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Conserved domains on  [gi|983538840|ref|WP_060690453|]
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AAA family ATPase [Persicobacter diffluens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 81-357 1.40e-57

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: 187.37  E-value: 1.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALEDtqGELIRDCIVQLHd 160
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLD--DAPLEDAIVPTE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 161 iSEQLYILPSYGKLNNLETseKLTTKQKLES-FKNIVNKIRFEYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFS 239
Cdd:COG1192   78 -IPGLDLIPANIDLAGAEI--ELVSRPGRELrLKRALAPLADDYDYILIDCPPSL-GLLTLNALAAADSVLIPVQPEYLS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 240 FDGLSRSVSYLKERKKD-NPLLKIGGAFFN----RTKPGKNQMEQIENYAlgaereGIYVFESIIRDSVGIQKAFTYRYd 314
Cdd:COG1192  154 LEGLAQLLETIEEVREDlNPKLEILGILLTmvdpRTRLSREVLEELREEF------GDKVLDTVIPRSVALAEAPSAGK- 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 983538840 315 pTVFlnkfnegeiadfpktQLEPIKNAKSDFMELTTELLNRIQ 357
Cdd:COG1192  227 -PVF---------------EYDPKSKGAKAYRALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 81-357 1.40e-57

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: 187.37  E-value: 1.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALEDtqGELIRDCIVQLHd 160
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLD--DAPLEDAIVPTE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 161 iSEQLYILPSYGKLNNLETseKLTTKQKLES-FKNIVNKIRFEYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFS 239
Cdd:COG1192   78 -IPGLDLIPANIDLAGAEI--ELVSRPGRELrLKRALAPLADDYDYILIDCPPSL-GLLTLNALAAADSVLIPVQPEYLS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 240 FDGLSRSVSYLKERKKD-NPLLKIGGAFFN----RTKPGKNQMEQIENYAlgaereGIYVFESIIRDSVGIQKAFTYRYd 314
Cdd:COG1192  154 LEGLAQLLETIEEVREDlNPKLEILGILLTmvdpRTRLSREVLEELREEF------GDKVLDTVIPRSVALAEAPSAGK- 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 983538840 315 pTVFlnkfnegeiadfpktQLEPIKNAKSDFMELTTELLNRIQ 357
Cdd:COG1192  227 -PVF---------------EYDPKSKGAKAYRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 81-262 4.07e-35

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: 126.54  E-value: 4.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALedTQGELIRDCIVqlHD 160
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELL--IGECNIEEAII--KT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  161 ISEQLYILPSYGKLNNLETsEKLTTKQKLESFKNIVNKIRFEYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFSF 240
Cdd:pfam13614  77 VIENLDLIPSNIDLAGAEI-ELIGIENRENILKEALEPVKDNYDYIIIDCPPSL-GLLTINALTASDSVLIPVQCEYYAL 154

                         170       180
                  ....*....|....*....|...
gi 983538840  241 DGLSRSVSYLKE-RKKDNPLLKI 262
Cdd:pfam13614 155 EGLSQLLNTIKLvKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 82-283 6.97e-27

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 103.39  E-value: 6.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWnidkqafpmeimdaledtqgelirdcivqlhdi 161
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 162 seqlyilpsygklnnletseklttkqklesfknivnkirfeYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFSFD 241
Cdd:cd02042   48 -----------------------------------------YDYILIDTPPSL-GLLTRNALAAADLVLIPVQPSPFDLD 85

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 983538840 242 GLSRSVSYLKE-RKKDNPLLKIGGAFFNRTKPGKNQMEQIENY 283
Cdd:cd02042   86 GLAKLLDTLEElKKQLNPPLLILGILLTRVDPRTKLAREVLEE 128
ParA_partition NF041546
ParA family partition ATPase;
83-303 2.14e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 65.27  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  83 ILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGnSTSLWN-IDKQAFPMEIMDALEDTqgeLIRDcivqlhdi 161
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG-SALDWAaAREDERPFPVVGLARPT---LHRE-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 162 seqlyilpsygklnnletseklttkqklesfkniVNKIRFEYDYILMDMRPDMYGLFSEApLGAAEWVFLPVEASLFSFD 241
Cdd:NF041546  69 ----------------------------------LPSLARDYDFVVIDGPPRAEDLARSA-IKAADLVLIPVQPSPYDLW 113

