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Conserved domains on  [gi|1242559760|gb|ATA80565|]
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chromosome partitioning protein ParA [Capnocytophaga sputigena]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

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 ...
 3-254 4.64e-126

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: 358.02  E-value: 4.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIAAHINLVAIEIELVDKEQREYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLL 162
Cdd:COG1192    82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 163 NTIKSVQKTFNPDLDIEGLLLTMYDARLRLSNQVVEEVQKHFSDMVFKTIIQRNVRLSEAPSFGETIINYDATSKGATNH 242
Cdd:COG1192   162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                         250
                  ....*....|..
gi 1242559760 243 INLAQEIIDKNK 254
Cdd:COG1192   242 RALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-254 4.64e-126

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: 358.02  E-value: 4.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIAAHINLVAIEIELVDKEQREYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLL 162
Cdd:COG1192    82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 163 NTIKSVQKTFNPDLDIEGLLLTMYDARLRLSNQVVEEVQKHFSDMVFKTIIQRNVRLSEAPSFGETIINYDATSKGATNH 242
Cdd:COG1192   162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                         250
                  ....*....|..
gi 1242559760 243 INLAQEIIDKNK 254
Cdd:COG1192   242 RALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 2.35e-89

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: 262.13  E-value: 2.35e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   2 GKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPN 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  82 LDLIAAHINLVAIEIELVDKEQREYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1242559760 162 LNTIKSVQKTFNPDLDI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 3.41e-49

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: 158.09  E-value: 3.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLgidvdsiehgtyellehtmeakdmivqtsspnl 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 dliaahinlvaieielvdkeqreymlkkalesikdeYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLL 162
Cdd:cd02042    48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1242559760 163 NTIKSVQKTFNPDLDIEGLLLTMYDARLRLSNQVVEEVQ 201
Cdd:cd02042    92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-148 1.74e-29

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: 113.92  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLG----IDVDsiEHGT-YELLEHTMEAKDM---IV 75
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGyqpeFDVG--ENETlYGAIRYDDERRPIseiIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  76 QTSSPNLDLIAAHINLVAIEIE----LVDKEQREYM----LKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVP 147
Cdd:TIGR03453 184 KTYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLIT 263


                  .
gi 1242559760 148 I 148
Cdd:TIGR03453 264 V 264
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-214 1.32e-28

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 111.61  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDA-DPQANATSGLGIDVDSIEHGTYELLEHTMEAKD----MIVQTS 78
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHGWVPDLHIHAEDTLLPFYLGEKDdatyAIKPTC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  79 SPNLDLIAAHINLVAIEIELVDKEQR-------EYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCE 151
Cdd:PRK13705  188 WPGLDIIPSCLALHRIETELMGKFDEgklptdpHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242559760 152 YF----ALEGLGKLLNTIKSVQ-KTFNPDLDIeglLLTMYDARLRLSNQVVEE-VQKHFSDMVFKTIIQ 214
Cdd:PRK13705  268 LFdytsALQFFDMLRDLLKNVDlKGFEPDVRI---LLTKYSNSNGSQSPWMEEqIRDAWGSMVLKNVVR 333
ParA_partition NF041546
ParA family partition ATPase;
4-248 2.49e-25

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 98.78  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATsglgidvdsiehGTYELLEHtmeakdmivqtsspnld 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL------------DWAAARED----------------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  84 liAAHINLVAIeielvDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLLN 163
Cdd:NF041546   52 --ERPFPVVGL-----ARPT----LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 164 TIKSVQKtFNPDLDIeGLLLTMYDARLRLSNQVVEEVQKHFSDmVFKTIIQRNVRLSEAPSFGETIINYDATSKgATNHI 243
Cdd:NF041546  121 LIKEARE-YTPGLKA-AFVLNRAIARTALGREVAEALAEYGLP-VLKTRIGQRVAFAESAAEGLTVFEAEPDGK-AAREI 196


                  ....*.
gi 1242559760 244 N-LAQE 248
Cdd:NF041546  197 RaLAKE 202
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-254 4.64e-126

