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Conserved domains on  [gi|504538402|ref|WP_014725504|]
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MULTISPECIES: ParA family protein [Burkholderia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA_partition super family cl49513
ParA family partition ATPase;
5-215 4.56e-55

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 174.66  E-value: 4.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPMTVLSLAPAgrGIGGEIKKQDANFDVI 84
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLARP--TLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLEDpRIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRnPNLSSALMLNSVNGKTKMREEILKILka 164
Cdd:NF041546  80 VIDGPPRAED-LARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYT-PGLKAAFVLNRAIARTALGREVAEAL-- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504538402 165 EEIGEHLLDSQIAQREVYRQTFALGTTIHHHNRylKGlkEARAEIEKLVTE 215
Cdd:NF041546 156 AEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEP--DG--KAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
5-215 4.56e-55

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 174.66  E-value: 4.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPMTVLSLAPAgrGIGGEIKKQDANFDVI 84
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLARP--TLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLEDpRIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRnPNLSSALMLNSVNGKTKMREEILKILka 164
Cdd:NF041546  80 VIDGPPRAED-LARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYT-PGLKAAFVLNRAIARTALGREVAEAL-- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504538402 165 EEIGEHLLDSQIAQREVYRQTFALGTTIHHHNRylKGlkEARAEIEKLVTE 215
Cdd:NF041546 156 AEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEP--DG--KAAREIRALAKE 202
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 5-221 1.11e-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: 139.61  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPMTV---------------------LSL 63
Cdd:COG1192    4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLydlllddapledaivpteipgLDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  64 APAGRGIGGE-----------------IKKQDANFDVIVVDCPGNLeDPRIASVLEVADFCLVPLSPSPADLYSTVAMIR 126
Cdd:COG1192   84 IPANIDLAGAeielvsrpgrelrlkraLAPLADDYDYILIDCPPSL-GLLTLNALAAADSVLIPVQPEYLSLEGLAQLLE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402 127 MIESMRAVRNPNLS-SALMLNSVNGKTKMREEILKILKaEEIGEHLLDSQIAQREVYRQTFALGTTIHHHNRYlkglKEA 205
Cdd:COG1192  163 TIEEVREDLNPKLEiLGILLTMVDPRTRLSREVLEELR-EEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPK----SKG 237

                        250
                 ....*....|....*.
gi 504538402 206 RAEIEKLVTEMAQYIA 221
Cdd:COG1192  238 AKAYRALAEELLERLE 253
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-163 7.69e-39

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: 130.74  E-value: 7.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVtsgentlpmtvlslapagrgiggeikkqdanFDVI 84
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-------------------------------YDYI 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLeDPRIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRNPNLS-SALMLNSVNGKTKMREEILKILK 163
Cdd:cd02042   52 LIDTPPSL-GLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLiLGILLTRVDPRTKLAREVLEELK 130
PHA02518 PHA02518
ParA-like protein; Provisional
 5-220 4.28e-35

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 123.81  E-value: 4.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPmtVLSLAPAGRGIGGEIKKQDANFDVI 84
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEP--LIPVVRMGKSIRADLPKVASGYDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLEDPrIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRNPNLSSALMLNSVNGKTKMREEILKILka 164
Cdd:PHA02518  81 VVDGAPQDSEL-ARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKAL-- 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504538402 165 EEIGEHLLDSQIAQREVYRQTFALGTtihhHNRYLKGLKEARAEIEKLVTEMAQYI 220
Cdd:PHA02518 158 AGYGLPILRNGTTQRVAYADAAEAGG----SVLELPEDDKAAEEIIQLVKELFRGI 209
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-167 3.51e-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: 80.08  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQG--TSVRWVTSGENT--------------------------- 55
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnnSSVEGLEGDIAPalqalaeglkgrvnldpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   56 ----LPM----TVLSLAPAGRGIGGEIKKQ----DANFDVIVVDCPGNLEDPRIASVLeVADFCLVPLSPSPadlYSTVA 123
Cdd:pfam01656  81 gldlIPGnidlEKFEKELLGPRKEERLREAlealKEDYDYVIIDGAPGLGELLRNALI-AADYVIIPLEPEV---ILVED 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504538402  124 MIRMIESMRAVRNPNLSSALML--------NSVNGKTKMREEILKILKAEEI 167
Cdd:pfam01656 157 AKRLGGVIAALVGGYALLGLKIigvvlnkvDGDNHGKLLKEALEELLRGLPV 208
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 5-194 1.18e-07

