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Conserved domains on  [gi|755043161|ref|WP_042395657|]
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ParA family protein [Pseudescherichia vulneris]

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
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 ...
2-203 1.25e-38

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: 138.45  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTgLTLGLDDYEsliqfydskQNTDLFNSLAPEFSLE 81
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLT-SGLGLDPDD---------LDPTLYDLLLDDAPLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  82 SVnhtpvgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlpVLRKFVgafnkltRKIADEHniDIVLVDMSPSV 161
Cdd:COG1192   71 DA---------IVPTEIPGLDLIPANIDLAGAEIELVSRPGREL---RLKRAL-------APLADDY--DYILIDCPPSL 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755043161 162 SSTNQCILMSSDYFIIPISPDFYCYQAIDSLSNVLPKWAKEI 203
Cdd:COG1192  130 GLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDL 171
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
2-203 1.25e-38

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: 138.45  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTgLTLGLDDYEsliqfydskQNTDLFNSLAPEFSLE 81
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLT-SGLGLDPDD---------LDPTLYDLLLDDAPLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  82 SVnhtpvgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlpVLRKFVgafnkltRKIADEHniDIVLVDMSPSV 161
Cdd:COG1192   71 DA---------IVPTEIPGLDLIPANIDLAGAEIELVSRPGREL---RLKRAL-------APLADDY--DYILIDCPPSL 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755043161 162 SSTNQCILMSSDYFIIPISPDFYCYQAIDSLSNVLPKWAKEI 203
Cdd:COG1192  130 GLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDL 171
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-196 4.93e-30

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: 113.45  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161    2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTgLTLGLDDYEsliqfydskQNTDLFNSLAPEFSLE 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAT-SGLGIDKNN---------VEKTIYELLIGECNIE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   82 SVnhtpvgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlpvlrkfvgAFNKLTRKIADEHniDIVLVDMSPSV 161
Cdd:pfam13614  71 EA---------IIKTVIENLDLIPSNIDLAGAEIELIGIENREN----------ILKEALEPVKDNY--DYIIIDCPPSL 129
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 755043161  162 SSTNQCILMSSDYFIIPISPDFYcyqAIDSLSNVL 196
Cdd:pfam13614 130 GLLTINALTASDSVLIPVQCEYY---ALEGLSQLL 161
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-203 1.43e-21

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: 89.14  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLtlglddyesliqFYdskqntdlfnslapefsles 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSW------------LY-------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  83 vnhtpvgttpitgtdnpnlyilagnirfseldtqiatamtssntlpvlrkfvgafnkltrkiadehniDIVLVDMSPSVS 162
Cdd:cd02042   49 --------------------------------------------------------------------DYILIDTPPSLG 60
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755043161 163 STNQCILMSSDYFIIPISPDFYCYQAIDSLSNVLPKWAKEI 203
Cdd:cd02042   61 LLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQL 101
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
4-175 1.56e-14

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: 74.24  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161    4 VISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLtLGlddyeSLIQFyDSKQNTDLFNSLapEFSLESV 83
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSAL-FG-----YQPEF-DVGENETLYGAI--RYDDERR 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   84 NHTPVgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlPVLRKFvgaFNKLTRKIAD-EHNIDIVLVDMSPS-- 160
Cdd:TIGR03453 177 PISEI----IRKTYFPGLDLVPGNLELMEFEHETPRALSRGQ--GGDTIF---FARVGEALAEvEDDYDVVVIDCPPQlg 247
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 755043161  161 -----------------------VSSTNQCILMSSDYF 175
Cdd:TIGR03453 248 fltlsalcaatgvlitvhpqmldVMSMSQFLLMTGDLL 285
ParA_partition NF041546
ParA family partition ATPase;
4-42 7.54e-11

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 61.03  E-value: 7.54e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755043161   4 VISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQ 42
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQ 39
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
3-196 6.55e-09

