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Conserved domains on  [gi|1539290271|emb|VDZ51303|]
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Plasmid partition protein A [Serratia odorifera]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 13-104 3.69e-60

ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.


:

Pssm-ID: 436616  Cd Length: 92  Bit Score: 189.55  E-value: 3.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271  13 AEKMLSALTEQIQLQKEELKENEYFQVYSKAAVAKFPKLTRANVDYTVSEMENGGYVFEKRAAGSSTKYAMTVQNIVDIY 92
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 1539290271  93 HHRGVPKYRDRH 104
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 107-392 2.14e-43

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: 151.55  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 107 AMTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVglVETTSAQAMLQNVSreel 186
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 187 LNEFIVPSVVPGVDVLPASIDdafiasgWESLCAEHLPGQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAA 266
Cdd:COG1192    69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 267 DLLMTPIPPAQVDFHSTLKYLTRLPElvsIIEASGCPCRLQGNIGFMSKLSNKPDHKVCHSLaKEIFGGDMLDAALPRLD 346
Cdd:COG1192   141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1539290271 347 GFERCGESFDTVISANPATyvgssealkNARTAAEDFAKAVFDRIE 392
Cdd:COG1192   217 ALAEAPSAGKPVFEYDPKS---------KGAKAYRALAEELLERLE 253
 
Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 13-104 3.69e-60

ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.


Pssm-ID: 436616  Cd Length: 92  Bit Score: 189.55  E-value: 3.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271  13 AEKMLSALTEQIQLQKEELKENEYFQVYSKAAVAKFPKLTRANVDYTVSEMENGGYVFEKRAAGSSTKYAMTVQNIVDIY 92
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 1539290271  93 HHRGVPKYRDRH 104
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 107-392 2.14e-43

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: 151.55  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 107 AMTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVglVETTSAQAMLQNVSreel 186
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 187 LNEFIVPSVVPGVDVLPASIDdafiasgWESLCAEHLPGQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAA 266
Cdd:COG1192    69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 267 DLLMTPIPPAQVDFHSTLKYLTRLPElvsIIEASGCPCRLQGNIGFMSKLSNKPDHKVCHSLaKEIFGGDMLDAALPRLD 346
Cdd:COG1192   141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1539290271 347 GFERCGESFDTVISANPATyvgssealkNARTAAEDFAKAVFDRIE 392
Cdd:COG1192   217 ALAEAPSAGKPVFEYDPKS---------KGAKAYRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 112-275 3.53e-24

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: 98.04  E-value: 3.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 112 VGNLKGGVSKTVSTVSLAHALRahphllFEDLRVLVIDLDPQSSATMflnhtrAVGL----VETTSAQAMLQNVSreelL 187
Cdd:pfam13614   6 IANQKGGVGKTTTSVNLAAALA------KKGKKVLLIDLDPQGNATS------GLGIdknnVEKTIYELLIGECN----I 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 188 NEFIVPSVVPGVDVLPASIDdafiASGWEslcAEHLPGQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:pfam13614  70 EEAIIKTVIENLDLIPSNID----LAGAE---IELIGIENRENILKE-ALEPVKDNYDYIIIDCPPSLGLLTINALTASD 141


                  ....*...
gi 1539290271 268 LLMTPIPP 275
Cdd:pfam13614 142 SVLIPVQC 149
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 108-298 7.05e-24

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: 95.68  E-value: 7.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 108 MTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLnhtravglvettsaqamlqnvsreell 187
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL--------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 188 nefivpsvvpgvdvlpasiddafiasgweslcaehlpgqnphavlreniidklksdYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:cd02042    48 --------------------------------------------------------YDYILIDTPPSLGLLTRNALAAAD 71

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1539290271 268 LLMTPIPPAQVDFHSTLKYLTRLPELVSIIE 298
Cdd:cd02042    72 LVLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 62-301 1.23e-18

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 86.60  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271  62 EMENGGYVfEKRAAgsstkyaMTVQNIVDIYHHRGVPKYRDRHPEAMTLFVGNLKGGVSKTVSTVSLAHALRAHPHllfe 141
Cdd:PHA02519   69 DFETRGRV-ERRAG-------YTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGH---- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 142 dlRVLVID-LDPQSSATMFLNHtraVGLVETTSAQAMLQNVSREELLNEF-IVPSVVPGVDVLPASIDDAFIASGWESL- 218
Cdd:PHA02519  137 --RVLLIEgNDPQGTASMYHGY---VPDLHIHADDTLLPFYLGERDNAEYaIKPTCWPGLDIIPSCLALHRIETDLMQYh 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 219 CAEHLPgQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIE 298
Cdd:PHA02519  212 DAGKLP-HPPHLMLRA-AIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVD 289


                  ...
gi 1539290271 299 ASG 301
Cdd:PHA02519  290 LGG 292
ParA_partition NF041546
ParA family partition ATPase;
114-279 4.09e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 64.88  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 114 NLKGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDPQSSATMFlnhtravglvettsAQAmlqnvsREEllnefivp 193
Cdd:NF041546    6 NQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED-------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 194 svvpgvdvlpasiDDAFIASGweslcaehLPGQNPHavlREniIDKLKSDYDFIFVDSGPHLDAFLKNAIAAADLLMTPI 273
Cdd:NF041546   52 -------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPV 105


                  ....*.
gi 1539290271 274 PPAQVD 279
Cdd:NF041546  106 QPSPYD 111
 
Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 13-104 3.69e-60

ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.