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 50.81  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGT-----SVRW---------VTSGENTLPMTVLSLA-----P 65
Cdd:TIGR03371   4 IAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLlrlhfGMDWsvrdgwaraLLNGADWAAAAYRSPDgvlflP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   66 AGRGIGGEIKK---QDANF-------------DVIVVDCPGNLEdPRIASVLEVADFCLVPLSPSPAdlySTVAMIRMIE 129
Cdd:TIGR03371  84 YGDLSADEREAyqaHDAGWlarllqqldlaarDWVLIDLPRGPS-PITRQALAAADLVLVVVNADAA---CYATLHQLAL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504538402  130 SMRAVRNPNLSSALMLNSVNGKTKMREEILKILKAeEIGEHLLDSQIAQREVYRQTFALGTTIHH 194
Cdd:TIGR03371 160 ALFAGSGPRDGPRFLINQFDPARQLSRDVRAVLRQ-TLGSRLLPFVIHRDEAVSEALARGTPVLN 223
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
5-215 4.56e-55

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 174.66  E-value: 4.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPMTVLSLAPAgrGIGGEIKKQDANFDVI 84
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLARP--TLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLEDpRIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRnPNLSSALMLNSVNGKTKMREEILKILka 164
Cdd:NF041546  80 VIDGPPRAED-LARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYT-PGLKAAFVLNRAIARTALGREVAEAL-- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504538402 165 EEIGEHLLDSQIAQREVYRQTFALGTTIHHHNRylKGlkEARAEIEKLVTE 215
Cdd:NF041546 156 AEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEP--DG--KAAREIRALAKE 202
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 5-221 1.11e-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: 139.61  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPMTV---------------------LSL 63
Cdd:COG1192    4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLydlllddapledaivpteipgLDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  64 APAGRGIGGE-----------------IKKQDANFDVIVVDCPGNLeDPRIASVLEVADFCLVPLSPSPADLYSTVAMIR 126
Cdd:COG1192   84 IPANIDLAGAeielvsrpgrelrlkraLAPLADDYDYILIDCPPSL-GLLTLNALAAADSVLIPVQPEYLSLEGLAQLLE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402 127 MIESMRAVRNPNLS-SALMLNSVNGKTKMREEILKILKaEEIGEHLLDSQIAQREVYRQTFALGTTIHHHNRYlkglKEA 205
Cdd:COG1192  163 TIEEVREDLNPKLEiLGILLTMVDPRTRLSREVLEELR-EEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPK----SKG 237

                        250
                 ....*....|....*.
gi 504538402 206 RAEIEKLVTEMAQYIA 221
Cdd:COG1192  238 AKAYRALAEELLERLE 253
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-163 7.69e-39

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: 130.74  E-value: 7.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVtsgentlpmtvlslapagrgiggeikkqdanFDVI 84
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-------------------------------YDYI 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLeDPRIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRNPNLS-SALMLNSVNGKTKMREEILKILK 163
Cdd:cd02042   52 LIDTPPSL-GLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLiLGILLTRVDPRTKLAREVLEELK 130
PHA02518 PHA02518
ParA-like protein; Provisional
 5-220 4.28e-35

