NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1055941243|ref|WP_067483676|]
View 

MULTISPECIES: ParA family protein [Enterococcus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-254 4.96e-138

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: 388.06  E-value: 4.96e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVLVNELPIAEATIVTEHEN 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  82 LNIVPATLQLAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQL 161
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 162 LNTVRLVQKHFNPDLEIAGVLLTMYDARTNLGTEVVEEVRKYFREKVYDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEV 241
Cdd:COG1192   161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                         250
                  ....*....|...
gi 1055941243 242 YQALAKEVVDREE 254
Cdd:COG1192   241 YRALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-254 4.96e-138

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: 388.06  E-value: 4.96e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVLVNELPIAEATIVTEHEN 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  82 LNIVPATLQLAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQL 161
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 162 LNTVRLVQKHFNPDLEIAGVLLTMYDARTNLGTEVVEEVRKYFREKVYDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEV 241
Cdd:COG1192   161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                         250
                  ....*....|...
gi 1055941243 242 YQALAKEVVDREE 254
Cdd:COG1192   241 YRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 7.55e-93

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: 270.99  E-value: 7.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVLVNELPIAEATIVTEHEN 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  82 LNIVPATLQLAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1055941243 162 LNTVRLVQKHFNPDLEI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 4-201 2.60e-51

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: 163.48  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVgvrkpdvkqdiydvlvnelpiaeativtehenln 83
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ivpatlqlagaeieltsmmaresrlkgslaevknqYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQLLN 163
Cdd:cd02042    48 -----------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLD 92

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1055941243 164 TVRLVQKHFNPDLEIAGVLLTMYDARTNLGTEVVEEVR 201
Cdd:cd02042    93 TLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-235 3.33e-36

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 129.87  E-value: 3.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   1 MAQIISVANQKGGVGKTTTTVNLGACLASL-GKKVLLVDMDAQGNATSGVG--VRKPDVKQDIYDVLvnELPIAEATIVT 77
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATQFLSktFNVPNFPQSFMKCV--EDGDLEKGIVH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  78 EHENLNIVPATLqlagAEIELTSMMARESR--------LKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAIlIPVQ 149
Cdd:NF041283   79 LTPNLDLIAGDY----DTRELGDFLADKFKseydrtfyLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYV-IVIQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 150 -CEYYALEGLSQLLNTVRLVQKHFNPD---LEIAGVLLTMYDARTNLGTEVVEEVRKYF-REKVYDTIIPRNVRLSEAPS 224
Cdd:NF041283  154 eTQQFAFEGSKKLILTYLQTLVDDFGDeinVQVAGILPVLLQARRPLQQKIVDETIEYFgKDNVFNNIIKNHARLEWYGE 233

                         250
                  ....*....|.
gi 1055941243 225 HGLPIIDYDPR 235
Cdd:NF041283  234 QGIQFEDYHDR 244
ParA_partition NF041546
ParA family partition ATPase;
4-248 1.41e-34

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 123.05  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRkpdvkqdiydvlvnelpiaeativtEHENLn 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAR-------------------------EDERP- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ivPATLQLAGAEIeltsmmAREsrlkgsLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQLLN 163
Cdd:NF041546   55 --FPVVGLARPTL------HRE------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 164 TVRLVQKhFNPDLEiAGVLLTMYDARTNLGTEVVEEVRKYfREKVYDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEVYQ 243
Cdd:NF041546  121 LIKEARE-YTPGLK-AAFVLNRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIR 197


                  ....*
gi 1055941243 244 ALAKE 248
Cdd:NF041546  198 ALAKE 202
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 4-250 6.13e-30

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: 112.52  E-value: 6.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD-AQGNATSGVGVRKPDVKqdIYDVLVNELPIAEATIVTEHeNL 82
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVT--LHDVLAGEADIKDAIYEGPF-GV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  83 NIVPATLQLAGAeieltsMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEyyalegLSQLL 162
Cdd:TIGR01969  79 KVIPAGVSLEGL------RKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE------ISSIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 163 NTVRLVQKHFNPDLEIAGVLLTMYdarTNLGTEV-VEEVRKYFREKVYdTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEV 241
Cdd:TIGR01969 147 DALKTKIVAEKLGTAILGVVLNRV---TRDKTELgREEIETILEVPVL-GVVPEDPEVRRAAAFGEPVVIYNPNSPAAQA 222


                  ....*....
gi 1055941243 242 YQALAKEVV 250
Cdd:TIGR01969 223 FMELAAELA 231
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-222 1.69e-24