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 56.99  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLtLGlddyesLIQFYDSKQNTDLFNSLapEFSLES 82
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSAL-LG------VLPETDVGANETLYAAI--RYDDTR 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  83 VNHTPVgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNTLPVLrkFVGAFNKLTRKIADEHniDIVLVDMSPSVS 162
Cdd:PRK13869 193 RPLRDV----IRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGL--FFTRVAQAFDEVADDY--DVVVIDCPPQLG 264
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755043161 163 STNQCILMSSDYFIIPISPDFYcyqAIDSLSNVL 196
Cdd:PRK13869 265 FLTLSGLCAATSMVITVHPQML---DIASMSQFL 295
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
2-203 1.25e-38

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: 138.45  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTgLTLGLDDYEsliqfydskQNTDLFNSLAPEFSLE 81
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLT-SGLGLDPDD---------LDPTLYDLLLDDAPLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  82 SVnhtpvgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlpVLRKFVgafnkltRKIADEHniDIVLVDMSPSV 161
Cdd:COG1192   71 DA---------IVPTEIPGLDLIPANIDLAGAEIELVSRPGREL---RLKRAL-------APLADDY--DYILIDCPPSL 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755043161 162 SSTNQCILMSSDYFIIPISPDFYCYQAIDSLSNVLPKWAKEI 203
Cdd:COG1192  130 GLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDL 171
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-196 4.93e-30

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: 113.45  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161    2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTgLTLGLDDYEsliqfydskQNTDLFNSLAPEFSLE 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAT-SGLGIDKNN---------VEKTIYELLIGECNIE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   82 SVnhtpvgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlpvlrkfvgAFNKLTRKIADEHniDIVLVDMSPSV 161
Cdd:pfam13614  71 EA---------IIKTVIENLDLIPSNIDLAGAEIELIGIENREN----------ILKEALEPVKDNY--DYIIIDCPPSL 129
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 755043161  162 SSTNQCILMSSDYFIIPISPDFYcyqAIDSLSNVL 196
Cdd:pfam13614 130 GLLTINALTASDSVLIPVQCEYY---ALEGLSQLL 161
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-203 1.43e-21

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: 89.14  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLtlglddyesliqFYdskqntdlfnslapefsles 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSW------------LY-------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  83 vnhtpvgttpitgtdnpnlyilagnirfseldtqiatamtssntlpvlrkfvgafnkltrkiadehniDIVLVDMSPSVS 162
Cdd:cd02042   49 --------------------------------------------------------------------DYILIDTPPSLG 60
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755043161 163 STNQCILMSSDYFIIPISPDFYCYQAIDSLSNVLPKWAKEI 203
Cdd:cd02042   61 LLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQL 101
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-225 5.15e-18

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 82.01  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161    5 ISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLTLGLDDYESLIQfydskqntDLFNSLAPEFSLESVn 84
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQ--------ALAEGLKGRVNLDPI- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   85 htpvgtTPITGTDNPNLYILAGNIRFSELDTQIATAMTSSNTLPVLRkfvgafnkltrkiADEHNIDIVLVDMSPSVSST 164
Cdd:pfam01656  72 ------LLKEKSDEGGLDLIPGNIDLEKFEKELLGPRKEERLREALE-------------ALKEDYDYVIIDGAPGLGEL 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755043161  165 NQCILMSSDYFIIPISPDFYCYQAIDSLSNVlpkwakeIATFKvggdHPLPKANPKMLGFI 225
Cdd:pfam01656 133 LRNALIAADYVIIPLEPEVILVEDAKRLGGV-------IAALV----GGYALLGLKIIGVV 182
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
4-175 1.56e-14

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: 74.24  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161    4 VISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLtLGlddyeSLIQFyDSKQNTDLFNSLapEFSLESV 83
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSAL-FG-----YQPEF-DVGENETLYGAI--RYDDERR 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   84 NHTPVgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNtlPVLRKFvgaFNKLTRKIAD-EHNIDIVLVDMSPS-- 160
Cdd:TIGR03453 177 PISEI----IRKTYFPGLDLVPGNLELMEFEHETPRALSRGQ--GGDTIF---FARVGEALAEvEDDYDVVVIDCPPQlg 247
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 755043161  161 -----------------------VSSTNQCILMSSDYF 175
Cdd:TIGR03453 248 fltlsalcaatgvlitvhpqmldVMSMSQFLLMTGDLL 285
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
3-182 2.37e-11