Pssm-ID: 436616  Cd Length: 92  Bit Score: 189.55  E-value: 3.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271  13 AEKMLSALTEQIQLQKEELKENEYFQVYSKAAVAKFPKLTRANVDYTVSEMENGGYVFEKRAAGSSTKYAMTVQNIVDIY 92
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 1539290271  93 HHRGVPKYRDRH 104
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 107-392 2.14e-43

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: 151.55  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 107 AMTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVglVETTSAQAMLQNVSreel 186
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 187 LNEFIVPSVVPGVDVLPASIDdafiasgWESLCAEHLPGQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAA 266
Cdd:COG1192    69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 267 DLLMTPIPPAQVDFHSTLKYLTRLPElvsIIEASGCPCRLQGNIGFMSKLSNKPDHKVCHSLaKEIFGGDMLDAALPRLD 346
Cdd:COG1192   141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1539290271 347 GFERCGESFDTVISANPATyvgssealkNARTAAEDFAKAVFDRIE 392
Cdd:COG1192   217 ALAEAPSAGKPVFEYDPKS---------KGAKAYRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 112-275 3.53e-24

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: 98.04  E-value: 3.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 112 VGNLKGGVSKTVSTVSLAHALRahphllFEDLRVLVIDLDPQSSATMflnhtrAVGL----VETTSAQAMLQNVSreelL 187
Cdd:pfam13614   6 IANQKGGVGKTTTSVNLAAALA------KKGKKVLLIDLDPQGNATS------GLGIdknnVEKTIYELLIGECN----I 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 188 NEFIVPSVVPGVDVLPASIDdafiASGWEslcAEHLPGQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:pfam13614  70 EEAIIKTVIENLDLIPSNID----LAGAE---IELIGIENRENILKE-ALEPVKDNYDYIIIDCPPSLGLLTINALTASD 141


                  ....*...
gi 1539290271 268 LLMTPIPP 275
Cdd:pfam13614 142 SVLIPVQC 149
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 108-298 7.05e-24

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: 95.68  E-value: 7.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 108 MTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLnhtravglvettsaqamlqnvsreell 187
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL--------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 188 nefivpsvvpgvdvlpasiddafiasgweslcaehlpgqnphavlreniidklksdYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:cd02042    48 --------------------------------------------------------YDYILIDTPPSLGLLTRNALAAAD 71

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1539290271 268 LLMTPIPPAQVDFHSTLKYLTRLPELVSIIE 298
Cdd:cd02042    72 LVLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 110-358 5.84e-19

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: 85.09  E-value: 5.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 110 LFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVGLVETTSAQAMLQNVSREELLne 189
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 190 FIVPSVVPGVDVLPASIDDAFIASGWESLCAEHLpgqnphavLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAADLL 269
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNIDLEKFEKELLGPRKEER--------LRE-ALEALKEDYDYVIIDGAPGLGELLRNALIAADYV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 270 MTPIPPAQVDFHStlkyLTRLPELVSIIEASGCPCRLQgNIGFM-SKLSNKPDHKVCHSLAKEIFGGDMLDAALPRLDGF 348
Cdd:pfam01656 144 IIPLEPEVILVED----AKRLGGVIAALVGGYALLGLK-IIGVVlNKVDGDNHGKLLKEALEELLRGLPVLGVIPRDEAV 218

                         250
                  ....*....|
gi 1539290271 349 ERCGESFDTV 358
Cdd:pfam01656 219 AEAPARGLPV 228
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 62-301 1.23e-18

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 86.60  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271  62 EMENGGYVfEKRAAgsstkyaMTVQNIVDIYHHRGVPKYRDRHPEAMTLFVGNLKGGVSKTVSTVSLAHALRAHPHllfe 141
Cdd:PHA02519   69 DFETRGRV-ERRAG-------YTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGH---- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 142 dlRVLVID-LDPQSSATMFLNHtraVGLVETTSAQAMLQNVSREELLNEF-IVPSVVPGVDVLPASIDDAFIASGWESL- 218
Cdd:PHA02519  137 --RVLLIEgNDPQGTASMYHGY---VPDLHIHADDTLLPFYLGERDNAEYaIKPTCWPGLDIIPSCLALHRIETDLMQYh 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 219 CAEHLPgQNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIE 298
Cdd:PHA02519  212 DAGKLP-HPPHLMLRA-AIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVD 289