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: 358.02  E-value: 4.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIAAHINLVAIEIELVDKEQREYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLL 162
Cdd:COG1192    82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 163 NTIKSVQKTFNPDLDIEGLLLTMYDARLRLSNQVVEEVQKHFSDMVFKTIIQRNVRLSEAPSFGETIINYDATSKGATNH 242
Cdd:COG1192   162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                         250
                  ....*....|..
gi 1242559760 243 INLAQEIIDKNK 254
Cdd:COG1192   242 RALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 2.35e-89

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: 262.13  E-value: 2.35e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   2 GKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPN 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  82 LDLIAAHINLVAIEIELVDKEQREYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1242559760 162 LNTIKSVQKTFNPDLDI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-229 6.22e-57

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: 181.39  E-value: 6.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   5 IAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATS--GLGIDVDSIEHGTYELLEHTMEAKD--MIVQTSSP 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSveGLEGDIAPALQALAEGLKGRVNLDPilLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  81 NLDLIAAHINLVAIEIELVDKEqREYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGK 160
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPR-KEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 161 LLNTIKSVQKTFNP-DLDIEGLLLTMYDARLRLSNQVVEEVQKHFSDMVFKtIIQRNVRLSEAPSFGETI 229
Cdd:pfam01656 160 LGGVIAALVGGYALlGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLG-VIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 3.41e-49

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: 158.09  E-value: 3.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLgidvdsiehgtyellehtmeakdmivqtsspnl 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 dliaahinlvaieielvdkeqreymlkkalesikdeYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLL 162
Cdd:cd02042    48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1242559760 163 NTIKSVQKTFNPDLDIEGLLLTMYDARLRLSNQVVEEVQ 201
Cdd:cd02042    92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-148 1.74e-29

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: 113.92  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLG----IDVDsiEHGT-YELLEHTMEAKDM---IV 75
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGyqpeFDVG--ENETlYGAIRYDDERRPIseiIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  76 QTSSPNLDLIAAHINLVAIEIE----LVDKEQREYM----LKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVP 147
Cdd:TIGR03453 184 KTYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLIT 263


                  .
gi 1242559760 148 I 148
Cdd:TIGR03453 264 V 264
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-214 1.32e-28

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 111.61  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDA-DPQANATSGLGIDVDSIEHGTYELLEHTMEAKD----MIVQTS 78
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHGWVPDLHIHAEDTLLPFYLGEKDdatyAIKPTC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  79 SPNLDLIAAHINLVAIEIELVDKEQR-------EYMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCE 151
Cdd:PRK13705  188 WPGLDIIPSCLALHRIETELMGKFDEgklptdpHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242559760 152 YF----ALEGLGKLLNTIKSVQ-KTFNPDLDIeglLLTMYDARLRLSNQVVEE-VQKHFSDMVFKTIIQ 214
Cdd:PRK13705  268 LFdytsALQFFDMLRDLLKNVDlKGFEPDVRI---LLTKYSNSNGSQSPWMEEqIRDAWGSMVLKNVVR 333
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-214 1.75e-25

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 103.17  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDA-DPQANATSGLGIDVDSIEHGTYELLEHTMEAKD----MIVQTS 78
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGnDPQGTASMYHGYVPDLHIHADDTLLPFYLGERDnaeyAIKPTC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  79 SPNLDLIAAHINLVAIEIELVDKEQRE-------YMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCE 151
Cdd:PHA02519  188 WPGLDIIPSCLALHRIETDLMQYHDAGklphpphLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAE 267

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242559760 152 YF----ALEGLGKLLNTIKSVQ-KTFNPDLDiegLLLTMYDarLRLSNQ---VVEEVQKHFSDMVFKTIIQ 214
Cdd:PHA02519  268 LFdyvsVLQFFTMLLDLLATVDlGGFEPVVR---LLLTKYS--LTVGNQsrwMEEQIRNTWGSMVLRQVVR 333
ParA_partition NF041546
ParA family partition ATPase;
4-248 2.49e-25

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 98.78  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATsglgidvdsiehGTYELLEHtmeakdmivqtsspnld 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL------------DWAAARED----------------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  84 liAAHINLVAIeielvDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLLN 163
Cdd:NF041546   52 --ERPFPVVGL-----ARPT----LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 164 TIKSVQKtFNPDLDIeGLLLTMYDARLRLSNQVVEEVQKHFSDmVFKTIIQRNVRLSEAPSFGETIINYDATSKgATNHI 243
Cdd:NF041546  121 LIKEARE-YTPGLKA-AFVLNRAIARTALGREVAEALAEYGLP-VLKTRIGQRVAFAESAAEGLTVFEAEPDGK-AAREI 196