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: 62.97  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADpqcnltgltLGLDDYESLIQFYDSKQNTDLFNSlapEFSLES 82
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD---------LGLANLDILLGLAPKKTLGDVLKG---RVSLED 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  83 VnhtpvgttPITGTDnpNLYILAGNIRFSELdTQIATAMtssntlpvLRKFVGAFNKLTRkiadehNIDIVLVDMSPSVS 162
Cdd:cd02038   69 I--------IVEGPE--GLDIIPGGSGMEEL-ANLDPEQ--------KAKLIEELSSLES------NYDYLLIDTGAGIS 123
                        170       180
                 ....*....|....*....|
gi 755043161 163 STNQCILMSSDYFIIPISPD 182
Cdd:cd02038  124 RNVLDFLLAADEVIVVTTPE 143
ParA_partition NF041546
ParA family partition ATPase;
4-42 7.54e-11

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 61.03  E-value: 7.54e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755043161   4 VISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQ 42
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQ 39
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
18-182 2.20e-09

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 57.21  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  18 TTVFHLGWKLATLGKRVLIIDADPQC-NLtGLTLGLDDYESLIQFydskqntdlfnsLAPEFSLESVnhtpVGTTPitgt 96
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLaNL-DVLLGLEPKATLADV------------LAGEADLEDA----IVQGP---- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  97 dnPNLYILAGNIRFSELDtqiatamtssnTLPVLRKFVGAFNKLtrkiadEHNIDIVLVDMSPSVSSTNQCILMSSDYFI 176
Cdd:COG0455   60 --GGLDVLPGGSGPAELA-----------ELDPEERLIRVLEEL------ERFYDVVLVDTGAGISDSVLLFLAAADEVV 120

                 ....*.
gi 755043161 177 IPISPD 182
Cdd:COG0455  121 VVTTPE 126
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
3-196 6.55e-09

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 56.99  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLtLGlddyesLIQFYDSKQNTDLFNSLapEFSLES 82
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSAL-LG------VLPETDVGANETLYAAI--RYDDTR 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  83 VNHTPVgttpITGTDNPNLYILAGNIRFSELDTQIATAMTSSNTLPVLrkFVGAFNKLTRKIADEHniDIVLVDMSPSVS 162
Cdd:PRK13869 193 RPLRDV----IRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGL--FFTRVAQAFDEVADDY--DVVVIDCPPQLG 264
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755043161 163 STNQCILMSSDYFIIPISPDFYcyqAIDSLSNVL 196
Cdd:PRK13869 265 FLTLSGLCAATSMVITVHPQML---DIASMSQFL 295
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
2-53 2.90e-08

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: 53.89  E-value: 2.90e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755043161    2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQcNLTGLTLGLD 53
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ-NLLRLHFGMD 51
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
3-54 3.15e-08

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: 53.97  E-value: 3.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755043161    3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDAD-PQCNLtGLTLGLDD 54
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANL-ELILGMED 52
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
1-40 1.44e-07

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 51.98  E-value: 1.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755043161   1 MAKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDAD 40
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
3-107 1.99e-07

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 51.43  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADpqCNLTGLT--LGLDDyesliqfydsKQNTDLFNSLAPEFSL 80
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--IGLRNLDliLGLEN----------RIVYTLVDVLEGECRL 68
                         90       100
                 ....*....|....*....|....*..
gi 755043161  81 ESvnhtpvgtTPITGTDNPNLYILAGN 107
Cdd:cd02036   69 EQ--------ALIKDKRWENLYLLPAS 87
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
2-40 7.93e-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: 50.03  E-value: 7.93e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 755043161    2 AKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDAD 40
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
minD CHL00175
septum-site determining protein; Validated
1-54 9.08e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 49.77  E-value: 9.08e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755043161   1 MAKVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLTLGLDD 54
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLEN 67
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
11-59 2.60e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 48.24  E-value: 2.60e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLtGLTLGLDDYESLI 59
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANL-AEALGLEVEADLI 55
PHA02518 PHA02518
ParA-like protein; Provisional
3-42 2.87e-06

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 47.54  E-value: 2.87e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQ 42
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQ 40
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
2-185 3.04e-06

