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Conserved domains on  [gi|504236077|ref|WP_014423179|]
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transcriptional regulator [Selenomonas ruminantium]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
86-368 1.92e-52

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: 177.61  E-value: 1.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077  86 ADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQLKPTRTMAFFSPKGHAGQTTMATILALELAKKSGESVALIDAD 165
Cdd:COG4963   62 LILLEALSESAALLADVLPLSPDELRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 166 LQFGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPYFHPLGNGVWIMSGPLQPEHAELVEADRLIDVVRMAGSLFRYVLL 245
Cdd:COG4963  142 LQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHSSGLSVLAAPADLERAEEVSPEAVERLLDLLRRHFDYVVV 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 246 DLPMGFNPISLALAECADTDFIVSMVNSGHeVWHMKRSMKMLHMWDSYGKKIYPVFSGVQNCTPAHKAKLEGELGRKVMM 325
Cdd:COG4963  222 DLPRGLNPWTLAALEAADEVVLVTEPDLPS-LRNAKRLLDLLRELGLPDDKVRLVLNRVPKRGEISAKDIEEALGLPVAA 300
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 504236077 326 ILPQERRIVDV-TGSGRIMKDLPEHTPYVQALAGLADDIVSGRR 368
Cdd:COG4963  301 VLPNDPKAVAEaANQGRPLAEVAPKSPLAKAIRKLAARLTGRPA 344
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-123 1.28e-12

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 64.61  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077   1 MSYRVVLVERNDEMLSLMAGTLKADDEFDLASTYHDVEMALGQSSVFRPNLFLLDVD--DSRAVELVPNFIETYPKAHVL 78
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYlpDGDGLELLRELRARGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504236077  79 GLMENWKADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQL 123
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRL 126
 
Name Accession Description Interval E-value
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
86-368 1.92e-52

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: 177.61  E-value: 1.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077  86 ADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQLKPTRTMAFFSPKGHAGQTTMATILALELAKKSGESVALIDAD 165
Cdd:COG4963   62 LILLEALSESAALLADVLPLSPDELRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 166 LQFGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPYFHPLGNGVWIMSGPLQPEHAELVEADRLIDVVRMAGSLFRYVLL 245
Cdd:COG4963  142 LQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHSSGLSVLAAPADLERAEEVSPEAVERLLDLLRRHFDYVVV 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 246 DLPMGFNPISLALAECADTDFIVSMVNSGHeVWHMKRSMKMLHMWDSYGKKIYPVFSGVQNCTPAHKAKLEGELGRKVMM 325
Cdd:COG4963  222 DLPRGLNPWTLAALEAADEVVLVTEPDLPS-LRNAKRLLDLLRELGLPDDKVRLVLNRVPKRGEISAKDIEEALGLPVAA 300
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 504236077 326 ILPQERRIVDV-TGSGRIMKDLPEHTPYVQALAGLADDIVSGRR 368
Cdd:COG4963  301 VLPNDPKAVAEaANQGRPLAEVAPKSPLAKAIRKLAARLTGRPA 344
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
127-361 5.76e-25

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: 101.20  E-value: 5.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 127 RTMAFFSPKGHAGQTTMATILALELAKKSGESVALIDADLQFGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPYFHPLG 206
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSAVTRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 207 NGVWIMSGPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDLPMGFNPISLALAECADTDFIVsMVNSGHEVWHMKRSMKM 286
Cdd:cd03111   81 SGLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLV-TQQDLPSLRNARRLLDS 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504236077 287 LHMWDSYGKKIYPVFSGV---QNCTPAHKAKLegeLGRKVMMILPQERRIV-DVTGSGRIMKDLPEHTPYVQALAGLAD 361
Cdd:cd03111  160 LRELEGSSDRLRLVLNRYdkkSEISPKDIEEA---LGLEVFATLPNDYKAVsESANTGRPLVEVAPRSALVRALQDLAA 235
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-123 1.28e-12

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 64.61  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077   1 MSYRVVLVERNDEMLSLMAGTLKADDEFDLASTYHDVEMALGQSSVFRPNLFLLDVD--DSRAVELVPNFIETYPKAHVL 78
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYlpDGDGLELLRELRARGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504236077  79 GLMENWKADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQL 123
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRL 126
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
130-272 1.96e-06

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: 48.50  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077  130 AFFSPKGHAGQTTMATILALELAKKsGESVALIDADLQ----FGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPyfHPL 205
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARR-GLRVLLIDLDPQsnnsSVEGLEGDIAPALQALAEGLKGRVNLDPILLKE--KSD 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504236077  206 GNGVWIMSGPLQPEHAELVEAD-----RLIDVVRMAGSLFRYVLLDLPMG--FNPISlalAECAdTDFIVSMVN 272
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGprkeeRLREALEALKEDYDYVIIDGAPGlgELLRN---ALIA-ADYVIIPLE 148
PRK09841 PRK09841
tyrosine-protein kinase;
134-289 1.61e-03

