETIEEVRED-LNPKLEILGI------LLTMVDPRTRLSREVLEELREE------FG-DKVLDTVI 212
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 10-212 1.81e-16

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: 73.73  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNfsqvmdvydqegtvanilegsgevkihnindnvdliagf 89
Cdd:cd02042     3 IAVANQKGGVGKTTLAVNLAAALA-LRGKRVLLIDLDPQGS--------------------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  90 nrlddvqeamvtserktmmLYMWLednyealninqYDFVIIDTHNDFGTATKNAMAVSHVTFSPIVPVAFS-DAV-TMQE 167
Cdd:cd02042    43 -------------------LTSWL-----------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDlDGLaKLLD 92

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2473272039 168 RLDEFRaDVIDFKTRESYIttdlklIANMVKHNTTNSREFEEHIA 212
Cdd:cd02042    93 TLEELK-KQLNPPLLILGI------LLTRVDPRTKLAREVLEELK 130
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 10-157 1.47e-14

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: 69.92  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDID--ENCNFSQVMDVYDQEGTVANILEGSGEVK---IHNINDNVD 84
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALA-KKGKKVLLIDLDpqGNATSGLGIDKNNVEKTIYELLIGECNIEeaiIKTVIENLD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473272039  85 LIAGFNRLDDVQEAMVTSERKTMMLymwlednYEALN--INQYDFVIIDTHNDFGTATKNAMAVSHvtfSPIVPV 157
Cdd:pfam13614  83 LIPSNIDLAGAEIELIGIENRENIL-------KEALEpvKDNYDYIIIDCPPSLGLLTINALTASD---SVLIPV 147
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 10-147 2.49e-04

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: 41.64  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDID-ENCNFSQVMDVYDQEGTVANILEGSGEVK--IHNINDNVDLI 86
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALA-KLGKKVLALDADiTMANLELILGMEDKPVTLHDVLAGEADIKdaIYEGPFGVKVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473272039  87 AGFNRLDDVQEAmvTSERktmmlymwLEDNYEALnINQYDFVIIDTHNDFGTATKNAMAVS 147
Cdd:TIGR01969  82 PAGVSLEGLRKA--DPDK--------LEDVLKEI-IDDTDFLLIDAPAGLERDAVTALAAA 131
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 10-231 7.90e-24

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: 96.47  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSQVMDV--YDQEGTVANILEGSGEVK---IHNINDNVD 84
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALA-RRGKRVLLIDLDPQGNLTSGLGLdpDDLDPTLYDLLLDDAPLEdaiVPTEIPGLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  85 LIAGFNRLDDVQEAMVTSERKTMMLYmwlednyEALN--INQYDFVIIDTHNDFGTATKNAMAVSHVTFSPIVPVAFS-D 161
Cdd:COG1192    83 LIPANIDLAGAEIELVSRPGRELRLK-------RALAplADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSlE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473272039 162 AVT-MQERLDEFRADvIDFKTRESYIttdlklIANMVKHNTTNSREFEEHIANNddyiakFPfKEIFNTSI 231
Cdd:COG1192   156 GLAqLLETIEEVRED-LNPKLEILGI------LLTMVDPRTRLSREVLEELREE------FG-DKVLDTVI 212
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 10-212 1.81e-16

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: 73.73  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNfsqvmdvydqegtvanilegsgevkihnindnvdliagf 89
Cdd:cd02042     3 IAVANQKGGVGKTTLAVNLAAALA-LRGKRVLLIDLDPQGS--------------------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  90 nrlddvqeamvtserktmmLYMWLednyealninqYDFVIIDTHNDFGTATKNAMAVSHVTFSPIVPVAFS-DAV-TMQE 167
Cdd:cd02042    43 -------------------LTSWL-----------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDlDGLaKLLD 92

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2473272039 168 RLDEFRaDVIDFKTRESYIttdlklIANMVKHNTTNSREFEEHIA 212
Cdd:cd02042    93 TLEELK-KQLNPPLLILGI------LLTRVDPRTKLAREVLEELK 130
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 10-157 1.47e-14