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 123.81  E-value: 4.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPmtVLSLAPAGRGIGGEIKKQDANFDVI 84
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEP--LIPVVRMGKSIRADLPKVASGYDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  85 VVDCPGNLEDPrIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRNPNLSSALMLNSVNGKTKMREEILKILka 164
Cdd:PHA02518  81 VVDGAPQDSEL-ARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKAL-- 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504538402 165 EEIGEHLLDSQIAQREVYRQTFALGTtihhHNRYLKGLKEARAEIEKLVTEMAQYI 220
Cdd:PHA02518 158 AGYGLPILRNGTTQRVAYADAAEAGG----SVLELPEDDKAAEEIIQLVKELFRGI 209
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-167 3.51e-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: 80.08  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQG--TSVRWVTSGENT--------------------------- 55
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnnSSVEGLEGDIAPalqalaeglkgrvnldpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   56 ----LPM----TVLSLAPAGRGIGGEIKKQ----DANFDVIVVDCPGNLEDPRIASVLeVADFCLVPLSPSPadlYSTVA 123
Cdd:pfam01656  81 gldlIPGnidlEKFEKELLGPRKEERLREAlealKEDYDYVIIDGAPGLGELLRNALI-AADYVIIPLEPEV---ILVED 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504538402  124 MIRMIESMRAVRNPNLSSALML--------NSVNGKTKMREEILKILKAEEI 167
Cdd:pfam01656 157 AKRLGGVIAALVGGYALLGLKIigvvlnkvDGDNHGKLLKEALEELLRGLPV 208
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 5-140 4.84e-18

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: 78.39  E-value: 4.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQG--------------TSVRWVTSGENTL-------PMTVLSL 63
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGnatsglgidknnveKTIYELLIGECNIeeaiiktVIENLDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   64 APAG---RGIGGE--------------IKKQDANFDVIVVDCPGNLedpriaSVLEV-----ADFCLVPLSPSPADLYST 121
Cdd:pfam13614  84 IPSNidlAGAEIEligienrenilkeaLEPVKDNYDYIIIDCPPSL------GLLTInaltaSDSVLIPVQCEYYALEGL 157

                         170
                  ....*....|....*....
gi 504538402  122 VAMIRMIESMRAVRNPNLS 140
Cdd:pfam13614 158 SQLLNTIKLVKKRLNPSLE 176
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 5-118 1.46e-14

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


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 70.56  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADP-QGTSVR-------WVTSGENTLPMT---VLSLAPAGRGIGGE 73
Cdd:pfam09140   3 IVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRyfenrsaTADRTGLSLPTPehlNLPDNDVAEVPDGE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504538402   74 ----------IKKQDANFDVIVVDCPGNlEDPRIASVLEVADFCLVPLSPSPADL 118
Cdd:pfam09140  83 niddarleeaFADLEARCDFIVIDTPGS-DSPLSRLAHSRADTLVTPLNDSFVDF 136
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 5-132 5.83e-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: 63.98  E-value: 5.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAF-EAGGNKVALIDADPQGTSV----------------------------RWVTSGENT 55
Cdd:COG4963  105 IAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFGDValyldleprrgladalrnpdrldetlldRALTRHSSG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  56 LpmTVLSlAPAGRGIGGEIKKQD---------ANFDVIVVDCPGNLeDPRIASVLEVADFCLVPLSPSPADLYSTVAMIR 126
Cdd:COG4963  185 L--SVLA-APADLERAEEVSPEAverlldllrRHFDYVVVDLPRGL-NPWTLAALEAADEVVLVTEPDLPSLRNAKRLLD 260


                 ....*.
gi 504538402 127 MIESMR 132
Cdd:COG4963  261 LLRELG 266
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-139 1.40e-11

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: 61.83  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  18 TISVNIAAAFEAGGNKVALIDADPQGTSVRW------------VTSGENTL-PMTV-----LSLAPAGRGIGG------- 72
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVllglepkatladVLAGEADLeDAIVqgpggLDVLPGGSGPAElaeldpe 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504538402  73 -----EIKKQDANFDVIVVDCPGNLEDPrIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRNPNL 139
Cdd:COG0455   81 erlirVLEELERFYDVVLVDTGAGISDS-VLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRRAGV 151
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 4-46 1.87e-09

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 55.59  E-value: 1.87e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 504538402   4 KIAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSV 46
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSI 44
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 4-46 1.95e-09

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 55.92  E-value: 1.95e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 504538402    4 KIAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSV 46
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSI 47
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 5-128 2.01e-09