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: 48.57  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   2 AKVISLFNHKGGVSKTTTVFHLGWKLATL-GKRVLIIDADPQCNLTGLTLGLDDYESLIQFYDSKQNTD--LFNSLAPEF 78
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDetLLDRALTRH 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  79 SlesvnhtpvgttpitgtdnPNLYILAGNIRFSEldtqiATAMTSSNTLPVLRKFVGAFnkltrkiadehniDIVLVDMS 158
Cdd:COG4963  182 S-------------------SGLSVLAAPADLER-----AEEVSPEAVERLLDLLRRHF-------------DYVVVDLP 224
                        170       180
                 ....*....|....*....|....*..
gi 755043161 159 PSVSSTNQCILMSSDYFIIPISPDFYC 185
Cdd:COG4963  225 RGLNPWTLAALEAADEVVLVTEPDLPS 251
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
4-213 4.55e-06

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 48.08  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   4 VISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDA-DPQCNLT---GLT--LGLDDYESLIQFYDSKQNTDLFnslape 77
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGnDPQGTASmyhGYVpdLHIHADDTLLPFYLGERDNAEY------ 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  78 fslesvnhtpvgttPITGTDNPNLYILAGNIRFSELDTQIaTAMTSSNTLPVLRKFVgaFNKLTRKIADehNIDIVLVDM 157
Cdd:PHA02519 182 --------------AIKPTCWPGLDIIPSCLALHRIETDL-MQYHDAGKLPHPPHLM--LRAAIESVWD--NYDIIVIDS 242
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755043161 158 SPSVSSTNQCILMSSDYFIIPISPDFYCYQAIDSLSNVLPKWakeIATFKVGGDHP 213
Cdd:PHA02519 243 APNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDL---LATVDLGGFEP 295
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
4-196 8.16e-06

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 47.28  E-value: 8.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   4 VISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDA-DPQCNLT---GLT--LGLDDYESLIQFYDSKQNtDLFNSLAPe 77
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASmyhGWVpdLHIHAEDTLLPFYLGEKD-DATYAIKP- 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  78 fslesvnhtpvgttpitgTDNPNLYILAGNIRFSELDTQIaTAMTSSNTLPVLrkfvgafNKLTRKIADE---HNIDIVL 154
Cdd:PRK13705 186 ------------------TCWPGLDIIPSCLALHRIETEL-MGKFDEGKLPTD-------PHLMLRLAIEtvaHDYDVIV 239
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755043161 155 VDMSPSVSSTNQCILMSSDYFIIPISPDFYCY----QAIDSLSNVL 196
Cdd:PRK13705 240 IDSAPNLGIGTINVVCAADVLIVPTPAELFDYtsalQFFDMLRDLL 285
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-160 1.84e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 45.97  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   1 MAKVIsLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLtGLTLGLDdyesliqfydskqntdlfnslapefsl 80
Cdd:COG0003    2 MTRII-FFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSL-GDVLGTE--------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  81 esVNHTPvgtTPITGtdnPNLYILagnirfsELDTQIATAMTSSNTLPVLRKFVG------------------AFNKLTR 142
Cdd:COG0003   53 --LGNEP---TEVAV---PNLYAL-------EIDPEAELEEYWERVRAPLRGLLPsagvdelaeslpgteelaALDELLE 117
                        170
                 ....*....|....*...
gi 755043161 143 kIADEHNIDIVLVDMSPS 160
Cdd:COG0003  118 -LLEEGEYDVIVVDTAPT 134
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
11-159 3.37e-05