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: 69.92  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDID--ENCNFSQVMDVYDQEGTVANILEGSGEVK---IHNINDNVD 84
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALA-KKGKKVLLIDLDpqGNATSGLGIDKNNVEKTIYELLIGECNIEeaiIKTVIENLD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473272039  85 LIAGFNRLDDVQEAMVTSERKTMMLymwlednYEALN--INQYDFVIIDTHNDFGTATKNAMAVSHvtfSPIVPV 157
Cdd:pfam13614  83 LIPSNIDLAGAEIELIGIENRENIL-------KEALEpvKDNYDYIIIDCPPSLGLLTINALTASD---SVLIPV 147
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 10-237 3.74e-11

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: 61.21  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSQVM--DVYDQEG--TVANILEGSGE-----VKIHNIN 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALA-RRGLRVLLIDLDPQSNNSSVEglEGDIAPAlqALAEGLKGRVNldpilLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  81 DNVDLIAGFNRLDDvQEAMVTSERKTMMlymwLEDNYEALNiNQYDFVIIDTHNDFGTATKNAMAVSHVTFSPIVPVAFS 160
Cdd:pfam01656  80 GGLDLIPGNIDLEK-FEKELLGPRKEER----LREALEALK-EDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVIL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039 161 --DAVTMQERLDEFRADVIDFKTResyittDLKLIANMVKHNTTNSREFE--EHIANNDDYIAKFPFKEIFNTSIQKKKS 236
Cdd:pfam01656 154 veDAKRLGGVIAALVGGYALLGLK------IIGVVLNKVDGDNHGKLLKEalEELLRGLPVLGVIPRDEAVAEAPARGLP 227


                  .
gi 2473272039 237 I 237
Cdd:pfam01656 228 V 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 24-245 4.41e-09

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: 55.28  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  24 IAFNFAMWLAlEKDKKILGIDIDENC-NFSQVMDVyDQEGTVANILEGSGEVK--IHNINDNVDLIAGFNRLDDVQEamV 100
Cdd:COG0455     2 VAVNLAAALA-RLGKRVLLVDADLGLaNLDVLLGL-EPKATLADVLAGEADLEdaIVQGPGGLDVLPGGSGPAELAE--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039 101 TSERKtmmlymwLEDNYEALnINQYDFVIIDTHNDFGTATKNAMAVSHVTFspIV----PVAFSDAVTMQERLdefradv 176
Cdd:COG0455    78 DPEER-------LIRVLEEL-ERFYDVVLVDTGAGISDSVLLFLAAADEVV--VVttpePTSITDAYALLKLL------- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473272039 177 idfktRESYITTDLKLIANMVKHNTTNSREFE-------EHIANNDDYIAKFPFKEIFNTSIQKKKSIteLLAYPK 245
Cdd:COG0455   141 -----RRRLGVRRAGVVVNRVRSEAEARDVFErleqvaeRFLGVRLRVLGVIPEDPAVREAVRRGRPL--VLAAPD 209
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 16-132 8.59e-08

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: 52.11  E-value: 8.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  16 KGGVGKTDIAFNFAMWLAlEKDKKILGIDID-ENCNFSQVMDVyDQEGTVANILEGSGEVK--IHNIN-DNVDLIAGFNR 91
Cdd:COG0489   101 KGGEGKSTVAANLALALA-QSGKRVLLIDADlRGPSLHRMLGL-ENRPGLSDVLAGEASLEdvIQPTEvEGLDVLPAGPL 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2473272039  92 LDDVQEAMVTSERKTMMlymwlednyEALNiNQYDFVIIDT 132
Cdd:COG0489   179 PPNPSELLASKRLKQLL---------EELR-GRYDYVIIDT 209
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 16-240 1.44e-06