                  ....*.
gi 1242559760 244 N-LAQE 248
Cdd:NF041546  197 RaLAKE 202
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-222 2.78e-23

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 97.44  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGI----DVDSIE--HGTYELLEHTMEAKDMIVQ 76
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlpetDVGANEtlYAAIRYDDTRRPLRDVIRP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  77 TSSPNLDLIAAHINLVAIE----IELVDKEQREYM----LKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPI 148
Cdd:PRK13869  202 TYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITV 281

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242559760 149 QCEYFALEGLGKLL---NTIKSVQKTFNPDL--DIEGLLLTMYDARLRLSNQVVEEVQKHFSDMVFKTIIQRNVRLSEA 222
Cdd:PRK13869  282 HPQMLDIASMSQFLlmtRDLLGVVKEAGGNLqyDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDA 360
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-252 4.02e-22

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: 91.10  E-value: 4.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  18 TTSVNLAASLGVLEKKVLLIDADPQ-ANATSGLGIDVdsiEHGTYELLEHTMEAKDMIVQTSSpNLDLIAAHINLVaiEI 96
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEP---KATLADVLAGEADLEDAIVQGPG-GLDVLPGGSGPA--EL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  97 ELVDKEQReymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLLNTIKSVQKTFNPdl 176
Cdd:COG0455    75 AELDPEER---LIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVRRA-- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 177 dieGLLLTMYDAR---LRLSNQVVEEVQKHFS-DMVFKTIIQRNVRLSEAPSFGETIINYDATSKGATNHINLAQEIIDK 252
Cdd:COG0455   150 ---GVVVNRVRSEaeaRDVFERLEQVAERFLGvRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 4-189 1.17e-20

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: 88.32  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADP-QANATSGLGIDvdsIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGLE---NRPGLSDVLAGEASLEDVIQPTEVEGL 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIAAhINLVAIEIELVDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTA-ANSVIVPIQCEYFALEGLGKL 161
Cdd:COG0489   171 DVLPA-GPLPPNPSELLASKR----LKQLLEELRGRYDYVIIDTPPGLGVADATLLASlVDGVLLVVRPGKTALDDVRKA 245

                         170       180
                  ....*....|....*....|....*...
gi 1242559760 162 LNTIKSVqktfnpDLDIEGLLLTMYDAR 189
Cdd:COG0489   246 LEMLEKA------GVPVLGVVLNMVCPK 267
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-249 4.38e-20

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: 85.72  E-value: 4.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD-PQANATSGLG----IDVDSIehgtyELLEHTMEAKDMIVQT 77
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGlenrIVYTLV-----DVLEGECRLEQALIKD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  78 S-SPNLDLIAAHINLvaiEIELVDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALE 156
Cdd:cd02036    76 KrWENLYLLPASQTR---DKDALTPEK----LEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 157 GLGKLLNTIKSVQKTfnpdldIEGLLLTMYDARLRLSNQV--VEEVQKHFSDMVFkTIIQRNVRLSEAPSFGETIINYDA 234
Cdd:cd02036   149 DADRVIGLLESKGIV------NIGLIVNRYRPEMVKSGDMlsVEDIQEILGIPLL-GVIPEDPEVIVATNRGEPLVLYKP 221

                         250
                  ....*....|....*
gi 1242559760 235 TSKGATNHINLAQEI 249
Cdd:cd02036   222 NSLAAKAFENIARRL 236
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-146 1.51e-19

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: 84.16  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD-PQANATSGLGIdvdSIEHGTYELLEHTMEAKDMIVQTsSPN 81
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGL---APKKTLGDVLKGRVSLEDIIVEG-PEG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242559760  82 LDLIAAHINLVaiEIELVDKEQREyMLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIV 146
Cdd:cd02038    77 LDIIPGGSGME--ELANLDPEQKA-KLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
PHA02518 PHA02518
ParA-like protein; Provisional
 3-248 4.76e-19