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 100.52  E-value: 1.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGV-RKPDVK--QDIYDVL---VNELPIAEATIV 76
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlPETDVGanETLYAAIrydDTRRPLRDVIRP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  77 TEHENLNIVPATLQLAgaEIELTSMMA------RE----SRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILI 146
Cdd:PRK13869  202 TYFDGLHLVPGNLELM--EFEHTTPKAlsdkgtRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 147 PVQCEYYALEGLSQLLNTVRL---VQKHFNPDLEIAGV--LLTMYDARTNLGTEVVEEVRKYFREKVYDTIIPRNVRLSE 221
Cdd:PRK13869  280 TVHPQMLDIASMSQFLLMTRDllgVVKEAGGNLQYDFIryLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSD 359


                  .
gi 1055941243 222 A 222
Cdd:PRK13869  360 A 360
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-254 4.96e-138

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: 388.06  E-value: 4.96e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVLVNELPIAEATIVTEHEN 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  82 LNIVPATLQLAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQL 161
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 162 LNTVRLVQKHFNPDLEIAGVLLTMYDARTNLGTEVVEEVRKYFREKVYDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEV 241
Cdd:COG1192   161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                         250
                  ....*....|...
gi 1055941243 242 YQALAKEVVDREE 254
Cdd:COG1192   241 YRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 7.55e-93

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: 270.99  E-value: 7.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVLVNELPIAEATIVTEHEN 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  82 LNIVPATLQLAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1055941243 162 LNTVRLVQKHFNPDLEI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-229 1.31e-61

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: 193.33  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   5 ISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATS--GVGVRKPDVKQDIYDVLVNELPIAEATIV--TEHE 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSveGLEGDIAPALQALAEGLKGRVNLDPILLKekSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  81 NLNIVPATLQLAGAEIELTSMmARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQ 160
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGP-RKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055941243 161 LLNTVRLVQKHFNP-DLEIAGVLLTMYDARtNLGTEVVEEVRKYFRE-KVYDtIIPRNVRLSEAPSHGLPI 229
Cdd:pfam01656 160 LGGVIAALVGGYALlGLKIIGVVLNKVDGD-NHGKLLKEALEELLRGlPVLG-VIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 4-201 2.60e-51

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: 163.48  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVgvrkpdvkqdiydvlvnelpiaeativtehenln 83
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ivpatlqlagaeieltsmmaresrlkgslaevknqYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQLLN 163
Cdd:cd02042    48 -----------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLD 92

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1055941243 164 TVRLVQKHFNPDLEIAGVLLTMYDARTNLGTEVVEEVR 201
Cdd:cd02042    93 TLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-235 3.33e-36

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 129.87  E-value: 3.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   1 MAQIISVANQKGGVGKTTTTVNLGACLASL-GKKVLLVDMDAQGNATSGVG--VRKPDVKQDIYDVLvnELPIAEATIVT 77
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATQFLSktFNVPNFPQSFMKCV--EDGDLEKGIVH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  78 EHENLNIVPATLqlagAEIELTSMMARESR--------LKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAIlIPVQ 149
Cdd:NF041283   79 LTPNLDLIAGDY----DTRELGDFLADKFKseydrtfyLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYV-IVIQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 150 -CEYYALEGLSQLLNTVRLVQKHFNPD---LEIAGVLLTMYDARTNLGTEVVEEVRKYF-REKVYDTIIPRNVRLSEAPS 224
Cdd:NF041283  154 eTQQFAFEGSKKLILTYLQTLVDDFGDeinVQVAGILPVLLQARRPLQQKIVDETIEYFgKDNVFNNIIKNHARLEWYGE 233

                         250
                  ....*....|.
gi 1055941243 225 HGLPIIDYDPR 235
Cdd:NF041283  234 QGIQFEDYHDR 244
ParA_partition NF041546
ParA family partition ATPase;
4-248 1.41e-34

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 123.05  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRkpdvkqdiydvlvnelpiaeativtEHENLn 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAR-------------------------EDERP- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ivPATLQLAGAEIeltsmmAREsrlkgsLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQLLN 163
Cdd:NF041546   55 --FPVVGLARPTL------HRE------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 164 TVRLVQKhFNPDLEiAGVLLTMYDARTNLGTEVVEEVRKYfREKVYDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEVYQ 243
Cdd:NF041546  121 LIKEARE-YTPGLK-AAFVLNRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIR 197


                  ....*
gi 1055941243 244 ALAKE 248
Cdd:NF041546  198 ALAKE 202
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-255 9.96e-33

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: 119.22  E-value: 9.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  18 TTTVNLGACLASLGKKVLLVDMD-AQGNATSGVGVrkpDVKQDIYDVLVNELPIAEATIVTEHeNLNIVPAtlqlaGAEI 96
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADlGLANLDVLLGL---EPKATLADVLAGEADLEDAIVQGPG-GLDVLPG-----GSGP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  97 ELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEYYALEGLSQLLNtvRLVQKHfnpDL 176
Cdd:COG0455    72 AELAELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLK--LLRRRL---GV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 177 EIAGVLLTMYDART---NLGTEVVEEVRKYFREKV-YDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEVYQALAKEVVDR 252
Cdd:COG0455   147 RRAGVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226


