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Conserved domains on  [gi|2063789493|emb|CAG7572087|]
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ParA family protein MPN_688 [Mycoplasmoides pneumoniae M129]

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 ...
 1-266 5.11e-53

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: 172.74  E-value: 5.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKVIL-DLDGQGNVSASFGQNPERLNNTLIDILLKvpkfngansSIEI 79
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARR---GKRVLLiDLDPQGNLTSGLGLDPDDLDPTLYDLLLD---------DAPL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPV-YEGLDILPCNFELNFADIDIARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEP 158
Cdd:COG1192    70 EDAIVPTeIPGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493 159 DQYSMLGLMRIVETIDTFKEK-NPNLKTI-LVPTKVNMRTRLHNDVIELVKsKAHKNNVAfsEHFVSLTSKSSAAVGYEK 236
Cdd:COG1192   150 EYLSLEGLAQLLETIEEVREDlNPKLEILgILLTMVDPRTRLSREVLEELR-EEFGDKVL--DTVIPRSVALAEAPSAGK 226

                         250       260       270
                  ....*....|....*....|....*....|
gi 2063789493 237 lPISLVSPTSnkKYQTEYLEITKEILNLVN 266
Cdd:COG1192   227 -PVFEYDPKS--KGAKAYRALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-266 5.11e-53

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: 172.74  E-value: 5.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKVIL-DLDGQGNVSASFGQNPERLNNTLIDILLKvpkfngansSIEI 79
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARR---GKRVLLiDLDPQGNLTSGLGLDPDDLDPTLYDLLLD---------DAPL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPV-YEGLDILPCNFELNFADIDIARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEP 158
Cdd:COG1192    70 EDAIVPTeIPGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493 159 DQYSMLGLMRIVETIDTFKEK-NPNLKTI-LVPTKVNMRTRLHNDVIELVKsKAHKNNVAfsEHFVSLTSKSSAAVGYEK 236
Cdd:COG1192   150 EYLSLEGLAQLLETIEEVREDlNPKLEILgILLTMVDPRTRLSREVLEELR-EEFGDKVL--DTVIPRSVALAEAPSAGK 226

                         250       260       270
                  ....*....|....*....|....*....|
gi 2063789493 237 lPISLVSPTSnkKYQTEYLEITKEILNLVN 266
Cdd:COG1192   227 -PVFEYDPKS--KGAKAYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-209 3.28e-35

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: 125.92  E-value: 3.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   3 ISFVNNKGGVLKTTMATNVAGSLVKLcpEQRKVILDLDGQGNVSASFGqNPERLNNTLIDIllkvpkFNGANSSIEIDDC 82
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR--GLRVLLIDLDPQSNNSSVEG-LEGDIAPALQAL------AEGLKGRVNLDPI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  83 LLPV---YEGLDILPCNFELNFADIDiARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:pfam01656  72 LLKEksdEGGLDLIPGNIDLEKFEKE-LLGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPE 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2063789493 160 QYSMLGLMRIVETIDTFKEKNPNLK---TILVPTKV--NMRTRLHNDVIELVKSK 209
Cdd:pfam01656 151 VILVEDAKRLGGVIAALVGGYALLGlkiIGVVLNKVdgDNHGKLLKEALEELLRG 205
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-207 1.97e-27

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: 102.62  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKV-ILDLDGQGNVSASFgqnperlnntlidillkvpkfnganssiei 79
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR---GKRVlLIDLDPQGSLTSWL------------------------------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 ddcllpvyegldilpcnfelnfadidiarkkykasdiaeivkqltrrYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:cd02042    48 -----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPS 80

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2063789493 160 QYSMLGLMRIVETIDTFKE--KNPNLKTILVPTKVNMRTRLHNDVIELVK 207
Cdd:cd02042    81 PFDLDGLAKLLDTLEELKKqlNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
2-208 2.36e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 88.76  E-value: 2.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKlcpEQRKVIL-DLDGQGnvSASfgqnperlnntlidillkvpKFNGANSsieiD 80
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALAR---RGYRVLLvDADPQG--SAL--------------------DWAAARE----D 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  81 DCLLPVyegldilpcnfelnfadIDIARkkykaSDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPDQ 160
Cdd:NF041546   52 ERPFPV-----------------VGLAR-----PTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSP 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2063789493 161 YSMLGLMRIVETIDTFKEKNPNLKTILVPTKVNMRTRLHNDVIELVKS 208
Cdd:NF041546  110 YDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTALGREVAEALAE 157
PHA02518 PHA02518
ParA-like protein; Provisional
 1-220 4.68e-12