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 82.59  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGlgidVDSIEHGtyellEHTMEAKDMivqtsSPNl 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW----AEAREEG-----EPLIPVVRM-----GKS- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 dliaahinlvaieielvdkeqreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGKLL 162
Cdd:PHA02518   66 -------------------------IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 163 NTIKSVQKtFNPDLDIEGLLLTMYDARLRLSNQvVEEVQKHFSDMVFKTIIQRNVRLSEAPSFGETIINYDATSKGATNH 242
Cdd:PHA02518  121 ELIKARQE-VTDGLPKFAFIISRAIKNTQLYRE-ARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198


                  ....*.
gi 1242559760 243 INLAQE 248
Cdd:PHA02518  199 IQLVKE 204
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-250 8.17e-19

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: 82.86  E-value: 8.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADpQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSpNL 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD-ITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPF-GV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIAAHINLVAIEIELVDKeqreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFAleglgkLL 162
Cdd:TIGR01969  79 KVIPAGVSLEGLRKADPDK------LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISS------IT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 163 NTIKSVQKTFNPDLDIEGLLLTMYDarlRLSNQV-VEEVQKHFSDMVFKTIIQR-NVRlsEAPSFGETIINYDATSKGAT 240
Cdd:TIGR01969 147 DALKTKIVAEKLGTAILGVVLNRVT---RDKTELgREEIETILEVPVLGVVPEDpEVR--RAAAFGEPVVIYNPNSPAAQ 221

                         250
                  ....*....|
gi 1242559760 241 NHINLAQEII 250
Cdd:TIGR01969 222 AFMELAAELA 231
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-200 1.30e-18

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: 83.63  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   2 GKIIAIANQKGGVGKTTTSVNLAASL-GVLEKKVLLIDADPQA-NATSGLGIDVDsieHGTYELLEHTMEAKDMIVQTS- 78
Cdd:COG4963   102 GRVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFgDVALYLDLEPR---RGLADALRNPDRLDETLLDRAl 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  79 ---SPNLDLIAAHINLVaiEIELVDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFAL 155
Cdd:COG4963   179 trhSSGLSVLAAPADLE--RAEEVSPEA----VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSL 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1242559760 156 EGLGKLLNTIKSVQKtfnPDLDIEgLLLTMYDARLRLSNQVVEEV 200
Cdd:COG4963   253 RNAKRLLDLLRELGL---PDDKVR-LVLNRVPKRGEISAKDIEEA 293
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-141 1.03e-16

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: 75.68  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD---PQANATSGLGidvdsIEHGTYELLEHTMEAKDMIVQTSS 79
Cdd:cd05387    20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGLP-----NEPGLSEVLSGQASLEDVIQSTNI 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1242559760  80 PNLDLIAAHiNLVAIEIELVDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAA 141
Cdd:cd05387    95 PNLDVLPAG-TVPPNPSELLSSPR----FAELLEELKEQYDYVIIDTPPVLAVADALILAPL 151
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-146 9.66e-14

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: 67.85  E-value: 9.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLgIDVDSIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGT-FKSQNKITGLTNFLSGTTDLSDAICDTNIENL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242559760  83 DLIAAHiNLVAIEIELVdkeQREYMlKKALESIKDEYDYILIDCAPsLGLITLNALTAA---NSVIV 146
Cdd:TIGR01007  97 DVITAG-PVPPNPTELL---QSSNF-KTLIETLRKRFDYIIIDTPP-IGTVTDAAIIARacdASILV 157
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-126 1.19e-13

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 68.55  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   1 MGKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADpqanatSGL-------GID-------VDSIEhGTYELleh 66
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD------IGLrnldlvmGLEnrivydlVDVIE-GECRL--- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  67 tMEAkdMIVQTSSPNLDLIAAHINLvaiEIELVDKEQreymLKKALESIKDEYDYILIDC 126
Cdd:COG2894    71 -KQA--LIKDKRFENLYLLPASQTR---DKDALTPEQ----MKKLVEELKEEFDYILIDS 120
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-146 1.49e-12

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: 65.44  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   2 GKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD-PQANATSGLGIDVDSIehgtYELLEhTMEAK-----DMIV 75
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiGLRNLDLLLGLENRIV----YTLVD-VVEGEcrlqqALIK 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242559760  76 QTSSPNLDLIAAHINLvaiEIELVDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIV 146
Cdd:TIGR01968  76 DKRLKNLYLLPASQTR---DKDAVTPEQ----MKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIV 139
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-239 1.50e-12