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983538840 242 GLSRSVSYLKERKKDNPLLKigGAFF-NRTkpgknqmeqIENYALGAE-RE-----GIYVFESIIRDSV 303
Cdd:NF041546 114 ASADTVDLIKEAREYTPGLK--AAFVlNRA---------IARTALGREvAEalaeyGLPVLKTRIGQRV 171
PHA02518 PHA02518
ParA-like protein; Provisional
 82-285 5.33e-12

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 64.49  E-value: 5.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSlWnidkqafpmeimdALEDTQGELIRDCIvqlhdi 161
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTD-W-------------AEAREEGEPLIPVV------ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 162 seqlyilpSYGKlnnletseklttkqkleSFKNIVNKIRFEYDYILMDMRPDMYGLFSEApLGAAEWVFLPVEASLFSFD 241
Cdd:PHA02518  61 --------RMGK-----------------SIRADLPKVASGYDYVVVDGAPQDSELARAA-LRIADMVLIPVQPSPFDIW 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 983538840 242 GLSRSVSYLKERKKDNPLLKIgGAFFN-----RTKPGKNQMEQIENYAL 285
Cdd:PHA02518 115 AAPDLVELIKARQEVTDGLPK-FAFIIsraikNTQLYREARKALAGYGL 162
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 81-209 2.39e-07

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: 51.18  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDyqgnsTSLWNID-----KQAFPMEIMDALEDT---QGELIR 152
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-----IGLRNLDlllglENRIVYTLVDVVEGEcrlQQALIK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 983538840  153 DCIVqlhdisEQLYILPSYgklnnlETSEKLTTKQklESFKNIVNKIRFEYDYILMD 209
Cdd:TIGR01968  76 DKRL------KNLYLLPAS------QTRDKDAVTP--EQMKKLVNELKEEFDYVIID 118
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 81-357 1.40e-57

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: 187.37  E-value: 1.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALEDtqGELIRDCIVQLHd 160
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLD--DAPLEDAIVPTE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 161 iSEQLYILPSYGKLNNLETseKLTTKQKLES-FKNIVNKIRFEYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFS 239
Cdd:COG1192   78 -IPGLDLIPANIDLAGAEI--ELVSRPGRELrLKRALAPLADDYDYILIDCPPSL-GLLTLNALAAADSVLIPVQPEYLS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 240 FDGLSRSVSYLKERKKD-NPLLKIGGAFFN----RTKPGKNQMEQIENYAlgaereGIYVFESIIRDSVGIQKAFTYRYd 314
Cdd:COG1192  154 LEGLAQLLETIEEVREDlNPKLEILGILLTmvdpRTRLSREVLEELREEF------GDKVLDTVIPRSVALAEAPSAGK- 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 983538840 315 pTVFlnkfnegeiadfpktQLEPIKNAKSDFMELTTELLNRIQ 357
Cdd:COG1192  227 -PVF---------------EYDPKSKGAKAYRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 81-262 4.07e-35

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: 126.54  E-value: 4.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALedTQGELIRDCIVqlHD 160
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELL--IGECNIEEAII--KT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  161 ISEQLYILPSYGKLNNLETsEKLTTKQKLESFKNIVNKIRFEYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFSF 240
Cdd:pfam13614  77 VIENLDLIPSNIDLAGAEI-ELIGIENRENILKEALEPVKDNYDYIIIDCPPSL-GLLTINALTASDSVLIPVQCEYYAL 154