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 63.72  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAgslVKLCPEQRKVIL-DLDGQGNvSASFGQnpERlnntlidillkvpkfnganssiEI 79
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLA---SWLHADGHKVLLvDLDPQGS-STDWAE--AR----------------------EE 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPVYEgldilpcnfelnfadidiarkkyKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:PHA02518   53 GEPLIPVVR-----------------------MGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPS 109

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493 160 QYSMLGLMRIVETIDTFKEKNPNL-KTILVPTKVNMRTRLHNDV--------IELVKSKAHkNNVAFSEH 220
Cdd:PHA02518  110 PFDIWAAPDLVELIKARQEVTDGLpKFAFIISRAIKNTQLYREArkalagygLPILRNGTT-QRVAYADA 178
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 2-167 2.32e-11

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: 63.07  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVklCPEQRKVILDLDGQGNVSASFGQNPE---RLNNTLIDillkvpkfngansSIE 78
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLA--LRGYRVLAIDLDPQASLSALFGYQPEfdvGENETLYG-------------AIR 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  79 IDDCLLPVYE--------GLDILPCNFELNFADIDIAR---KKYKASDI-----AEIVKQLTRRYDFVLLDTPPNMATLV 142
Cdd:TIGR03453 171 YDDERRPISEiirktyfpGLDLVPGNLELMEFEHETPRalsRGQGGDTIffarvGEALAEVEDDYDVVVIDCPPQLGFLT 250

                         170       180
                  ....*....|....*....|....*
gi 2063789493 143 STAMSLSDVIVIPFEPdqySMLGLM 167
Cdd:TIGR03453 251 LSALCAATGVLITVHP---QMLDVM 272
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-266 5.11e-53

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: 172.74  E-value: 5.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKVIL-DLDGQGNVSASFGQNPERLNNTLIDILLKvpkfngansSIEI 79
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARR---GKRVLLiDLDPQGNLTSGLGLDPDDLDPTLYDLLLD---------DAPL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPV-YEGLDILPCNFELNFADIDIARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEP 158
Cdd:COG1192    70 EDAIVPTeIPGLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493 159 DQYSMLGLMRIVETIDTFKEK-NPNLKTI-LVPTKVNMRTRLHNDVIELVKsKAHKNNVAfsEHFVSLTSKSSAAVGYEK 236
Cdd:COG1192   150 EYLSLEGLAQLLETIEEVREDlNPKLEILgILLTMVDPRTRLSREVLEELR-EEFGDKVL--DTVIPRSVALAEAPSAGK 226

                         250       260       270
                  ....*....|....*....|....*....|
gi 2063789493 237 lPISLVSPTSnkKYQTEYLEITKEILNLVN 266
Cdd:COG1192   227 -PVFEYDPKS--KGAKAYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-209 3.28e-35

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: 125.92  E-value: 3.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   3 ISFVNNKGGVLKTTMATNVAGSLVKLcpEQRKVILDLDGQGNVSASFGqNPERLNNTLIDIllkvpkFNGANSSIEIDDC 82
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR--GLRVLLIDLDPQSNNSSVEG-LEGDIAPALQAL------AEGLKGRVNLDPI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  83 LLPV---YEGLDILPCNFELNFADIDiARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:pfam01656  72 LLKEksdEGGLDLIPGNIDLEKFEKE-LLGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPE 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2063789493 160 QYSMLGLMRIVETIDTFKEKNPNLK---TILVPTKV--NMRTRLHNDVIELVKSK 209
Cdd:pfam01656 151 VILVEDAKRLGGVIAALVGGYALLGlkiIGVVLNKVdgDNHGKLLKEALEELLRG 205
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-184 1.10e-33

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: 120.38  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKLcpEQRKVILDLDGQGNVSASFGQNPERLNNTLIDILLKVpkfnganssIEIDD 81
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKK--GKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGE---------CNIEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  82 CLLP-VYEGLDILPCNFELNFADIDIARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPDQ 160
Cdd:pfam13614  72 AIIKtVIENLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEY 151

                         170       180
                  ....*....|....*....|....*
gi 2063789493 161 YSMLGLMRIVETIDTFKEK-NPNLK 184
Cdd:pfam13614 152 YALEGLSQLLNTIKLVKKRlNPSLE 176
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-207 1.97e-27