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: 65.44  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQaNATsGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ-NLL-RLHFGMDWSVRDGWARALLNGADWAAAAYRSPDGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIA-AHINLVAIEIELvdkEQREYMLKKALESIK-DEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGK 160
Cdd:TIGR03371  80 LFLPyGDLSADEREAYQ---AHDAGWLARLLQQLDlAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242559760 161 LLNTIKSVQKTFnpdlDIEGLLLTMYDARLRLSNQVVEEVQKHFSDMVFKTIIQRNVRLSEAPSFGETIINYDATSKGA 239
Cdd:TIGR03371 157 LALALFAGSGPR----DGPRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQAA 231
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-230 2.12e-12

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: 64.61  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEK-KVLLIDADPQAnATSGLGIDVDSiEHGTYELLE--HTMEA---KDMIVQ 76
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPF-GDLGLYLNLRP-DYDLADVIQnlDRLDRtllDSAVTR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  77 TSSpNLDLIAAHINLVAIEIelVDKEQreymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALE 156
Cdd:cd03111    79 HSS-GLSLLPAPQELEDLEA--LGAEQ----VDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242559760 157 GLGKLLNTIKSvqktFNPDLDIEGLLLTMYDARLRLSNQVVEEVqkhFSDMVFKTIIQRNVRLSEAPSFGETII 230
Cdd:cd03111   152 NARRLLDSLRE----LEGSSDRLRLVLNRYDKKSEISPKDIEEA---LGLEVFATLPNDYKAVSESANTGRPLV 218
minD CHL00175
septum-site determining protein; Validated
 1-146 4.04e-11

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 61.71  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   1 MGKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD-PQANATSGLGIDvDSIEHGTYELLEHTMEAKDMIVQTSS 79
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLE-NRVLYTAMDVLEGECRLDQALIRDKR 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1242559760  80 -PNLDLIAAHINlvaieielvdkEQREYMLKKALESIKD-----EYDYILIDCAPSLGLITLNALTAANSVIV 146
Cdd:CHL00175   93 wKNLSLLAISKN-----------RQRYNVTRKNMNMLVDslknrGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 3-126 1.17e-10

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 59.80  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANqKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTY----ELLEHTMEAKDMIVQTS 78
Cdd:COG3640     1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLIKPLgemrELIKERTGAPGGGMFKL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  79 SPNLDLI-------AAHINLVAI-EIELVDKEQREYM---LKKALES-IKDEYDYILIDC 126
Cdd:COG3640    80 NPKVDDIpeeylveGDGVDLLVMgTIEEGGSGCYCPEnalLRALLNHlVLGNYEYVVVDM 139
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-40 2.68e-10

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: 59.00  E-value: 2.68e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD 40
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 1.86e-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: 55.97  E-value: 1.86e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD 40
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-161 3.98e-08

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: 52.84  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLlidadpqanatsglGIDVDSIEHGTYELLEHTMEAKDmivqtsSPNLD 83
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVA--------------AIDLDLRQRTFHRYFENRSATAD------RTGLS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  84 L-IAAHINLVAIEIELVDKEQREYM--LKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQCEYFALEGLGK 160
Cdd:pfam09140  62 LpTPEHLNLPDNDVAEVPDGENIDDarLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLLGQ 141


                  .
gi 1242559760 161 L 161
Cdd:pfam09140 142 V 142
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-135 9.75e-08

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: 51.35  E-value: 9.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDS-----IEHG--------TYELLEHTMEAKD----- 72
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGGetpvkGAPNlwameidpEEALEEYWEEVKEllaqy 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242559760  73 ----------MIVQTSSPNLDLIAAhinLVAIeielvdkeqREYMLkkalesiKDEYDYILIDCAP---SLGLITL 135
Cdd:cd02035    88 lrlpgldevyAEELLSLPGMDEAAA---FDEL---------REYVE-------SGEYDVIVFDTAPtghTLRLLSL 144
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-46 1.84e-07

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 50.73  E-value: 1.84e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1242559760   1 MGKIIAIANqKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANAT 46
Cdd:PRK13185    1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 3-187 2.06e-07