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: 55.65  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSV------------RWVTSGENTLPMTV------LSLAPA 66
Cdd:cd02038    3 IAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLdillglapkktlGDVLKGRVSLEDIIvegpegLDIIPG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504538402  67 GRGIGG--------------EIKKQDANFDVIVVDCPGNLEDPRIASVLeVADFCLVPLSPSPADLYSTVAMIRMI 128
Cdd:cd02038   83 GSGMEElanldpeqkaklieELSSLESNYDYLLIDTGAGISRNVLDFLL-AADEVIVVTTPEPTSITDAYALIKVL 157
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
5-46 7.55e-09

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 55.05  E-value: 7.55e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSV 46
Cdd:PRK11670 110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSI 151
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 5-194 1.18e-07

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 50.81  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGT-----SVRW---------VTSGENTLPMTVLSLA-----P 65
Cdd:TIGR03371   4 IAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLlrlhfGMDWsvrdgwaraLLNGADWAAAAYRSPDgvlflP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   66 AGRGIGGEIKK---QDANF-------------DVIVVDCPGNLEdPRIASVLEVADFCLVPLSPSPAdlySTVAMIRMIE 129
Cdd:TIGR03371  84 YGDLSADEREAyqaHDAGWlarllqqldlaarDWVLIDLPRGPS-PITRQALAAADLVLVVVNADAA---CYATLHQLAL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504538402  130 SMRAVRNPNLSSALMLNSVNGKTKMREEILKILKAeEIGEHLLDSQIAQREVYRQTFALGTTIHH 194
Cdd:TIGR03371 160 ALFAGSGPRDGPRFLINQFDPARQLSRDVRAVLRQ-TLGSRLLPFVIHRDEAVSEALARGTPVLN 223
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 3-41 1.44e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 50.55  E-value: 1.44e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 504538402   3 FKIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADP 41
Cdd:COG3640    1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 5-133 1.58e-07

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: 50.96  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRW------------VTSGENTLPMTV-------LSLAP 65
Cdd:COG0489   95 IAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRmlglenrpglsdVLAGEASLEDVIqptevegLDVLP 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  66 AGRGI--------GGEIKK--QDAN--FDVIVVDCPGNLEDPRIASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRA 133
Cdd:COG0489  175 AGPLPpnpsellaSKRLKQllEELRgrYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGV 254
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 5-167 1.61e-07

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: 50.28  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTLPMTV----------------------LS 62
Cdd:cd02036    3 IVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLvdvlegecrleqalikdkrwenLY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  63 LAPAGR-----GIGGE-----IKKQDANFDVIVVDCPGNLEDPRIASVLEvADFCLVPLSPSPADLYSTVAMIRMIESMr 132
Cdd:cd02036   83 LLPASQtrdkdALTPEkleelVKELKDSFDFILIDSPAGIESGFINAIAP-ADEAIIVTNPEISSVRDADRVIGLLESK- 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504538402 133 AVRNPNlssaLMLNSVNGKTKMREEILKILKAEEI 167
Cdd:cd02036  161 GIVNIG----LIVNRYRPEMVKSGDMLSVEDIQEI 191
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 5-169 3.92e-07

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 49.34  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD-----------PQGTSVRW--VTSGENTL-------PMTVLSLa 64
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAKLGKKVLALDADitmanlelilgMEDKPVTLhdVLAGEADIkdaiyegPFGVKVI- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   65 PAGRGIGGeIKKQDAN------------FDVIVVDCPGNLEDPRIASVLeVADFCLVPLSPspaDLYSTVAMIRMIESMR 132
Cdd:TIGR01969  82 PAGVSLEG-LRKADPDkledvlkeiiddTDFLLIDAPAGLERDAVTALA-AADELLLVVNP---EISSITDALKTKIVAE 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 504538402  133 AVRNPNLssALMLNSV-NGKTKM-REEILKILKAEEIGE 169
Cdd:TIGR01969 157 KLGTAIL--GVVLNRVtRDKTELgREEIETILEVPVLGV 193
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-40 4.41e-07

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 49.29  E-value: 4.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504538402   1 MAFKIAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
 5-139 8.32e-07

helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.