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: 102.62  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKV-ILDLDGQGNVSASFgqnperlnntlidillkvpkfnganssiei 79
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR---GKRVlLIDLDPQGSLTSWL------------------------------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 ddcllpvyegldilpcnfelnfadidiarkkykasdiaeivkqltrrYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:cd02042    48 -----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPS 80

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2063789493 160 QYSMLGLMRIVETIDTFKE--KNPNLKTILVPTKVNMRTRLHNDVIELVK 207
Cdd:cd02042    81 PFDLDGLAKLLDTLEELKKqlNPPLLILGILLTRVDPRTKLAREVLEELK 130
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-204 2.03e-21

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: 92.10  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKLcpEQRKVIL-DLDGQ-GNVSASFGQNPERlnnTLIDILlkvpkfnganSSIE- 78
Cdd:COG4963   104 VIAVVGAKGGVGATTLAVNLAWALARE--SGRRVLLvDLDLQfGDVALYLDLEPRR---GLADAL----------RNPDr 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  79 -----IDDCLLPVYEGLDILPcnFELNFADIDIARkkykASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIV 153
Cdd:COG4963   169 ldetlLDRALTRHSSGLSVLA--APADLERAEEVS----PEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVV 242

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2063789493 154 IPFEPDqysMLGLMRIVETIDTFKEKNPNL-KTILVPTKVNMRTRLHNDVIE 204
Cdd:COG4963   243 LVTEPD---LPSLRNAKRLLDLLRELGLPDdKVRLVLNRVPKRGEISAKDIE 291
ParA_partition NF041546
ParA family partition ATPase;
2-208 2.36e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 88.76  E-value: 2.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKlcpEQRKVIL-DLDGQGnvSASfgqnperlnntlidillkvpKFNGANSsieiD 80
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALAR---RGYRVLLvDADPQG--SAL--------------------DWAAARE----D 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  81 DCLLPVyegldilpcnfelnfadIDIARkkykaSDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPDQ 160
Cdd:NF041546   52 ERPFPV-----------------VGLAR-----PTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSP 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2063789493 161 YSMLGLMRIVETIDTFKEKNPNLKTILVPTKVNMRTRLHNDVIELVKS 208
Cdd:NF041546  110 YDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTALGREVAEALAE 157
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 16-194 3.38e-16

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: 75.31  E-value: 3.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  16 TMATNVAGSLVKLcpEQRKVILDLD-GQGNVSASFGQNPERlnnTLIDILlkvpkfngaNSSIEIDDCLLPVYEGLDILP 94
Cdd:COG0455     1 TVAVNLAAALARL--GKRVLLVDADlGLANLDVLLGLEPKA---TLADVL---------AGEADLEDAIVQGPGGLDVLP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  95 CNFELN-FADIDiarkkyKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPDQYSmlgLMRIVETI 173
Cdd:COG0455    67 GGSGPAeLAELD------PEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTS---ITDAYALL 137

                         170       180
                  ....*....|....*....|.
gi 2063789493 174 DTFKEKNPNLKTILVptkVNM 194
Cdd:COG0455   138 KLLRRRLGVRRAGVV---VNR 155
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-246 2.30e-12

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: 64.90  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKV-ILDLD-GQGNVSASFGQNPERlnnTLIDILlkvpkfngaNSSIEI 79
Cdd:cd02038     2 IIAVTSGKGGVGKTNVSANLALALSKL---GKRVlLLDADlGLANLDILLGLAPKK---TLGDVL---------KGRVSL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPVYEGLDILP--CNFElNFADIDIARKKykasDIAEIVKQLTRRYDFVLLDTPPNMA-TLVSTAMSLSDVIVI-- 154
Cdd:cd02038    67 EDIIVEGPEGLDIIPggSGME-ELANLDPEQKA----KLIEELSSLESNYDYLLIDTGAGISrNVLDFLLAADEVIVVtt 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493 155 PfEP----DQYSMLGLMrivetidTFKEKNPNLKTIlvptkVNMrTRLHNDVIELVK--SKAHKNNVAFSEHFV---SLT 225
Cdd:cd02038   142 P-EPtsitDAYALIKVL-------SRRGGKKNFRLI-----VNM-ARSPKEGRATFErlKKVAKRFLDINLDFVgfiPYD 207

                         250       260
                  ....*....|....*....|.
gi 2063789493 226 SKSSAAVgYEKLPISLVSPTS 246
Cdd:cd02038   208 QSVRRAV-RSQKPFVLLFPNS 227
PHA02518 PHA02518
ParA-like protein; Provisional
 1-220 4.68e-12