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 40.66  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 134 PKGHAGQTTMATILALELAKkSGESVALIDADLQFGDVAMFFDAVPQHNVVEAThDIKLLTPATLEPYFHplGNGVWIMS 213
Cdd:PRK09841 539 ATPDSGKTFVSSTLAAVIAQ-SDQKVLFIDADLRRGYSHNLFTVSNEHGLSEYL-AGKDELNKVIQHFGK--GGFDVITR 614
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 214 GPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDLP--MGFNPISLAlAECADTDFIVSM--VNSGHEvwhMKRSMKMLHM 289
Cdd:PRK09841 615 GQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPpmLAVSDAAVV-GRSVGTSLLVARfgLNTAKE---VSLSMQRLEQ 690
 
Name Accession Description Interval E-value
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
86-368 1.92e-52

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: 177.61  E-value: 1.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077  86 ADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQLKPTRTMAFFSPKGHAGQTTMATILALELAKKSGESVALIDAD 165
Cdd:COG4963   62 LILLEALSESAALLADVLPLSPDELRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 166 LQFGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPYFHPLGNGVWIMSGPLQPEHAELVEADRLIDVVRMAGSLFRYVLL 245
Cdd:COG4963  142 LQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHSSGLSVLAAPADLERAEEVSPEAVERLLDLLRRHFDYVVV 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 246 DLPMGFNPISLALAECADTDFIVSMVNSGHeVWHMKRSMKMLHMWDSYGKKIYPVFSGVQNCTPAHKAKLEGELGRKVMM 325
Cdd:COG4963  222 DLPRGLNPWTLAALEAADEVVLVTEPDLPS-LRNAKRLLDLLRELGLPDDKVRLVLNRVPKRGEISAKDIEEALGLPVAA 300
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 504236077 326 ILPQERRIVDV-TGSGRIMKDLPEHTPYVQALAGLADDIVSGRR 368
Cdd:COG4963  301 VLPNDPKAVAEaANQGRPLAEVAPKSPLAKAIRKLAARLTGRPA 344
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
127-361 5.76e-25

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: 101.20  E-value: 5.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 127 RTMAFFSPKGHAGQTTMATILALELAKKSGESVALIDADLQFGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPYFHPLG 206
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSAVTRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 207 NGVWIMSGPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDLPMGFNPISLALAECADTDFIVsMVNSGHEVWHMKRSMKM 286
Cdd:cd03111   81 SGLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLV-TQQDLPSLRNARRLLDS 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504236077 287 LHMWDSYGKKIYPVFSGV---QNCTPAHKAKLegeLGRKVMMILPQERRIV-DVTGSGRIMKDLPEHTPYVQALAGLAD 361
Cdd:cd03111  160 LRELEGSSDRLRLVLNRYdkkSEISPKDIEEA---LGLEVFATLPNDYKAVsESANTGRPLVEVAPRSALVRALQDLAA 235
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
142-269 6.21e-15

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: 73.39  E-value: 6.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 142 TMATILALELAKKsGESVALIDADLQFGDVAMFFDAVPQHNVVEATHDiklltPATLEPYFHPLGNGVWIMSGPLQPEH- 220
Cdd:COG0455    1 TVAVNLAAALARL-GKRVLLVDADLGLANLDVLLGLEPKATLADVLAG-----EADLEDAIVQGPGGLDVLPGGSGPAEl 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504236077 221 AELVEADRLIDVVRMAGSLFRYVLLDLPMGFNPISLALAECADTDFIVS 269
Cdd:COG0455   75 AELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVT 123
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
110-271 3.46e-13

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: 67.60  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 110 IRKALEIAtrrGQLKPTRTMAFFSPKGHAGQTTMATILALELAKkSGESVALIDADLQFGDVAMFFDAVPQHNVVEAthd 189
Cdd:cd05387    6 LRTNLLFA---GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQ-SGKRVLLIDADLRRPSLHRLLGLPNEPGLSEV--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 190 ikLLTPATLEPYFHPLG-NGVWIM-SGPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDLPmgfnpislALAECADTDFI 267
Cdd:cd05387   79 --LSGQASLEDVIQSTNiPNLDVLpAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTP--------PVLAVADALIL 148

                 ....
gi 504236077 268 VSMV 271
Cdd:cd05387  149 APLV 152
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
113-289 9.21e-13