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: 45.18  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADP-QCNLTGLtLGLDDyesliqfydskqNTDLFNSLAPEFSLESVnhtpvg 89
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRM-LGLEN------------RPGLSDVLAGEASLEDV------ 161
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755043161  90 ttpITGTDNPNLYIL-AGNIrfseldtqiatamTSSNTLPVLRKfvgAFNKLTRKIADEHniDIVLVDMSP 159
Cdd:COG0489  162 ---IQPTEVEGLDVLpAGPL-------------PPNPSELLASK---RLKQLLEELRGRY--DYVIIDTPP 211
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-51 1.25e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 43.20  E-value: 1.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755043161   11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLTLG 51
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLG 48
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
3-53 1.38e-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: 42.75  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755043161    3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQcNLTGLTLGLD 53
Cdd:pfam06564   2 KILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSPD-NLLRLHFNVP 51
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
11-53 1.78e-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: 42.68  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLtGLTLGLD 53
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNL-AETLGVE 49
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
3-45 1.84e-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: 42.72  E-value: 1.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 755043161    3 KVIsLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNL 45
Cdd:pfam02374   2 RWI-FFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSL 43
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
1-42 2.64e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.26  E-value: 2.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755043161   1 MAKVISLFNhKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQ 42
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
11-159 7.54e-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: 40.57  E-value: 7.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLtgltlglddyesliqfydskqnTDLFNSlapEFSlesvnhtpvGT 90
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSL----------------------SDAFGQ---KLG---------GE 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  91 TPITGtdNPNLYILagnirfsELDTQIATA---------MTSSNTLPVLRKFVG-------------AFNKLtRKIADEH 148
Cdd:cd02035   54 TPVKG--APNLWAM-------EIDPEEALEeyweevkelLAQYLRLPGLDEVYAeellslpgmdeaaAFDEL-REYVESG 123
                        170
                 ....*....|.
gi 755043161 149 NIDIVLVDMSP 159
Cdd:cd02035  124 EYDVIVFDTAP 134
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
7-51 1.09e-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: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 755043161    7 LFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLT---GLTLG 51
Cdd:TIGR04291   7 FFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGqvfGQTIG 54
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
3-51 1.12e-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: 40.59  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755043161   3 KVISLFNhKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLTLG 51
Cdd:cd02033   32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFG 79
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
11-40 1.74e-03

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: 39.41  E-value: 1.74e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDAD 40
Cdd:cd02037    9 KGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
11-51 1.88e-03

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: 39.66  E-value: 1.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLTGLTLG 51
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTG 48
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
3-163 2.07e-03

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: 39.18  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161   3 KVISLFNHKGGVSKTTTVFHLGWKLATLGK-RVLIIDADpqcnltgLTLG-LDDYESLIQFYDSKQNTDLFNSLAPEFSL 80
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLD-------LPFGdLGLYLNLRPDYDLADVIQNLDRLDRTLLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161  81 ESVNHTPVGttpitgtdnpnLYILAGNIRFSelDTQIATAMTSSNTLPVLRKFVGA--------FNKLTRKIADEhnIDI 152
Cdd:cd03111   74 SAVTRHSSG-----------LSLLPAPQELE--DLEALGAEQVDKLLQVLRAFYDHiivdlghfLDEVTLAVLEA--ADE 138
                        170
                 ....*....|.
gi 755043161 153 VLVDMSPSVSS 163
Cdd:cd03111  139 ILLVTQQDLPS 149
PRK10037 PRK10037
cellulose biosynthesis protein BcsQ;
1-53 4.50e-03

cellulose biosynthesis protein BcsQ;


Pssm-ID: 182204  Cd Length: 250  Bit Score: 38.32  E-value: 4.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755043161   1 MAkVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQcNLTGLTLGLD 53
Cdd:PRK10037   1 MA-ILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACPD-NLLRLSFNVD 51
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
11-46 4.70e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 38.21  E-value: 4.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755043161  11 KGGVSKTTTVFHLGWKLATLGKRVLIIDADPQCNLT 46
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCT 44
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
11-40 8.89e-03

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: 37.43  E-value: 8.89e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 755043161   11 KGGVSKTTTVFHLGWKLATLGKRVLIIDAD 40
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
3-113 9.05e-03

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: 37.03  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043161    3 KVISLFNHKGGVSKTTTVFHLGWKLATLGKRVLIIDADPQ-------CNLTGLTLGLDDYESliqfydskQNTDLFNSLA 75
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRnsvmsgtFKSQNKITGLTNFLS--------GTTDLSDAIC 89
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755043161   76 pEFSLESVNHTPVGTTPitgtdnPNLYILAGNIRFSEL 113
Cdd:TIGR01007  90 -DTNIENLDVITAGPVP------PNPTELLQSSNFKTL 120
 
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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