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: 51.64  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD-PQANATSGLGIDVDSiehGTYELLEHTMEAKDMIVQTSSPN 81
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFGKAPKP---GLLDLLAGEASIEAGIHRDQRPG 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  82 LDLIAAHinlvaiEIELVDKEQREYMLKKAL----ESIKDEYDYILIDCAPSLGLITLNALTA-ANSVIVPIQceyFALE 156
Cdd:TIGR01005 631 LAFIAAG------GASHFPHNPNELLANPAMaeliDNARNAFDLVLVDLAALAAVADAAAFAAlADGILFVTE---FERS 701

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1242559760 157 GLGKLLNTIKSVQKTfnpDLDIEGLLLTMYD 187
Cdd:TIGR01005 702 PLGEIRDLIHQEPHA---NSDVLGVIFNALD 729
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-49 3.10e-07

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: 50.06  E-value: 3.10e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGL 49
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-135 5.57e-07

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 49.66  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   4 IIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADpqanatsglgIDVDSIEHgtyeLLEHTMEakdmivQTSSPN-- 81
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD----------IYGPSIPT----MLGAEDQ------RPTSPDgt 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242559760  82 -LDLIAAHiNLVAIEIE-LVDKEQ----REYMLKKAL-----ESIKDEYDYILIDCAPSLGLITL 135
Cdd:PRK11670  169 hMAPIMAH-GLATNSIGyLVTDDNamvwRGPMASKALmqmlqETLWPDLDYLVLDMPPGTGDIQL 232
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-256 9.64e-07

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 48.61  E-value: 9.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGL-GIDVDSIEHGTYELLEHTMEAKDMI---------VQTSSP 80
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLvGEKIPTVLDVLREKGIDNLGLEDIIyegfngiycVESGGP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  81 NLDL-IAAHINLVAIEielvdkeqreyMLKK--ALESIKDE---YDyILID--CApslGLITLNALTAANSVIVPIQCEY 152
Cdd:PRK13230   89 EPGYgCAGRGVITAID-----------LLKKlgVFEELGPDvviYD-ILGDvvCG---GFAMPLQKGLADDVYIVTTCDP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 153 FALEGLGKLLNTIKSVQKTFNPDLDieGLLltmYDARLRLSN-QVVEEVQKHFSDMVFKTIIQRNVrLSEAPSFGETIIN 231
Cdd:PRK13230  154 MAIYAANNICKGIKRFAKRGKSALG--GII---YNGRSVIDApDIVEEFAKKIGTNVIGKIPMSNI-ITEAEIYGKTVIE 227

                         250       260
                  ....*....|....*....|....*
gi 1242559760 232 YDATSKGATNHINLAQEIIDKNKTA 256
Cdd:PRK13230  228 YAPDSEISNIFRELAEAIYENNTGT 252
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 3-46 1.01e-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: 48.45  E-value: 1.01e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1242559760   3 KIIAIANqKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANAT 46
Cdd:cd02032     1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-97 1.39e-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: 45.88  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDsIEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGGGGLETG-LLLGTIVALLALKKADEVIVVVDPELG 79

                          90
                  ....*....|....*
gi 1242559760  83 DLIAAHINLVAIEIE 97
Cdd:cd01983    80 SLLEAVKLLLALLLL 94
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
3-47 2.17e-06

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 47.82  E-value: 2.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1242559760   3 KIIAIANqKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATS 47
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTR 44
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-49 5.22e-06

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: 46.35  E-value: 5.22e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGL 49
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLL 46
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-129 8.56e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 45.97  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIehgtyellehtmeakdmIVQTSSPNLDliaahin 90
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNE-----------------PTEVAVPNLY------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242559760  91 lvAIEIElVDKEQREYM--LKKALESI------------------------------KDEYDYILIDCAPS 129
Cdd:COG0003    67 --ALEID-PEAELEEYWerVRAPLRGLlpsagvdelaeslpgteelaaldellelleEGEYDVIVVDTAPT 134
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 5-57 1.25e-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: 45.38  E-value: 1.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1242559760   5 IAIANqKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIE 57
Cdd:cd02034     3 IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLP 54
PRK09841 PRK09841
tyrosine-protein kinase;
3-183 3.54e-05