                         170       180
                  ....*....|....*....|...
gi 983538840  241 DGLSRSVSYLKE-RKKDNPLLKI 262
Cdd:pfam13614 155 EGLSQLLNTIKLvKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 82-283 6.97e-27

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 103.39  E-value: 6.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWnidkqafpmeimdaledtqgelirdcivqlhdi 161
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 162 seqlyilpsygklnnletseklttkqklesfknivnkirfeYDYILMDMRPDMyGLFSEAPLGAAEWVFLPVEASLFSFD 241
Cdd:cd02042   48 -----------------------------------------YDYILIDTPPSL-GLLTRNALAAADLVLIPVQPSPFDLD 85

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 983538840 242 GLSRSVSYLKE-RKKDNPLLKIGGAFFNRTKPGKNQMEQIENY 283
Cdd:cd02042   86 GLAKLLDTLEElKKQLNPPLLILGILLTRVDPRTKLAREVLEE 128
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 84-308 2.92e-19

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 85.48  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   84 LAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQG-NSTSLWNIDKQAFPME-IMDALEDtqGELIRDCIVQLHDI 161
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnNSSVEGLEGDIAPALQaLAEGLKG--RVNLDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  162 SEQLYILPSYgklNNLETSEKLTTKQKLESF-KNIVNKIRFEYDYILMDMRPDMYGLFSEApLGAAEWVFLPVEASLFS- 239
Cdd:pfam01656  79 EGGLDLIPGN---IDLEKFEKELLGPRKEERlREALEALKEDYDYVIIDGAPGLGELLRNA-LIAADYVIIPLEPEVILv 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983538840  240 --FDGLSRSVSYLKERKKDNPLLKIgGAFFNRTKPGKNQMEQIENYAlgAEREGIYVFeSIIRDSVGIQKA 308
Cdd:pfam01656 155 edAKRLGGVIAALVGGYALLGLKII-GVVLNKVDGDNHGKLLKEALE--ELLRGLPVL-GVIPRDEAVAEA 221
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 68-288 1.12e-13

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: 71.30  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  68 LTEEQLIELVQDA--------AKILAFWNQKGGVGKTTCCNSIAGVLTDQ-GKKVLVMDCDYQGNSTSLW-NIDKqafPM 137
Cdd:COG4963   81 LSPDELRAALARLldpgaarrGRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYlDLEP---RR 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 138 EIMDALEDTQ---GELIRDCIVQlhdISEQLYILPSygkLNNLETSEKLTTkqklESFKNIVNKIRFEYDYILMDMrPDM 214
Cdd:COG4963  158 GLADALRNPDrldETLLDRALTR---HSSGLSVLAA---PADLERAEEVSP----EAVERLLDLLRRHFDYVVVDL-PRG 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983538840 215 YGLFSEAPLGAAEWVFLPVEASLFSFDGLSRSVSYLKERKKDNPLLKIggaFFNR-TKPGKNQMEQIENyALGAE 288
Cdd:COG4963  227 LNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDKVRL---VLNRvPKRGEISAKDIEE-ALGLP 297
ParA_partition NF041546
ParA family partition ATPase;
83-303 2.14e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 65.27  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  83 ILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGnSTSLWN-IDKQAFPMEIMDALEDTqgeLIRDcivqlhdi 161
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG-SALDWAaAREDERPFPVVGLARPT---LHRE-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 162 seqlyilpsygklnnletseklttkqklesfkniVNKIRFEYDYILMDMRPDMYGLFSEApLGAAEWVFLPVEASLFSFD 241
Cdd:NF041546  69 ----------------------------------LPSLARDYDFVVIDGPPRAEDLARSA-IKAADLVLIPVQPSPYDLW 113

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983538840 242 GLSRSVSYLKERKKDNPLLKigGAFF-NRTkpgknqmeqIENYALGAE-RE-----GIYVFESIIRDSV 303
Cdd:NF041546 114 ASADTVDLIKEAREYTPGLK--AAFVlNRA---------IARTALGREvAEalaeyGLPVLKTRIGQRV 171
PHA02518 PHA02518
ParA-like protein; Provisional
 82-285 5.33e-12