                  ...
gi 1539290271 299 ASG 301
Cdd:PHA02519  290 LGG 292
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 87-301 1.04e-17

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 83.87  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271  87 NIVDIYHHRGVPKYRDRHPEA---MTLFVGNLKGGVSKTVSTVSLAHalrahpHLLFEDLRVLVID-LDPQSSATMFlnH 162
Cdd:PRK13705   83 TIEQINHMRDVFGTRLRRAEDvfpPVIGVAAHKGGVYKTSVSVHLAQ------DLALKGLRVLLVEgNDPQGTASMY--H 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 163 TRAVGLVETTSAQAMLQNVSREELLNEFIVPSVVPGVDVLPASIDDAFIASGWESLCAEHLPGQNPHAVLREnIIDKLKS 242
Cdd:PRK13705  155 GWVPDLHIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRL-AIETVAH 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1539290271 243 DYDFIFVDSGPHLDAFLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIEASG 301
Cdd:PRK13705  234 DYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKG 292
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 108-290 4.38e-14

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: 72.84  E-value: 4.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 108 MTLFVGnLKGGVSKTVSTVSLAHALRAHPhllfeDLRVLVIDLDPQS-SATMFLNHTRAVGLVEttsaqaMLQNVSR--E 184
Cdd:COG4963   104 VIAVVG-AKGGVGATTLAVNLAWALARES-----GRRVLLVDLDLQFgDVALYLDLEPRRGLAD------ALRNPDRldE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 185 ELLNEFIVPsVVPGVDVLPASIDdafiasgweslcAEHLPGQNPHAVLRenIIDKLKSDYDFIFVDSGPHLDAFLKNAIA 264
Cdd:COG4963   172 TLLDRALTR-HSSGLSVLAAPAD------------LERAEEVSPEAVER--LLDLLRRHFDYVVVDLPRGLNPWTLAALE 236

                         170       180
                  ....*....|....*....|....*....
gi 1539290271 265 AAD---LLMTPIPPAQVDFHSTLKYLTRL 290
Cdd:COG4963   237 AADevvLVTEPDLPSLRNAKRLLDLLREL 265
ParA_partition NF041546
ParA family partition ATPase;
114-279 4.09e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 64.88  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 114 NLKGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDPQSSATMFlnhtravglvettsAQAmlqnvsREEllnefivp 193
Cdd:NF041546    6 NQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED-------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 194 svvpgvdvlpasiDDAFIASGweslcaehLPGQNPHavlREniIDKLKSDYDFIFVDSGPHLDAFLKNAIAAADLLMTPI 273
Cdd:NF041546   52 -------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPV 105


                  ....*.
gi 1539290271 274 PPAQVD 279
Cdd:NF041546  106 QPSPYD 111
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 110-391 8.20e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 66.24  E-value: 8.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 110 LFVGNLKGGVSKTVSTVSLAHalrahpHLLFEDLRVLVIDLDPQSSATMFLNHTRAVGLVETTSAQAMLQNVSREELLNE 189
Cdd:PRK13869  124 IAVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTRRPLRD 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 190 FIVPSVVPGVDVLPASIddafiasgwESLCAEHlpgQNPHAV----LRENI--------IDKLKSDYDFIFVDSGPHLDA 257
Cdd:PRK13869  198 VIRPTYFDGLHLVPGNL---------ELMEFEH---TTPKALsdkgTRDGLfftrvaqaFDEVADDYDVVVIDCPPQLGF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 258 FLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIEASGcpcrlqGNI--GFMSKL------SNKPDHKVChSLA 329
Cdd:PRK13869  266 LTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAG------GNLqyDFIRYLltryepQDAPQTKVA-ALL 338

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539290271 330 KEIFGGDMLDAALPRLDGFERCGESFDTVI-----SANPATYVGSSEALKNARTAAEDFAKAVFDRI 391
Cdd:PRK13869  339 RNMFEDHVLTNPMVKSAAVSDAGLTKQTLYeigreNLTRSTYDRAMESLDAVNSEIEALIKMAWGRA 405
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 116-253 2.03e-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: 60.97  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 116 KGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDP-QSSATMFLNHTRAVGLVETTSAQAMLQNVsreellnefIVPS 194
Cdd:COG0489   101 KGGEGKSTVAANLALALAQ------SGKRVLLIDADLrGPSLHRMLGLENRPGLSDVLAGEASLEDV---------IQPT 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539290271 195 VVPGVDVLPASiddafiasgweslcaehLPGQNPHAVLR----ENIIDKLKSDYDFIFVDSGP 253
Cdd:COG0489   166 EVEGLDVLPAG-----------------PLPPNPSELLAskrlKQLLEELRGRYDYVIIDTPP 211
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 109-272 3.67e-10