Pssm-ID: 274798 [Multi-domain]  Cd Length: 322  Bit Score: 48.87  E-value: 8.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGT------------SVRW--VTSGENTLPMTVLSLAP----- 65
Cdd:TIGR03815  96 VAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADPWGGgldlllgaedvpGLRWpdLSQARGRLPAGALRDALprrgg 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   66 -----AGRGIGGEIKKQ---------DANFDVIVVDCPGnLEDPRIASVLEVADFCLVPLspsPADLYSTVAMIRMIeSM 131
Cdd:TIGR03815 176 lsvlsWGRAVGAALPPAavravldaaRRGGDLVVVDLPR-RLTPAAETALESADLVLVVV---PADVRAVAAAARVC-PE 250


                  ....*...
gi 504538402  132 RAVRNPNL 139
Cdd:TIGR03815 251 LGRRNPDL 258
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-78 1.17e-06

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 48.13  E-value: 1.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504538402  11 KGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENtlPMTVLSLApAGRGIGGEIKKQD 78
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKV--PPTIDEML-TEDGTAEELRRED 72
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 4-129 2.05e-06

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 45.11  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   4 KIAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADpqgtsvrwvtsgentlpmtvlslapagrgiggeikkqdanfDV 83
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD-----------------------------------------DY 40

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504538402  84 IVVDCPGNLEDPRIAS------VLEVADFCLVPLSPSPADLYSTVAMIRMIE 129
Cdd:cd01983   41 VLIDGGGGLETGLLLGtivallALKKADEVIVVVDPELGSLLEAVKLLLALL 92
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 5-40 4.12e-06

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 46.56  E-value: 4.12e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 5-169 5.53e-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: 45.73  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAF-EAGGNKVALIDAD-PQGT------------------------------SVRWVTSG 52
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELaQRAKDKVLLIDLDlPFGDlglylnlrpdydladviqnldrldrtlldsAVTRHSSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  53 ENTLPMTVLSlaPAGRGIGGE-----IKKQDANFDVIVVDCPGNLeDPRIASVLEVADFCLVPLSPSPADLYSTVAMIRM 127
Cdd:cd03111   83 LSLLPAPQEL--EDLEALGAEqvdklLQVLRAFYDHIIVDLGHFL-DEVTLAVLEAADEILLVTQQDLPSLRNARRLLDS 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504538402 128 IESMRAVRNPnlsSALMLNSVNGKTKMR-EEILKILKAEEIGE 169
Cdd:cd03111  160 LRELEGSSDR---LRLVLNRYDKKSEISpKDIEEALGLEVFAT 199
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 4-133 6.25e-06

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 45.75  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   4 KIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSvrwvtsgenTLPMT---------VLSLA---------- 64
Cdd:cd02032    2 VIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDS---------TFTLTgfliptvidVLQSVdfhyeevwpe 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  65 ------------------PAGRGIGGEI--------KKQDA--NFDVIVVDCPGNLEDPRIASVLEVADFCLVplsPSPA 116
Cdd:cd02032   72 dviftgyggvdcveaggpPAGTGCGGYVvgetvkllKELNAfdEYDVILFDVLGDVVCGGFAAPLNYADYCLI---VTAN 148

                        170
                 ....*....|....*..
gi 504538402 117 DLYSTVAMIRMIESMRA 133
Cdd:cd02032  149 DFDSLFAANRIAAAVRE 165
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 5-40 1.02e-05

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 44.48  E-value: 1.02e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:cd05387   22 IAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD 57
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 4-41 1.11e-05

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 44.99  E-value: 1.11e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 504538402   4 KIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADP 41
Cdd:cd02034    2 KIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 5-40 1.47e-05

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 44.35  E-value: 1.47e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:TIGR01007  20 LLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD 55
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-40 1.54e-05

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 44.68  E-value: 1.54e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 504538402   4 KIAVSNQKGGTGKTTISVNIAAAFEaggnKVALIDAD 40
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLLY----NVILVDCD 33
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 4-76 1.90e-05