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 64.49  E-value: 5.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSlWnidkqafpmeimdALEDTQGELIRDCIvqlhdi 161
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTD-W-------------AEAREEGEPLIPVV------ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 162 seqlyilpSYGKlnnletseklttkqkleSFKNIVNKIRFEYDYILMDMRPDMYGLFSEApLGAAEWVFLPVEASLFSFD 241
Cdd:PHA02518  61 --------RMGK-----------------SIRADLPKVASGYDYVVVDGAPQDSELARAA-LRIADMVLIPVQPSPFDIW 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 983538840 242 GLSRSVSYLKERKKDNPLLKIgGAFFN-----RTKPGKNQMEQIENYAL 285
Cdd:PHA02518 115 AAPDLVELIKARQEVTDGLPK-FAFIIsraikNTQLYREARKALAGYGL 162
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 90-212 1.04e-10

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 61.74  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCD-YQGNSTSLWNIDKQAfpmEIMDALEDTQGelIRDCIVQLHdiSEQLYIL 168
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADlRGPSLHRMLGLENRP---GLSDVLAGEAS--LEDVIQPTE--VEGLDVL 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 983538840 169 PSyGKLNNlETSEKLTTKQklesFKNIVNKIRFEYDYILMDMRP 212
Cdd:COG0489  174 PA-GPLPP-NPSELLASKR----LKQLLEELRGRYDYVIIDTPP 211
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 90-209 1.15e-09

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: 57.98  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCDyqgnsTSLWNID-----KQAFPMEIMDALE---DTQGELIRDcivqlhDI 161
Cdd:cd02036    9 KGGVGKTTTTANLGVALAKLGKKVLLIDAD-----IGLRNLDlilglENRIVYTLVDVLEgecRLEQALIKD------KR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 983538840 162 SEQLYILPSYgklnnlETSEKltTKQKLESFKNIVNKIRFEYDYILMD 209
Cdd:cd02036   78 WENLYLLPAS------QTRDK--DALTPEKLEELVKELKDSFDFILID 117
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 90-209 9.09e-09

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 55.45  E-value: 9.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCDyqgnsTSLWNIDKqafpmeIM--------DALEDTQGE------LIRDCI 155
Cdd:COG2894   11 KGGVGKTTTTANLGTALALLGKKVVLIDAD-----IGLRNLDL------VMglenrivyDLVDVIEGEcrlkqaLIKDKR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983538840 156 VqlhdisEQLYILPSYgklnnlETSEK--LTTKQklesFKNIVNKIRFEYDYILMD 209
Cdd:COG2894   80 F------ENLYLLPAS------QTRDKdaLTPEQ----MKKLVEELKEEFDYILID 119
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 96-313 5.74e-08

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: 52.97  E-value: 5.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  96 TTCCNsIAGVLTDQGKKVLVMDCD-YQGNSTSLWNIDKQAFpmeIMDALEDTQGelIRDCIVQlhdISEQLYILPSygkL 174
Cdd:COG0455    1 TVAVN-LAAALARLGKRVLLVDADlGLANLDVLLGLEPKAT---LADVLAGEAD--LEDAIVQ---GPGGLDVLPG---G 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 175 NNLETSEKLTTKQKLEsfkNIVNKIRFEYDYILMDMRPdmyGLFSEA--PLGAAEWVFLPVEASLFSFDGLSRSVSYLKE 252
Cdd:COG0455   69 SGPAELAELDPEERLI---RVLEELERFYDVVLVDTGA---GISDSVllFLAAADEVVVVTTPEPTSITDAYALLKLLRR 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983538840 253 RKKDNPLLKIggafFNRTKPGK------NQMEQIENYALGAEREGIYV--FESIIRDSVGIQKAFTYRY 313
Cdd:COG0455  143 RLGVRRAGVV----VNRVRSEAeardvfERLEQVAERFLGVRLRVLGVipEDPAVREAVRRGRPLVLAA 207
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 81-209 2.39e-07