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: 67.90  E-value: 9.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 113 ALEIATRRGQLKPTRTMAFFSPKGHAGQTTMATILALELAKkSGESVALIDADLQFGDVAMFFDAVPQHNVVEAthdikL 192
Cdd:COG0489   79 LLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPGLSDV-----L 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 193 LTPATLEPYFHPLGN-GVWIMS-GPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDLP--MGFNPISLaLAECADTDFIV 268
Cdd:COG0489  153 AGEASLEDVIQPTEVeGLDVLPaGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPpgLGVADATL-LASLVDGVLLV 231
                        170       180
                 ....*....|....*....|..
gi 504236077 269 smVNSGHEVWHM-KRSMKMLHM 289
Cdd:COG0489  232 --VRPGKTALDDvRKALEMLEK 251
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-123 1.28e-12

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 64.61  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077   1 MSYRVVLVERNDEMLSLMAGTLKADDEFDLASTYHDVEMALGQSSVFRPNLFLLDVD--DSRAVELVPNFIETYPKAHVL 78
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYlpDGDGLELLRELRARGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504236077  79 GLMENWKADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQL 123
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRL 126
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
127-247 1.19e-06

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: 47.15  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 127 RTMAFFSPKGHAGQTTMATILALELAKKsGESVALIDADlqfgdvamffdavPQHNVVEATHDIKLL-TPATLEPYFHP- 204
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALR-GKRVLLIDLD-------------PQGSLTSWLYDYILIdTPPSLGLLTRNa 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504236077 205 --LGNGVWImsgPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDL 247
Cdd:cd02042   67 laAADLVLI---PVQPSPFDLDGLAKLLDTLEELKKQLNPPLLIL 108
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
127-268 1.82e-06

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 48.33  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 127 RTMAFFSPKGHAGQTTMATILALELAKKsGESVALIDADLQFGDVAMFFDAVPQHN---VVEAT---HDIKLLTPATLep 200
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKL-GKRVLLLDADLGLANLDILLGLAPKKTlgdVLKGRvslEDIIVEGPEGL-- 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504236077 201 YFHPLGNGVWIMSGpLQPEHAelveaDRLIDVVRMAGSLFRYVLLDLPMGFNPISLALAECADTDFIV 268
Cdd:cd02038   78 DIIPGGSGMEELAN-LDPEQK-----AKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVV 139
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
130-272 1.96e-06

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: 48.50  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077  130 AFFSPKGHAGQTTMATILALELAKKsGESVALIDADLQ----FGDVAMFFDAVPQHNVVEATHDIKLLTPATLEPyfHPL 205
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARR-GLRVLLIDLDPQsnnsSVEGLEGDIAPALQALAEGLKGRVNLDPILLKE--KSD 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504236077  206 GNGVWIMSGPLQPEHAELVEAD-----RLIDVVRMAGSLFRYVLLDLPMG--FNPISlalAECAdTDFIVSMVN 272
Cdd:pfam01656  79 EGGLDLIPGNIDLEKFEKELLGprkeeRLREALEALKEDYDYVIIDGAPGlgELLRN---ALIA-ADYVIIPLE 148
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-122 1.14e-04

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 42.64  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077   1 MSYRVVLVERNDEMLSLMAGTLKADDeFDLASTYHDVEMALGQSSVFRPNLFLLDVD-DSRAVELVPNFIETYPKAHVLG 79
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAG-YEVVAEAADGEDAVELVRELKPDLVIVDIDmPDRDGLEAARQISEERPAPVIL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504236077  80 LMENWKADVAEKVLAAGGDGCMLKPFHTPDIRKALEIATRRGQ 122
Cdd:COG3707   81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFR 123
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
127-250 1.40e-03

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: 39.88  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 127 RTMAFFSPKGHAGQTTMATILALELAKKsGESVALIDADLQFG--DVAM------FFDAvpqHNVVEAThdiklltpATL 198
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKL-GKKVLLIDADIGLRnlDLILglenriVYTL---VDVLEGE--------CRL 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504236077 199 EP--YFHPLGNGVWIMSGPLQPEHAELvEADRLIDVVRMAGSLFRYVLLDLPMG 250
Cdd:cd02036   69 EQalIKDKRWENLYLLPASQTRDKDAL-TPEKLEELVKELKDSFDFILIDSPAG 121
PRK09841 PRK09841
tyrosine-protein kinase;
134-289 1.61e-03

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 40.66  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 134 PKGHAGQTTMATILALELAKkSGESVALIDADLQFGDVAMFFDAVPQHNVVEAThDIKLLTPATLEPYFHplGNGVWIMS 213
Cdd:PRK09841 539 ATPDSGKTFVSSTLAAVIAQ-SDQKVLFIDADLRRGYSHNLFTVSNEHGLSEYL-AGKDELNKVIQHFGK--GGFDVITR 614
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504236077 214 GPLQPEHAELVEADRLIDVVRMAGSLFRYVLLDLP--MGFNPISLAlAECADTDFIVSM--VNSGHEvwhMKRSMKMLHM 289
Cdd:PRK09841 615 GQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPpmLAVSDAAVV-GRSVGTSLLVARfgLNTAKE---VSLSMQRLEQ 690
 
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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