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 63.72  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAgslVKLCPEQRKVIL-DLDGQGNvSASFGQnpERlnntlidillkvpkfnganssiEI 79
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLA---SWLHADGHKVLLvDLDPQGS-STDWAE--AR----------------------EE 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPVYEgldilpcnfelnfadidiarkkyKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:PHA02518   53 GEPLIPVVR-----------------------MGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPS 109

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493 160 QYSMLGLMRIVETIDTFKEKNPNL-KTILVPTKVNMRTRLHNDV--------IELVKSKAHkNNVAFSEH 220
Cdd:PHA02518  110 PFDIWAAPDLVELIKARQEVTDGLpKFAFIISRAIKNTQLYREArkalagygLPILRNGTT-QRVAYADA 178
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 2-167 2.32e-11

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: 63.07  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVklCPEQRKVILDLDGQGNVSASFGQNPE---RLNNTLIDillkvpkfngansSIE 78
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLA--LRGYRVLAIDLDPQASLSALFGYQPEfdvGENETLYG-------------AIR 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  79 IDDCLLPVYE--------GLDILPCNFELNFADIDIAR---KKYKASDI-----AEIVKQLTRRYDFVLLDTPPNMATLV 142
Cdd:TIGR03453 171 YDDERRPISEiirktyfpGLDLVPGNLELMEFEHETPRalsRGQGGDTIffarvGEALAEVEDDYDVVVIDCPPQLGFLT 250

                         170       180
                  ....*....|....*....|....*
gi 2063789493 143 STAMSLSDVIVIPFEPdqySMLGLM 167
Cdd:TIGR03453 251 LSALCAATGVLITVHP---QMLDVM 272
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 9-183 4.42e-10

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: 59.04  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   9 KGGVLKTTMATNVAGSLVKLcpeQRKVIL-DLDGQG-NVSASFGQNPERlnnTLIDILLkvpkfnganSSIEIDDCLLPV 86
Cdd:COG0489   101 KGGEGKSTVAANLALALAQS---GKRVLLiDADLRGpSLHRMLGLENRP---GLSDVLA---------GEASLEDVIQPT 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  87 -YEGLDILPCNFELNFADIDIARKKykasdIAEIVKQLTRRYDFVLLDTPPNMA-TLVSTAMSLSDVIVIPFEPDQysmL 164
Cdd:COG0489   166 eVEGLDVLPAGPLPPNPSELLASKR-----LKQLLEELRGRYDYVIIDTPPGLGvADATLLASLVDGVLLVVRPGK---T 237

                         170
                  ....*....|....*....
gi 2063789493 165 GLMRIVETIDTFKEKNPNL 183
Cdd:COG0489   238 ALDDVRKALEMLEKAGVPV 256
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-188 4.49e-09

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


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 55.54  E-value: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKLcpEQRKVILDLDGQGNVSASFGQN-PERLNNTLIDilLKVPKFNGANSSIEID 80
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYK--GARVAAIDLDLRQRTFHRYFENrSATADRTGLS--LPTPEHLNLPDNDVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  81 dcllpVYEGLDILPCNFELNFADidiarkkykasdiaeivkqLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEpDQ 160
Cdd:pfam09140  78 -----VPDGENIDDARLEEAFAD-------------------LEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLN-DS 132

                         170       180
                  ....*....|....*....|....*...
gi 2063789493 161 YSMLGLMRIVETiDTFKEKNPNLKTILV 188
Cdd:pfam09140 133 FVDFDLLGQVDP-ETFKVKRPSFYAEMV 159
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-187 1.44e-08

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: 53.82  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKlcPEQRKVIL-DLDGQ-GNVSASFGQNPERlnnTLIDILlkvpkfngANSS--- 76
Cdd:cd03111     2 VVAVVGAKGGVGASTLAVNLAQELAQ--RAKDKVLLiDLDLPfGDLGLYLNLRPDY---DLADVI--------QNLDrld 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  77 -IEIDDCLLPVYEGLDILPCNFELNfaDIDIARkkykASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIP 155
Cdd:cd03111    69 rTLLDSAVTRHSSGLSLLPAPQELE--DLEALG----AEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLV 142

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2063789493 156 FEPDQYSMLGLMRIVETIDTFKEKNPNLKTIL 187
Cdd:cd03111   143 TQQDLPSLRNARRLLDSLRELEGSSDRLRLVL 174
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 2-158 5.64e-08