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: 51.18  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDyqgnsTSLWNID-----KQAFPMEIMDALEDT---QGELIR 152
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-----IGLRNLDlllglENRIVYTLVDVVEGEcrlQQALIK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 983538840  153 DCIVqlhdisEQLYILPSYgklnnlETSEKLTTKQklESFKNIVNKIRFEYDYILMD 209
Cdd:TIGR01968  76 DKRL------KNLYLLPAS------QTRDKDAVTP--EQMKKLVNELKEEFDYVIID 118
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 92-212 7.62e-07

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: 49.11  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  92 GVGKTTCCNSIAGVLTDQGKKVLVMDCDY-QGNSTSLWNIDKqafPMEIMDALEDTqgELIRDCIvqLHDISEQLYILPS 170
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPN---EPGLSEVLSGQ--ASLEDVI--QSTNIPNLDVLPA 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 983538840 171 yGKlNNLETSEKLTTkqklESFKNIVNKIRFEYDYILMDMRP 212
Cdd:cd05387  103 -GT-VPPNPSELLSS----PRFAELLEELKEQYDYVIIDTPP 138
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 82-281 1.02e-06

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: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDY-QGNSTSLWNIDKQafPMEIMDALedtQGEL-IRDCIvqlH 159
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADItMANLELILGMEDK--PVTLHDVL---AGEAdIKDAI---Y 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  160 DISEQLYILPSYGKLNNLEtseklttKQKLESFKNIVNKIRFEYDYILMDMrPDMYGLFSEAPLGAAEWVFLPVEASLFS 239
Cdd:TIGR01969  73 EGPFGVKVIPAGVSLEGLR-------KADPDKLEDVLKEIIDDTDFLLIDA-PAGLERDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 983538840  240 F-DGLSRSVSylkERKKDNPLLkigGAFFNRTKPGKNQM--EQIE 281
Cdd:TIGR01969 145 ItDALKTKIV---AEKLGTAIL---GVVLNRVTRDKTELgrEEIE 183
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 82-210 1.80e-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: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDyqgnsTSLWNIDKQ---AFPMEIMDALEDTQGelIRDCIVQl 158
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD-----LGLANLDILlglAPKKTLGDVLKGRVS--LEDIIVE- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 983538840 159 hdISEQLYILPS---YGKLNNLetsekltTKQKLESFKNIVNKIRFEYDYILMDM 210
Cdd:cd02038   73 --GPEGLDIIPGgsgMEELANL-------DPEQKAKLIEELSSLESNYDYLLIDT 118
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 90-145 1.11e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 46.30  E-value: 1.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSlwNIDKQAFPMeIMDALED 145
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTR--NLVGEKIPT-VLDVLRE 61
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 81-355 2.89e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.95  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  81 AKILAFWNqKGGVGK-TTCCNsIAGVLTDQGKKVLVMDCDYQGNSTslWNIDKQAFPMeIMDALEDtqgelirdciVQLH 159
Cdd:PRK13185   2 ALVLAVYG-KGGIGKsTTSSN-LSAAFAKLGKKVLQIGCDPKHDST--FTLTGKLVPT-VIDILEE----------VDFH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 160 --DISEQLYILPSYGKLNNLE--------------TSEKLTTKQKLESFKnivnkirfEYDYILMDMRPDMY-GLFSeAP 222
Cdd:PRK13185  67 seELRPEDFVYEGYNGVDCVEaggppagtgcggyvVGETVKLLKEHHLLD--------DYDVILFDVLGDVVcGGFA-AP 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 223 LGAAEWVfLPVEASlfSFDGL---SRSVSYLKERKKDNPlLKIGGAFFNRTKpGKNQMEQIeNYALGAEREGIYVFESII 299
Cdd:PRK13185 138 LQYADYA-LIVTAN--DFDSIfaaNRIAAAIQAKAKNYK-VRLAGVIANRSA-GTDLIDKF-NEAVGLKVLAHVPDLDAI 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983538840 300 RDSVGIQKaftyrydpTVFlnkfnegEIADFPktqlEPIKNAKSDFMELTTELLNR 355
Cdd:PRK13185 212 RRSRLKGK--------TLF-------EMEETD----PGLEEVQNEYLRLAEQLLAG 248
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 90-284 5.61e-05