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: 59.60  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 109 TLFVGnLKGGVSKTVSTVSLAHALRAHPhllfeDLRVLVIDLD-PQSSATMFLNHTRAVGLVEttsaqaMLQNVSR--EE 185
Cdd:cd03111     3 VAVVG-AKGGVGASTLAVNLAQELAQRA-----KDKVLLIDLDlPFGDLGLYLNLRPDYDLAD------VIQNLDRldRT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 186 LLNEFIVPsVVPGVDVL--PASIDDAfiasgwESLCAEHLpgqnphavlrENIIDKLKSDYDFIFVDSGPHLDAFLKNAI 263
Cdd:cd03111    71 LLDSAVTR-HSSGLSLLpaPQELEDL------EALGAEQV----------DKLLQVLRAFYDHIIVDLGHFLDEVTLAVL 133

                         170
                  ....*....|..
gi 1539290271 264 AAAD---LLMTP 272
Cdd:cd03111   134 EAADeilLVTQQ 145
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 125-289 2.40e-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: 57.21  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 125 TVSLAHALRAHPHllfedlRVLVIDLDPQSsATMflnHTRaVGLVETTSaqamLQNVSREEL-LNEFIVPsVVPGVDVLP 203
Cdd:COG0455     3 AVNLAAALARLGK------RVLLVDADLGL-ANL---DVL-LGLEPKAT----LADVLAGEAdLEDAIVQ-GPGGLDVLP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 204 ASIDdafiASGWESLcaehlpgqNPHAVLREnIIDKLKSDYDFIFVDSGPHLDAFLKNAIAAAD---LLMTPIPPAQVDF 280
Cdd:COG0455    67 GGSG----PAELAEL--------DPEERLIR-VLEELERFYDVVLVDTGAGISDSVLLFLAAADevvVVTTPEPTSITDA 133


                  ....*....
gi 1539290271 281 HSTLKYLTR 289
Cdd:COG0455   134 YALLKLLRR 142
PHA02518 PHA02518
ParA-like protein; Provisional
 108-299 3.17e-09

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 56.40  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 108 MTLFVGNLKGGVSKTVSTVSLAHALRAHPHllfedlRVLVIDLDPQSSAtmflnhtravglveTTSAQAmlqnvsREEll 187
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGH------KVLLVDLDPQGSS--------------TDWAEA------REE-- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 188 nefivpsvvpgvdvlpasIDDAFIASGWESLCAEHLPgqnphavlreniidKLKSDYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:PHA02518   53 ------------------GEPLIPVVRMGKSIRADLP--------------KVASGYDYVVVDGAPQDSELARAALRIAD 100

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539290271 268 LLMTPIPPAQVDFHStlkyltrLPELVSIIEA 299
Cdd:PHA02518  101 MVLIPVQPSPFDIWA-------APDLVELIKA 125
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 116-289 8.83e-08

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: 52.57  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 116 KGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDpqssatmflnhtraVGL----------VETTSAQAMLQNVSREE 185
Cdd:cd02038     9 KGGVGKTNVSANLALALSK------LGKRVLLLDAD--------------LGLanldillglaPKKTLGDVLKGRVSLED 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 186 llnefIVPSVVPGVDVLPASIDDafiaSGWESLCAEHLpgqnphAVLRENIiDKLKSDYDFIFVDSGPHLDAFLKNAIAA 265
Cdd:cd02038    69 -----IIVEGPEGLDIIPGGSGM----EELANLDPEQK------AKLIEEL-SSLESNYDYLLIDTGAGISRNVLDFLLA 132

                         170       180
                  ....*....|....*....|....*..
gi 1539290271 266 AD---LLMTPIPPAQVDFHSTLKYLTR 289
Cdd:cd02038   133 ADeviVVTTPEPTSITDAYALIKVLSR 159
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 121-253 1.12e-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: 48.72  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539290271 121 KTVSTVSLAHALRAhphllfEDLRVLVIDLDP-QSSATMFLNHTRAVGLVETtsaqamlqnVSREELLNEFIVPSVVPGV 199
Cdd:cd05387    33 KSTVAANLAVALAQ------SGKRVLLIDADLrRPSLHRLLGLPNEPGLSEV---------LSGQASLEDVIQSTNIPNL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1539290271 200 DVLPASiddAFIASGWESLCAEHLpgqnphavlrENIIDKLKSDYDFIFVDSGP 253
Cdd:cd05387    98 DVLPAG---TVPPNPSELLSSPRF----------AELLEELKEQYDYVIIDTPP 138
 
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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