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 44.51  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLgIDVDSiEHGTYELLEHTMEAKDMIVQTSSPNL 82
Cdd:PRK09841  532 NILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNL-FTVSN-EHGLSEYLAGKDELNKVIQHFGKGGF 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  83 DLIA-AHINLVAIEIELVDKeqreymLKKALESIKDEYDYILIDCAPSLGLI--TLNALTAANSVIVPiqceYFALEGLG 159
Cdd:PRK09841  610 DVITrGQVPPNPSELLMRDR------MRQLLEWANDHYDLVIVDTPPMLAVSdaAVVGRSVGTSLLVA----RFGLNTAK 679

                         170       180
                  ....*....|....*....|....
gi 1242559760 160 KLLNTIKSVQKTfnpDLDIEGLLL 183
Cdd:PRK09841  680 EVSLSMQRLEQA---GVNIKGAIL 700
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 11-228 3.92e-05

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: 43.88  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDvdsIEHGTYELLEhtmeakdmivqtsspnldliaahiN 90
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQK---FGHEPTKVKE------------------------N 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  91 LVAIEI-------ELVDKEQREY-------MLKKALESI---------------------KDEYDYILIDCAP---SLGL 132
Cdd:pfam02374  62 LSAMEIdpnmeleEYWQEVQKYMnallglrMLEGILAEElaslpgideaasfdefkkymdEGEYDVVVFDTAPtghTLRL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760 133 ITLnaltaansvivPIQCEYFaLEGLGKLLNTIKSVQKTFNP--DLDIEGLLLTMYDARLRLsnqvvEEVQKHFSDMVFK 210
Cdd:pfam02374 142 LSL-----------PTVLGWY-LEKIVKLKNQIGPLAKPFLGmgGVSIPEALESLEETKERI-----ERAREILTDPERT 204

                         250
                  ....*....|....*...
gi 1242559760 211 TIiqRNVRLSEAPSFGET 228
Cdd:pfam02374 205 SF--RLVCIPEKMSLYET 220
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-40 1.23e-04

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: 42.37  E-value: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1242559760   4 IIAIANQKGGVGKTTtsvnLAASLGVLEKKVLLIDAD 40
Cdd:cd03110     1 IIAVLSGKGGTGKTT----ITANLAVLLYNVILVDCD 33
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 3-49 2.59e-04

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: 41.74  E-value: 2.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1242559760   3 KIIAIANqKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGL 49
Cdd:cd02033    32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLL 77
PRK10818 PRK10818
septum site-determining protein MinD;
1-40 3.06e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 41.08  E-value: 3.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1242559760   1 MGKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDAD 40
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 3-149 3.16e-04

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 40.82  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760   3 KIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPqANATsGLGIDVDsIEHGTYELLEHtMEAKDMivQTSS--- 79
Cdd:pfam06564   2 KILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSP-DNLL-RLHFNVP-FEHRQGWARAE-LDGADW--RDAAley 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242559760  80 -PNLDLIA-AHINLVAIEI--ELVDKEQReymLKKALESIKDEYDYILIDCAPSLGLITLNALTAANSVIVPIQ 149
Cdd:pfam06564  76 tPGLDLLPfGRLSVEEQENlqQLQPDPGA---WCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVN 146
chlL CHL00072
photochlorophyllide reductase subunit L
 11-46 3.38e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 41.26  E-value: 3.38e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANAT 46
Cdd:CHL00072    8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDST 43
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-44 4.46e-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: 41.23  E-value: 4.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQAN 44
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-129 1.35e-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: 39.69  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242559760  11 KGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVDSIEHGTYELLEHTMEAKDMIVQTSSPNLDliAAHIN 90
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKELD--EDGKA 406

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1242559760  91 LvaIEIELVDKEQREYMLKKALESIKDEYD--YILIDCAPS 129
Cdd:TIGR04291 407 Y--LEEDLRSPCTEEIAVFQAFSRIIREAGdrFVVMDTAPT 445
nifH PRK13233
nitrogenase iron protein;
1-46 1.79e-03

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 39.03  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1242559760   1 MGKIIAIANqKGGVGKTTTSVNLAASLGVL-EKKVLLIDADPQANAT 46
Cdd:PRK13233    1 MTRKIAIYG-KGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADST 46
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 1-49 6.35e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 37.08  E-value: 6.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1242559760   1 MGKIIAIANqKGGVGKTTTSVNLAASLGVlEKKVLLIDADPQANATSGL 49
Cdd:PRK13231    1 VMKKIAIYG-KGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTRTL 47
 
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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