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: 44.21  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  90 KGGVGK-TTCCN-SIAgvLTDQGKKVLVMDCDYQGNSTslWNIDKQAFPMeIMDALEDtqgelirdciVQLH--DISEQL 165
Cdd:cd02032    8 KGGIGKsTTSSNlSAA--FAKRGKKVLQIGCDPKHDST--FTLTGFLIPT-VIDVLQS----------VDFHyeEVWPED 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 166 YILPSYGKLNNLE--------------TSEKLTTKQKLESFknivnkirFEYDYILMDMRPDMY-GLFSeAPLGAAEWVf 230
Cdd:cd02032   73 VIFTGYGGVDCVEaggppagtgcggyvVGETVKLLKELNAF--------DEYDVILFDVLGDVVcGGFA-APLNYADYC- 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983538840 231 LPVEASlfSFDGL---SRSVSYLKERKKDNPlLKIGGAFFNRTkpgkNQMEQIENYA 284
Cdd:cd02032  143 LIVTAN--DFDSLfaaNRIAAAVREKAKTYP-VRLAGIIGNRT----DKTDLIDKFV 192
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
82-333 7.15e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 43.97  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840   82 KILAFWNqKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLwnidkqAFPMEIMDALEDTQGE--LIRDciVQLH 159
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRL------LLGGKLQPTVLDTAREkgYVED--VEVE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  160 DIseqlyILPSYGKLNNLETSEK-----------LTTKQKLESfknivNKIRFEYDYILMDMRPDMY-GLFSeAPL--GA 225
Cdd:pfam00142  72 DV-----VYKGYGGVKCVESGGPepgvgcagrgvITAINLLEE-----LGAYDDLDFVLYDVLGDVVcGGFA-MPIreGK 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  226 AEWVFLPVEA---SLFSFDGLSRSVSYLKERKKdnplLKIGGAFFNrTKPGKNQMEQIENYalgAEREGIYVFESIIRDS 302
Cdd:pfam00142 141 AQEIYIVTSNemmALYAANNIAKGIQKYAKSGG----VRLGGIICN-SRKVDDERELIDAF---AEELGTQVLHFVPRDN 212

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 983538840  303 VgIQKA-----FTYRYDPTV-FLNKFNE--GEIADFPKT 333
Cdd:pfam00142 213 I-VRKAelrkqTVIEYAPDSeQAQEYRElaRKILENPKG 250
PRK10818 PRK10818
septum site-determining protein MinD;
81-209 8.42e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 43.77  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  81 AKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDyqgnsTSLWNIDKqafpmeIM--------DALEDTQGE--- 149
Cdd:PRK10818   2 ARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD-----IGLRNLDL------IMgcerrvvyDFVNVIQGDatl 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983538840 150 ---LIRDcivqlhDISEQLYILPSYgklnnlETSEK-LTTKQKLESFKNIVNKIRFeyDYILMD 209
Cdd:PRK10818  71 nqaLIKD------KRTENLYILPAS------QTRDKdALTREGVAKVLDDLKAMDF--EFIVCD 120
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 90-119 1.18e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 43.23  E-value: 1.18e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCD 119
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDAD 37
chlL CHL00072
photochlorophyllide reductase subunit L
 90-270 1.41e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 43.19  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  90 KGGVGK-TTCCN-SIAgvLTDQGKKVLVMDCDYQGNSTslwnIDKQAFPM-EIMDALEdtqgelIRDciVQLHDISEQLY 166
Cdd:CHL00072   8 KGGIGKsTTSCNiSIA--LARRGKKVLQIGCDPKHDST----FTLTGFLIpTIIDTLQ------SKD--YHYEDVWPEDV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840 167 ILPSYGKLNNLE--------------TSEKLTTKQKLESFknivnkirFEYDYILMDMRPDMY-GLFSeAPLGAAEWVFL 231
Cdd:CHL00072  74 IYKGYGGVDCVEaggppagagcggyvVGETVKLLKELNAF--------YEYDIILFDVLGDVVcGGFA-APLNYADYCII 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 983538840 232 PVEAslfSFDGL---SRSVSYLKERKKDNPlLKIGGAFFNRT 270
Cdd:CHL00072 145 ITDN---GFDALfaaNRIAASVREKARTHP-LRLAGLVGNRT 182
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 82-127 2.03e-04