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 44.43  E-value: 1.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504538402   4 KIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENtLPmTVLSLApAGRGIGGEIKK 76
Cdd:cd02040    2 QIAIYG-KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKA-IP-TVLDTL-REKGEVEELED 70
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-133 2.55e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.18  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   1 MAFKIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTsgeNTLPMTVLSL----------------- 63
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLT---GKLVPTVIDIleevdfhseelrpedfv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  64 --------------APAGRGIGGEI--------KKQDA--NFDVIVVDCPGNLEDPRIASVLEVADFCLVplsPSPADLY 119
Cdd:PRK13185  77 yegyngvdcveaggPPAGTGCGGYVvgetvkllKEHHLldDYDVILFDVLGDVVCGGFAAPLQYADYALI---VTANDFD 153

                        170
                 ....*....|....
gi 504538402 120 STVAMIRMIESMRA 133
Cdd:PRK13185 154 SIFAANRIAAAIQA 167
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-44 6.76e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 43.13  E-value: 6.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGT 44
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQAS 163
chlL CHL00072
photochlorophyllide reductase subunit L
 4-109 7.47e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 42.80  E-value: 7.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   4 KIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSG----------------ENTLPMTVLSLA--- 64
Cdd:CHL00072   2 KLAVYG-KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFliptiidtlqskdyhyEDVWPEDVIYKGygg 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504538402  65 ---------PAGRGIGGEI--------KKQDA--NFDVIVVDCPGNLEDPRIASVLEVADFCLV 109
Cdd:CHL00072  81 vdcveaggpPAGAGCGGYVvgetvkllKELNAfyEYDIILFDVLGDVVCGGFAAPLNYADYCII 144
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 5-132 1.07e-04

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 42.66  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402   5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDA-DPQGTSVR---WVTS----GENT-LPMTV--------------- 60
Cdd:PRK13705 109 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMyhgWVPDlhihAEDTlLPFYLgekddatyaikptcw 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  61 --LSLAP---AGRGIGGEI-KKQDA--------------------NFDVIVVDCPGNLEDPRIaSVLEVADFCLVplsPS 114
Cdd:PRK13705 189 pgLDIIPsclALHRIETELmGKFDEgklptdphlmlrlaietvahDYDVIVIDSAPNLGIGTI-NVVCAADVLIV---PT 264

                        170
                 ....*....|....*...
gi 504538402 115 PADLYSTVAMIRMIESMR 132
Cdd:PRK13705 265 PAELFDYTSALQFFDMLR 282
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
4-82 1.39e-04

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 42.05  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504538402    4 KIAVSNqKGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWVTSGENTlpMTVLSLApAGRGIGGEIKKQDANFD 82
Cdd:pfam00142   2 QIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQ--PTVLDTA-REKGYVEDVEVEDVVYK 76
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 5-42 1.94e-04

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 41.89  E-value: 1.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDADPQ 42
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQ 144
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
11-148 3.06e-04

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 40.60  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504538402  11 KGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVRWvtsGENTLPM----TVLSLAPAGRGIGGEIKKQDA---NFDV 83
Cdd:PRK13849  10 KGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRW---KENALRSntwdPACEVYAADELPLLEAAYEDAelqGFDY 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504538402  84 IVVDCPGNLEDPRiASVLEVADFCLVPLSPSPADLYSTVAMIRMIESMRAVRNPNLSSALMLNSV 148
Cdd:PRK13849  87 ALADTHGGSSELN-NTIIASSNLLLIPTMLTPLDIDEALSTYRYVIELLLSENLAIPTAILRQRV 150
minD CHL00175
septum-site determining protein; Validated
 1-40 3.50e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.91  E-value: 3.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504538402   1 MAFKIAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-47 1.88e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 38.60  E-value: 1.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 504538402  11 KGGTGKTTISVNIAAAFEAGGNKVALIDADPQGTSVR 47
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTR 45
PRK10818 PRK10818
septum site-determining protein MinD;
1-40 4.27e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 37.61  E-value: 4.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504538402   1 MAFKIAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 5-40 7.23e-03

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 37.39  E-value: 7.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 504538402    5 IAVSNQKGGTGKTTISVNIAAAFEAGGNKVALIDAD 40
Cdd:TIGR01005 556 IAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDAD 591
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-41 9.09e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 36.33  E-value: 9.09e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 504538402  11 KGGTGKTTISVNIAAAFEAGGNKVALIDADP 41
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
 
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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