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: 48.08  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  16 KGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSQVMDVydqEGTVANILEGSGEVKIHNINDNVDLIAGFN---RL 92
Cdd:cd02034     8 KGGVGKTTIAALLIRYLA-KKGGKVLAVDADPNSNLAETLGV---EVEKLPLIKTIGDIRERTGAKKGEPPEGMSlnpYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  93 DDVQEAMVTSERKTMMLYM----------------WLEDNYEALNINQYDFVIIDT-----HndFGTATKNamavsHVTF 151
Cdd:cd02034    84 DDIIKEIIVEPDGIDLLVMgrpegggsgcycpvnaLLRELLRHLALKNYEYVVIDMeagieH--LSRGTIR-----AVDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039 152 SPIVPVAFSDAVTMQERLDEFrADVIDFKtresyittDLKLIANMVKHNTTNsrEFEEHIANNDDYIAKFPFKEIFNTSI 231
Cdd:cd02034   157 LIIVIEPSKRSIQTAKRIKEL-AEELGIK--------KIYLIVNKVRNEEEQ--ELIEELLIKLKLIGVIPYDEEIMEAD 225


                  ....*....
gi 2473272039 232 QKKKSITEL 240
Cdd:cd02034   226 LKGKPLFDL 234
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 9-132 6.16e-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: 6.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039   9 FITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDenCNFSQVmdvydqegtvaNILEG-----------SGEVKIH 77
Cdd:cd02038     2 IIAVTSGKGGVGKTNVSANLALALS-KLGKRVLLLDAD--LGLANL-----------DILLGlapkktlgdvlKGRVSLE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2473272039  78 NI----NDNVDLIAGfnRLDDVQEAMVTSERKTMMLymwleDNYEALNiNQYDFVIIDT 132
Cdd:cd02038    68 DIivegPEGLDIIPG--GSGMEELANLDPEQKAKLI-----EELSSLE-SNYDYLLIDT 118
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 10-211 8.94e-06

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: 46.26  E-value: 8.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLALEKDKKILGIDIDEncnfsqvmdvydQEGTVANILegsgevkihNINDN---VDLI 86
Cdd:COG4963   105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDL------------QFGDVALYL---------DLEPRrglADAL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  87 AGFNRLDD--VQEAMVTSERKtmmLY---------MWLEDNYEALNI------NQYDFVIIDTHNDFGTATKNAMAVSHV 149
Cdd:COG4963   164 RNPDRLDEtlLDRALTRHSSG---LSvlaapadleRAEEVSPEAVERlldllrRHFDYVVVDLPRGLNPWTLAALEAADE 240

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473272039 150 tfspIVPVA---FSDAVTMQERLDEFRadvidfktRESYITTDLKLIANMV-KHNTTNSREFEEHI 211
Cdd:COG4963   241 ----VVLVTepdLPSLRNAKRLLDLLR--------ELGLPDDKVRLVLNRVpKRGEISAKDIEEAL 294
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 18-132 9.14e-05

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: 42.17  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  18 GVGKTDIAFNFAMWLALEkDKKILGIDidenCNF--SQVMDVYDQEGT--VANILEGSGEVK--IHNIN-DNVDLIAGFN 90
Cdd:cd05387    30 GEGKSTVAANLAVALAQS-GKRVLLID----ADLrrPSLHRLLGLPNEpgLSEVLSGQASLEdvIQSTNiPNLDVLPAGT 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2473272039  91 RLDDVQEaMVTSERKTMMLYMWLEdnyealninQYDFVIIDT 132
Cdd:cd05387   105 VPPNPSE-LLSSPRFAELLEELKE---------QYDYVIIDT 136
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 10-145 1.60e-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: 41.80  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENC-NFSQVMDVydqEG----TVANILEgsGEVKIHNI----- 79
Cdd:cd02036     3 IVITSGKGGVGKTTTTANLGVALA-KLGKKVLLIDADIGLrNLDLILGL---ENrivyTLVDVLE--GECRLEQAlikdk 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473272039  80 -NDNVDLIAGFNRLDDVqeaMVTSERktmmlymwLEDNYEALnINQYDFVIIDTHNDFGTATKNAMA 145
Cdd:cd02036    77 rWENLYLLPASQTRDKD---ALTPEK--------LEELVKEL-KDSFDFILIDSPAGIESGFINAIA 131
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 10-147 2.49e-04