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 53.14  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVklCPEQRKVILDLDGQGNVSASFGQNPE---RLNNTLIDILlkvpKFNGANSSIE 78
Cdd:PRK13869  123 VIAVTNFKGGSGKTTTSAHLAQYLA--LQGYRVLAVDLDPQASLSALLGVLPEtdvGANETLYAAI----RYDDTRRPLR 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  79 idDCLLPVY-EGLDILPCNFELnfadIDIARKKYKA------------SDIAEIVKQLTRRYDFVLLDTPPNMATLVSTA 145
Cdd:PRK13869  197 --DVIRPTYfDGLHLVPGNLEL----MEFEHTTPKAlsdkgtrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSG 270

                         170
                  ....*....|...
gi 2063789493 146 MSLSDVIVIPFEP 158
Cdd:PRK13869  271 LCAATSMVITVHP 283
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 1-169 3.88e-07

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: 49.73  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVKLcpEQRKVILDLD-GQGNVSASFGQnpERLNNTLIDILlkvpkfngaNSSIEI 79
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKL--GKKVLALDADiTMANLELILGM--EDKPVTLHDVL---------AGEADI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPVYEGLDILPCNFELNfadidiARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:TIGR01969  68 KDAIYEGPFGVKVIPAGVSLE------GLRKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE 141

                         170
                  ....*....|
gi 2063789493 160 QYSMLGLMRI 169
Cdd:TIGR01969 142 ISSITDALKT 151
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-149 2.95e-06

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: 46.79  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGgvlKTTMATNVAGSLVKlcpEQRKVIL-DLDG-QGNVSASFGQNPERlnnTLIDILlkvpkfngaNSSIE 78
Cdd:cd05387    23 AVTSASPGEG---KSTVAANLAVALAQ---SGKRVLLiDADLrRPSLHRLLGLPNEP---GLSEVL---------SGQAS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2063789493  79 IDDCLLP-VYEGLDILPCN------FELnfadidIARKKykasdIAEIVKQLTRRYDFVLLDTPPNMAtlVSTAMSLS 149
Cdd:cd05387    85 LEDVIQStNIPNLDVLPAGtvppnpSEL------LSSPR-----FAELLEELKEQYDYVIIDTPPVLA--VADALILA 149
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-183 4.54e-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: 46.43  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   2 IISFVNNKGGVLKTTMATNVAGSLVKLcpeQRKVIL-DLD-GQGNVSASFGQNpERLNNTLIDILlkvpkfngaNSSIEI 79
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKL---GKKVLLiDADiGLRNLDLILGLE-NRIVYTLVDVL---------EGECRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLL--PVYEGLDILPCNFElnfadidiaRKKYKAS--DIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIP 155
Cdd:cd02036    69 EQALIkdKRWENLYLLPASQT---------RDKDALTpeKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIV 139

                         170       180
                  ....*....|....*....|....*...
gi 2063789493 156 FEPDQYSMLGLMRIVETIDTFKEKNPNL 183
Cdd:cd02036   140 TNPEISSVRDADRVIGLLESKGIVNIGL 167
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 89-159 2.16e-04

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


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 41.59  E-value: 2.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063789493  89 GLDILPCNfELNFADI-DIARKKYKASDIAEIVKQLTRRYDFVLLDTPPNMATLVSTAMSLSDVIVIPFEPD 159
Cdd:pfam06564  78 GLDLLPFG-RLSVEEQeNLQQLQPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD 148
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 1-174 4.52e-04

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 41.15  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493   1 MIISFVNNKGGVLKTTMATNVAGSLVklCPEQRKVILD-LDGQGNVSASFGQNPERlnntlidillkvpkfngansSIEI 79
Cdd:PHA02519  107 VVLAVMSHKGGVYKTSSAVHTAQWLA--LQGHRVLLIEgNDPQGTASMYHGYVPDL--------------------HIHA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063789493  80 DDCLLPVY----------------EGLDILPCNFELNFADIDIArkKYKASDIAEIVKQLTRR---------YDFVLLDT 134
Cdd:PHA02519  165 DDTLLPFYlgerdnaeyaikptcwPGLDIIPSCLALHRIETDLM--QYHDAGKLPHPPHLMLRaaiesvwdnYDIIVIDS 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2063789493 135 PPNMATLVSTAMSLSDVIVIPFEPDQYSMLG-------LMRIVETID 174
Cdd:PHA02519  243 APNLGTGTINVVCAADVIVVATPAELFDYVSvlqfftmLLDLLATVD 289
 
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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