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: 42.35  E-value: 2.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 983538840  82 KILAFWNqKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSL 127
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLL 45
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 82-119 2.91e-04

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: 39.72  E-value: 2.91e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 983538840  82 KILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCD 119
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 90-127 2.96e-04

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: 42.11  E-value: 2.96e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 983538840  90 KGGVGK-TTCCNsIAGVLTDQGKKVLVMDCDYQGNSTSL 127
Cdd:cd02040    8 KGGIGKsTTASN-LSAALAEMGKKVLHVGCDPKADSTRL 45
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 86-148 2.97e-04

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 42.77  E-value: 2.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983538840   86 FWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNStslwnidKQAFPMEIMDALEDTQG 148
Cdd:TIGR04291   7 FFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNV-------GQVFGQTIGNKITAIAG 62
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 90-116 3.47e-04

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: 41.72  E-value: 3.47e-04
                         10        20
                 ....*....|....*....|....*..
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVM 116
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLV 34
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
79-116 3.92e-04

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.73  E-value: 3.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 983538840  79 DAAKILAFWNqKGGVGKTTCCNSIAGVLTDQGKKVLVM 116
Cdd:COG0003    1 DMTRIIFFTG-KGGVGKTTVAAATALALAERGKRTLLV 37
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 90-124 5.14e-04

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: 40.95  E-value: 5.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNS 124
Cdd:cd02037    9 KGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPS 43
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 86-150 5.54e-04

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 41.18  E-value: 5.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983538840   86 FWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALE----DTQGEL 150
Cdd:pfam02374   5 FFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEPTKVKENLSameiDPNMEL 73
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 90-147 7.85e-04

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: 40.76  E-value: 7.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  90 KGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIM--DALEDTQ 147
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKTigDIRERTG 67
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 72-119 1.17e-03

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.84  E-value: 1.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 983538840   72 QLIELVQDAAKI---LAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCD 119
Cdd:TIGR04291 308 SLSRLIDEIAKSekgLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 79-210 4.21e-03

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 38.29  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983538840  79 DAAKILAFWNQKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSLWNIDKQAFPMEIMDALEDTQGELIRDCIVQL 158
Cdd:cd17869    1 DATSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLMSDHLYTLKSRKANLADKLESCV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 983538840 159 HDISEQLYILPSY---GKLNNLETSEKLTTKQKLESFKNivnkirfeYDYILMDM 210
Cdd:cd17869   81 KQHESGVYYFSPFksaLDILEIKKDDILHMITKLVEAHA--------YDYIIMDL 127
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 82-127 4.72e-03

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 38.66  E-value: 4.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 983538840  82 KILAFWNqKGGVGKTTCCNSIAGVLTDQGKKVLVMDCDYQGNSTSL 127
Cdd:cd02033   32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSL 76
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 92-138 9.20e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 36.85  E-value: 9.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 983538840   92 GVGKTTCCNSIAGVLTDQGKKVLVMDCD-YQGNST-----SLWNIDKQAFPME 138
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDvGQSEIGppgtiSLALVERPIDVPE 56
 
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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