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: 41.64  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKKILGIDID-ENCNFSQVMDVYDQEGTVANILEGSGEVK--IHNINDNVDLI 86
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALA-KLGKKVLALDADiTMANLELILGMEDKPVTLHDVLAGEADIKdaIYEGPFGVKVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473272039  87 AGFNRLDDVQEAmvTSERktmmlymwLEDNYEALnINQYDFVIIDTHNDFGTATKNAMAVS 147
Cdd:TIGR01969  82 PAGVSLEGLRKA--DPDK--------LEDVLKEI-IDDTDFLLIDAPAGLERDAVTALAAA 131
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 10-131 1.43e-03

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: 39.18  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLALEKDKKILGIDIDEncnfsqvmdvydQEGTVANILEGSGEvkiHNIndnVDLIAGF 89
Cdd:cd03111     3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDL------------PFGDLGLYLNLRPD---YDL---ADVIQNL 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2473272039  90 NRLDDV--QEAMVTSERKTMMLYM--WLEDNYEA--------LNI--NQYDFVIID 131
Cdd:cd03111    65 DRLDRTllDSAVTRHSSGLSLLPApqELEDLEALgaeqvdklLQVlrAFYDHIIVD 120
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 16-49 2.03e-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: 37.03  E-value: 2.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2473272039  16 KGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENC 49
Cdd:cd01983     9 KGGVGKTTLAAALAVALA-AKGYKVLLIDLDDYV 41
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 16-132 3.75e-03

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 38.10  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  16 KGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSqvmDVYDQE--GTVANILEG--------SGEVK--IHNINDNV 83
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLS-ELGKKVLLISTDPAHSLS---DSFNQKfgHEPTKVKENlsameidpNMELEeyWQEVQKYM 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473272039  84 DLIAGFNRLDDVQEAMVTSERKT--MMLYMWLEDNYEALNinqYDFVIIDT 132
Cdd:pfam02374  85 NALLGLRMLEGILAEELASLPGIdeAASFDEFKKYMDEGE---YDVVVFDT 132
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 16-61 4.54e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 38.15  E-value: 4.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2473272039  16 KGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNfsqVMDVYDQE 61
Cdd:TIGR04291  11 KGGVGKTSIACATAINLA-DQGKRVLLVSTDPASN---VGQVFGQT 52
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 16-132 6.61e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 37.07  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  16 KGGVGKTDIAFNFAMWLAlEKDKKILGIDIDENCNFSQVMDV---YDQEGTVANILE------GSGEVKIHNINDNVDli 86
Cdd:COG3640     8 KGGVGKTTLSALLARYLA-EKGKPVLAVDADPNANLAEALGLeveADLIKPLGEMRElikertGAPGGGMFKLNPKVD-- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473272039  87 agfnrlDDVQEAMVTSERKTMML-------------YM--WLEDNYEALNINQYDFVIIDT 132
Cdd:COG3640    85 ------DIPEEYLVEGDGVDLLVmgtieeggsgcycPEnaLLRALLNHLVLGNYEYVVVDM 139
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 10-132 7.69e-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: 36.71  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473272039  10 ITVSMLKGGVGKTDIAFNFAMWLAlEKDKK--ILGIDIdenCNFS--QVMDVYDQEgtvaniLEGSGEVKIHNINDNVDL 85
Cdd:cd02037     3 IAVLSGKGGVGKSTVAVNLALALA-KKGYKvgLLDADI---YGPSipRLLGVEGKP------LHQSEEGIVPVEVGGIKV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473272039  86 IA-GFnrLDDVQEAMV-TSERKTMMLYMWLED-NYEALninqyDFVIIDT 132
Cdd:cd02037    73 MSiGF--LLPEDDAVIwRGPMKSGAIKQFLKDvDWGEL-----DYLIIDL 115
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH