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Conserved domains on  [gi|1597971800|ref|WP_133625159|]
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AAA family ATPase [Erwinia aphidicola]

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 ...
 15-106 4.72e-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: 4.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  15 AGKMLTALTDQIQAQKQEFSEDRYFQVYAKAALSKLPKLTRANVDYAVSEMEENGYVFDKRSAGSSTKYAMTIQNIIDIY 94
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 1597971800  95 HHRGVPKYRDRH 106
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 109-367 5.60e-40

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: 142.69  E-value: 5.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 109 ALTVFIGNLKGGVSKTVSTVSLAHAMRAHphllheDLRILVVDLDPQSSATMFLNHTRAVgmVDTTSAQAMLQNVSreel 188
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 189 IEEFIVPSVVPGVDVLPASIDdafiasgWEQLCLEHLPGQNPHAVLRqNIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAA 268
Cdd:COG1192    69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLK-RALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 269 DVLMTPVPPAQVDFHSTLKYLTRLPElvsIIESSGCECRLLANIGFMSKLSNKADHKMCHSLaKEIFGGDMLDAALPRLD 348
Cdd:COG1192   141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216

                         250
                  ....*....|....*....
gi 1597971800 349 GFERCGESFDTVISANPST 367
Cdd:COG1192   217 ALAEAPSAGKPVFEYDPKS 235
 
Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 15-106 4.72e-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: 4.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  15 AGKMLTALTDQIQAQKQEFSEDRYFQVYAKAALSKLPKLTRANVDYAVSEMEENGYVFDKRSAGSSTKYAMTIQNIIDIY 94
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 1597971800  95 HHRGVPKYRDRH 106
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 109-367 5.60e-40

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: 142.69  E-value: 5.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 109 ALTVFIGNLKGGVSKTVSTVSLAHAMRAHphllheDLRILVVDLDPQSSATMFLNHTRAVgmVDTTSAQAMLQNVSreel 188
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 189 IEEFIVPSVVPGVDVLPASIDdafiasgWEQLCLEHLPGQNPHAVLRqNIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAA 268
Cdd:COG1192    69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLK-RALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 269 DVLMTPVPPAQVDFHSTLKYLTRLPElvsIIESSGCECRLLANIGFMSKLSNKADHKMCHSLaKEIFGGDMLDAALPRLD 348
Cdd:COG1192   141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216

                         250
                  ....*....|....*....
gi 1597971800 349 GFERCGESFDTVISANPST 367
Cdd:COG1192   217 ALAEAPSAGKPVFEYDPKS 235
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 114-277 1.96e-23

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: 96.11  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 114 IGNLKGGVSKTVSTVSLAHAMRahphllHEDLRILVVDLDPQSSATMflnhtrAVGMVDTTSAQAMLQNVSREELIEEFI 193
Cdd:pfam13614   6 IANQKGGVGKTTTSVNLAAALA------KKGKKVLLIDLDPQGNATS------GLGIDKNNVEKTIYELLIGECNIEEAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 194 VPSVVPGVDVLPASIDdafiASGWEqlcLEHLPGQNPHAVLRqNIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMT 273
Cdd:pfam13614  74 IKTVIENLDLIPSNID----LAGAE---IELIGIENRENILK-EALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLI 145


                  ....
gi 1597971800 274 PVPP 277
Cdd:pfam13614 146 PVQC 149
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 111-311 1.71e-22

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: 91.83  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 111 TVFIGNLKGGVSKTVSTVSLAHAmrahphLLHEDLRILVVDLDPQSSATMFLnhtravgmvdttsaqamlqnvsreelie 190
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAA------LALRGKRVLLIDLDPQGSLTSWL---------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 191 efivpsvvpgvdvlpasiddafiasgweqlclehlpgqnphavlrqniveklehdYDFIFIDSGPHLDAFLNNAIAAADV 270
Cdd:cd02042    48 -------------------------------------------------------YDYILIDTPPSLGLLTRNALAAADL 72

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1597971800 271 LMTPVPPAQVDFHSTLKYLTRLPELVSIIESSGCECRLLAN 311
Cdd:cd02042    73 VLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLT 113
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 64-320 9.77e-20

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 90.07  E-value: 9.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  64 EMEENGYVfdKRSAGsstkyaMTIQNIIDIYHHRGVPKYRDRHSEALTVFIGNLKGGVSKTVSTVSLAHAMRAHPHllhe 143
Cdd:PHA02519   69 DFETRGRV--ERRAG------YTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGH---- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 144 dlRILVVD-LDPQSSATMFLNHTRAVGM-VDTTSAQAMLqnvSREELIEEFIVPSVVPGVDVLPASIDDAFIASGWEQL- 220
Cdd:PHA02519  137 --RVLLIEgNDPQGTASMYHGYVPDLHIhADDTLLPFYL---GERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYh 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 221 CLEHLPgQNPHAVLRQNIvEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMTPVPPAQVDFHSTLKYLTRLPELVSIIE 300
Cdd:PHA02519  212 DAGKLP-HPPHLMLRAAI-ESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVD 289

                         250       260
                  ....*....|....*....|..
gi 1597971800 301 SSGCE--CRLLanigfMSKLSN 320
Cdd:PHA02519  290 LGGFEpvVRLL-----LTKYSL 306
ParA_partition NF041546
ParA family partition ATPase;
116-281 4.51e-11

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 61.80  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 116 NLKGGVSKTVSTVSLAHAmrahphlLHED-LRILVVDLDPQSSATMFlnhtravgmvdttsAQAmlqnvsREElieefiv 194
Cdd:NF041546    6 NQKGGVGKTTLATHLAAA-------LARRgYRVLLVDADPQGSALDW--------------AAA------RED------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 195 psvvpgvdvlpasiDDAFIASGweqlclehLPGQNphavLRQNIvEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMTP 274
Cdd:NF041546   52 --------------ERPFPVVG--------LARPT----LHREL-PSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIP 104


                  ....*..
gi 1597971800 275 VPPAQVD 281
Cdd:NF041546  105 VQPSPYD 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 ...
 15-106 4.72e-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: 4.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  15 AGKMLTALTDQIQAQKQEFSEDRYFQVYAKAALSKLPKLTRANVDYAVSEMEENGYVFDKRSAGSSTKYAMTIQNIIDIY 94
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 1597971800  95 HHRGVPKYRDRH 106
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 109-367 5.60e-40

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: 142.69  E-value: 5.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 109 ALTVFIGNLKGGVSKTVSTVSLAHAMRAHphllheDLRILVVDLDPQSSATMFLNHTRAVgmVDTTSAQAMLQNVSreel 188
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 189 IEEFIVPSVVPGVDVLPASIDdafiasgWEQLCLEHLPGQNPHAVLRqNIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAA 268
Cdd:COG1192    69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLK-RALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 269 DVLMTPVPPAQVDFHSTLKYLTRLPElvsIIESSGCECRLLANIGFMSKLSNKADHKMCHSLaKEIFGGDMLDAALPRLD 348
Cdd:COG1192   141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216

                         250
                  ....*....|....*....
gi 1597971800 349 GFERCGESFDTVISANPST 367
Cdd:COG1192   217 ALAEAPSAGKPVFEYDPKS 235
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 114-277 1.96e-23

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: 96.11  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 114 IGNLKGGVSKTVSTVSLAHAMRahphllHEDLRILVVDLDPQSSATMflnhtrAVGMVDTTSAQAMLQNVSREELIEEFI 193
Cdd:pfam13614   6 IANQKGGVGKTTTSVNLAAALA------KKGKKVLLIDLDPQGNATS------GLGIDKNNVEKTIYELLIGECNIEEAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 194 VPSVVPGVDVLPASIDdafiASGWEqlcLEHLPGQNPHAVLRqNIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMT 273
Cdd:pfam13614  74 IKTVIENLDLIPSNID----LAGAE---IELIGIENRENILK-EALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLI 145


                  ....
gi 1597971800 274 PVPP 277
Cdd:pfam13614 146 PVQC 149
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 111-311 1.71e-22

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: 91.83  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 111 TVFIGNLKGGVSKTVSTVSLAHAmrahphLLHEDLRILVVDLDPQSSATMFLnhtravgmvdttsaqamlqnvsreelie 190
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAA------LALRGKRVLLIDLDPQGSLTSWL---------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 191 efivpsvvpgvdvlpasiddafiasgweqlclehlpgqnphavlrqniveklehdYDFIFIDSGPHLDAFLNNAIAAADV 270
Cdd:cd02042    48 -------------------------------------------------------YDYILIDTPPSLGLLTRNALAAADL 72

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1597971800 271 LMTPVPPAQVDFHSTLKYLTRLPELVSIIESSGCECRLLAN 311
Cdd:cd02042    73 VLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLT 113
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 64-320 9.77e-20

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 90.07  E-value: 9.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  64 EMEENGYVfdKRSAGsstkyaMTIQNIIDIYHHRGVPKYRDRHSEALTVFIGNLKGGVSKTVSTVSLAHAMRAHPHllhe 143
Cdd:PHA02519   69 DFETRGRV--ERRAG------YTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGH---- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 144 dlRILVVD-LDPQSSATMFLNHTRAVGM-VDTTSAQAMLqnvSREELIEEFIVPSVVPGVDVLPASIDDAFIASGWEQL- 220
Cdd:PHA02519  137 --RVLLIEgNDPQGTASMYHGYVPDLHIhADDTLLPFYL---GERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYh 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 221 CLEHLPgQNPHAVLRQNIvEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMTPVPPAQVDFHSTLKYLTRLPELVSIIE 300
Cdd:PHA02519  212 DAGKLP-HPPHLMLRAAI-ESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVD 289

                         250       260
                  ....*....|....*....|..
gi 1597971800 301 SSGCE--CRLLanigfMSKLSN 320
Cdd:PHA02519  290 LGGFEpvVRLL-----LTKYSL 306
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 112-360 1.33e-18

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: 83.93  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 112 VFIGNLKGGVSKTVSTVSLAHAMRAHphllheDLRILVVDLDPQSSATMFLNHTRAVGMVDTTSAQAMLQNVSREELIee 191
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 192 FIVPSVVPGVDVLPASIDDAFIASGWEQLCLEHLpgqnphavLRqNIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVL 271
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNIDLEKFEKELLGPRKEER--------LR-EALEALKEDYDYVIIDGAPGLGELLRNALIAADYV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 272 MTPVPPAQVDFHSTLKYLTRLPELVSIIESSGcecrlLANIGFM-SKLSNKADHKMCHSLAKEIFGGDMLDAALPRLDGF 350
Cdd:pfam01656 144 IIPLEPEVILVEDAKRLGGVIAALVGGYALLG-----LKIIGVVlNKVDGDNHGKLLKEALEELLRGLPVLGVIPRDEAV 218

                         250
                  ....*....|
gi 1597971800 351 ERCGESFDTV 360
Cdd:pfam01656 219 AEAPARGLPV 228
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 89-320 4.63e-18

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 85.03  E-value: 4.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  89 NIIDIYHHRGVPKYR-DRHSEALTVFIG--NLKGGVSKTVSTVSLAHAMRAhphllhEDLRILVVD-LDPQSSATMFLNH 164
Cdd:PRK13705   83 TIEQINHMRDVFGTRlRRAEDVFPPVIGvaAHKGGVYKTSVSVHLAQDLAL------KGLRVLLVEgNDPQGTASMYHGW 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 165 TRAVGM--VDTTSAQAMLQNVSREELIEefivPSVVPGVDVLPASIDDAFIASgweQLCLEHLPGQ---NPHAVLRQNIv 239
Cdd:PRK13705  157 VPDLHIhaEDTLLPFYLGEKDDATYAIK----PTCWPGLDIIPSCLALHRIET---ELMGKFDEGKlptDPHLMLRLAI- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 240 EKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMTPVPPAQVDFHSTLKYLTRLPELVSIIESSGCE--CRLLanigfMSK 317
Cdd:PRK13705  229 ETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEpdVRIL-----LTK 303


                  ...
gi 1597971800 318 LSN 320
Cdd:PRK13705  304 YSN 306
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 110-292 6.83e-12

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: 66.29  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 110 LTVFIGnLKGGVSKTVSTVSLAHAMRAHPhllheDLRILVVDLDPQS-SATMFLNHTRAVGMVDttsaqaMLQNVSR--E 186
Cdd:COG4963   104 VIAVVG-AKGGVGATTLAVNLAWALARES-----GRRVLLVDLDLQFgDVALYLDLEPRRGLAD------ALRNPDRldE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 187 ELIEEFIVPsVVPGVDVLPASIDdafiasgweqlcLEHLPGQNPHAVLRqnIVEKLEHDYDFIFIDSGPHLDAFLNNAIA 266
Cdd:COG4963   172 TLLDRALTR-HSSGLSVLAAPAD------------LERAEEVSPEAVER--LLDLLRRHFDYVVVDLPRGLNPWTLAALE 236

                         170       180
                  ....*....|....*....|....*....
gi 1597971800 267 AAD---VLMTPVPPAQVDFHSTLKYLTRL 292
Cdd:COG4963   237 AADevvLVTEPDLPSLRNAKRLLDLLREL 265
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 91-303 1.55e-11

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 65.47  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800  91 IDIYHHRgvpkyrdRHSEALTVF-IGNLKGGVSKTVSTVSLAHamrahpHLLHEDLRILVVDLDPQSSATMFLNHTRAVG 169
Cdd:PRK13869  109 IDFVPHR-------RGSEHLQVIaVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETD 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 170 MVDTTSAQAMLQNVSREELIEEFIVPSVVPGVDVLPASIddafiasgwEQLCLEHlpgQNPHAVLRQNIVEKL------- 242
Cdd:PRK13869  176 VGANETLYAAIRYDDTRRPLRDVIRPTYFDGLHLVPGNL---------ELMEFEH---TTPKALSDKGTRDGLfftrvaq 243

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1597971800 243 -----EHDYDFIFIDSGPHLDAFLNNAIAAADVLMTPVPPAQVDFHSTLKYLTRLPELVSIIESSG 303
Cdd:PRK13869  244 afdevADDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAG 309
ParA_partition NF041546
ParA family partition ATPase;
116-281 4.51e-11

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 61.80  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 116 NLKGGVSKTVSTVSLAHAmrahphlLHED-LRILVVDLDPQSSATMFlnhtravgmvdttsAQAmlqnvsREElieefiv 194
Cdd:NF041546    6 NQKGGVGKTTLATHLAAA-------LARRgYRVLLVDADPQGSALDW--------------AAA------RED------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 195 psvvpgvdvlpasiDDAFIASGweqlclehLPGQNphavLRQNIvEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMTP 274
Cdd:NF041546   52 --------------ERPFPVVG--------LARPT----LHREL-PSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIP 104


                  ....*..
gi 1597971800 275 VPPAQVD 281
Cdd:NF041546  105 VQPSPYD 111
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 127-291 2.28e-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: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 127 TVSLAHAMRAHPHllhedlRILVVDLDPQSsATMflnHTRaVGMVDTTSaqamLQNVSREEL-IEEFIVPsVVPGVDVLP 205
Cdd:COG0455     3 AVNLAAALARLGK------RVLLVDADLGL-ANL---DVL-LGLEPKAT----LADVLAGEAdLEDAIVQ-GPGGLDVLP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 206 ASIDdafiASGWEQLclehlpgqNPHAVLRQnIVEKLEHDYDFIFIDSGPHLDAFLNNAIAAAD---VLMTPVPPAQVDF 282
Cdd:COG0455    67 GGSG----PAELAEL--------DPEERLIR-VLEELERFYDVVLVDTGAGISDSVLLFLAAADevvVVTTPEPTSITDA 133


                  ....*....
gi 1597971800 283 HSTLKYLTR 291
Cdd:COG0455   134 YALLKLLRR 142
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 118-291 2.47e-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: 54.11  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 118 KGGVSKTVSTVSLAHAMRahphllHEDLRILVVDLDpqssatmflnhtraVGM--VDTtsaqaMLQNVSREEL------- 188
Cdd:cd02038     9 KGGVGKTNVSANLALALS------KLGKRVLLLDAD--------------LGLanLDI-----LLGLAPKKTLgdvlkgr 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 189 --IEEFIVpSVVPGVDVLPASIDDafiaSGWEQLCLEHLpgqnphAVLRQNiVEKLEHDYDFIFIDSGPHLDAFLNNAIA 266
Cdd:cd02038    64 vsLEDIIV-EGPEGLDIIPGGSGM----EELANLDPEQK------AKLIEE-LSSLESNYDYLLIDTGAGISRNVLDFLL 131

                         170       180
                  ....*....|....*....|....*...
gi 1597971800 267 AAD---VLMTPVPPAQVDFHSTLKYLTR 291
Cdd:cd02038   132 AADeviVVTTPEPTSITDAYALIKVLSR 159
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 118-255 2.59e-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: 54.81  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 118 KGGVSKTVSTVSLAHAMRAhphllhEDLRILVVDLDP-QSSATMFLNHTRAVGMVDTTSAQAMLQNVsreelieefIVPS 196
Cdd:COG0489   101 KGGEGKSTVAANLALALAQ------SGKRVLLIDADLrGPSLHRMLGLENRPGLSDVLAGEASLEDV---------IQPT 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1597971800 197 VVPGVDVLPASiddafiasgweqlclehLPGQNPHAVLR----QNIVEKLEHDYDFIFIDSGP 255
Cdd:COG0489   166 EVEGLDVLPAG-----------------PLPPNPSELLAskrlKQLLEELRGRYDYVIIDTPP 211
PHA02518 PHA02518
ParA-like protein; Provisional
 114-301 1.89e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 51.39  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 114 IGNLKGGVSKTVSTVSLAhamrahPHLLHEDLRILVVDLDPQSSATMFLNhTRAVGMvDTTSAQAMLQNVSREelieefi 193
Cdd:PHA02518    5 VLNQKGGAGKTTVATNLA------SWLHADGHKVLLVDLDPQGSSTDWAE-AREEGE-PLIPVVRMGKSIRAD------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 194 vpsvvpgvdvlpasiddafiasgweqlclehlpgqnphavlrqniVEKLEHDYDFIFIDSGPHLDAFLNNAIAAADVLMT 273
Cdd:PHA02518   70 ---------------------------------------------LPKVASGYDYVVVDGAPQDSELARAALRIADMVLI 104

                         170       180
                  ....*....|....*....|....*...
gi 1597971800 274 PVPPAQVDFHStlkyltrLPELVSIIES 301
Cdd:PHA02518  105 PVQPSPFDIWA-------APDLVELIKA 125
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 110-278 1.03e-06

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: 49.58  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 110 LTVFIGnLKGGVSKTVSTVSLAHAMRAHPhllheDLRILVVDLD-PQSSATMFLNHTRAVGMVDttsaqaMLQNVSR--E 186
Cdd:cd03111     2 VVAVVG-AKGGVGASTLAVNLAQELAQRA-----KDKVLLIDLDlPFGDLGLYLNLRPDYDLAD------VIQNLDRldR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 187 ELIEEFIVPsVVPGVDVLPASIddafiasgwEQLCLEHLpgqNPHAVLRqnIVEKLEHDYDFIFIDSGPHLDAFLNNAIA 266
Cdd:cd03111    70 TLLDSAVTR-HSSGLSLLPAPQ---------ELEDLEAL---GAEQVDK--LLQVLRAFYDHIIVDLGHFLDEVTLAVLE 134

                         170
                  ....*....|....*
gi 1597971800 267 AAD---VLMTPVPPA 278
Cdd:cd03111   135 AADeilLVTQQDLPS 149
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 123-255 2.64e-04

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: 41.79  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597971800 123 KTVSTVSLAHAmrahphLLHEDLRILVVDLDP-QSSATMFLNHTRAVGMVDTtsaqamlqnVSREELIEEFIVPSVVPGV 201
Cdd:cd05387    33 KSTVAANLAVA------LAQSGKRVLLIDADLrRPSLHRLLGLPNEPGLSEV---------LSGQASLEDVIQSTNIPNL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1597971800 202 DVLPASiddAFIASGWEQLCLEHLpgqnphavlrQNIVEKLEHDYDFIFIDSGP 255
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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