                  ...
gi 1055941243 253 EEK 255
Cdd:COG0455   227 PVP 229
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 4-250 6.13e-30

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: 112.52  E-value: 6.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD-AQGNATSGVGVRKPDVKqdIYDVLVNELPIAEATIVTEHeNL 82
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVT--LHDVLAGEADIKDAIYEGPF-GV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  83 NIVPATLQLAGAeieltsMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEyyalegLSQLL 162
Cdd:TIGR01969  79 KVIPAGVSLEGL------RKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE------ISSIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 163 NTVRLVQKHFNPDLEIAGVLLTMYdarTNLGTEV-VEEVRKYFREKVYdTIIPRNVRLSEAPSHGLPIIDYDPRSRGAEV 241
Cdd:TIGR01969 147 DALKTKIVAEKLGTAILGVVLNRV---TRDKTELgREEIETILEVPVL-GVVPEDPEVRRAAAFGEPVVIYNPNSPAAQA 222


                  ....*....
gi 1055941243 242 YQALAKEVV 250
Cdd:TIGR01969 223 FMELAAELA 231
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 3-148 4.21e-28

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: 110.45  E-value: 4.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRkP--DVKQD--IYDVLVNE---LPIAEATI 75
Cdd:TIGR03453 105 QVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQ-PefDVGENetLYGAIRYDderRPISEIIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  76 VTEHENLNIVPATLQLAGAEIEL-TSMMARES-------RLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIP 147
Cdd:TIGR03453 184 KTYFPGLDLVPGNLELMEFEHETpRALSRGQGgdtiffaRVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLIT 263


                  .
gi 1055941243 148 V 148
Cdd:TIGR03453 264 V 264
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 4-249 2.16e-27

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: 105.36  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgVGVRKPD--------VKQDIYDVLVNELPIAEATI 75
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--------IGLRNLDlilglenrIVYTLVDVLEGECRLEQALI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  76 VT-EHENLNIVPATLqlagaeiELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEyya 154
Cdd:cd02036    74 KDkRWENLYLLPASQ-------TRDKDALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPE--- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 155 legLSQLLNTVRLVQKHFNPDLEIAGVLLTMYD-ARTNLGTEV-VEEVRKYFREKVYdTIIPRNVRLSEAPSHGLPIIDY 232
Cdd:cd02036   144 ---ISSVRDADRVIGLLESKGIVNIGLIVNRYRpEMVKSGDMLsVEDIQEILGIPLL-GVIPEDPEVIVATNRGEPLVLY 219

                         250
                  ....*....|....*..
gi 1055941243 233 DPRSRGAEVYQALAKEV 249
Cdd:cd02036   220 KPNSLAAKAFENIARRL 236
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-254 1.59e-25

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: 102.89  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLA-SLGKKVLLVDMDAQ-GNATSGVGVrkpDVKQDIYDVLVNELPIAEATI---V 76
Cdd:COG4963   102 GRVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQfGDVALYLDL---EPRRGLADALRNPDRLDETLLdraL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  77 TEHE-NLNIVPATLQLAGAEieltsmMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEyyal 155
Cdd:COG4963   179 TRHSsGLSVLAAPADLERAE------EVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPD---- 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 156 egLSQLLNTVRLVQ--KHFNPDLEIAGVLLTMYDARTNLGtevVEEVRKYFREKVyDTIIPRNVR-LSEAPSHGLPIIDY 232
Cdd:COG4963   249 --LPSLRNAKRLLDllRELGLPDDKVRLVLNRVPKRGEIS---AKDIEEALGLPV-AAVLPNDPKaVAEAANQGRPLAEV 322

                         250       260
                  ....*....|....*....|..
gi 1055941243 233 DPRSRGAEVYQALAKEVVDREE 254
Cdd:COG4963   323 APKSPLAKAIRKLAARLTGRPA 344
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-222 1.69e-24

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 100.52  E-value: 1.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGV-RKPDVK--QDIYDVL---VNELPIAEATIV 76
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlPETDVGanETLYAAIrydDTRRPLRDVIRP 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  77 TEHENLNIVPATLQLAgaEIELTSMMA------RE----SRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILI 146
Cdd:PRK13869  202 TYFDGLHLVPGNLELM--EFEHTTPKAlsdkgtRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 147 PVQCEYYALEGLSQLLNTVRL---VQKHFNPDLEIAGV--LLTMYDARTNLGTEVVEEVRKYFREKVYDTIIPRNVRLSE 221
Cdd:PRK13869  280 TVHPQMLDIASMSQFLLMTRDllgVVKEAGGNLQYDFIryLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSD 359


                  .
gi 1055941243 222 A 222
Cdd:PRK13869  360 A 360
PHA02518 PHA02518
ParA-like protein; Provisional
 4-252 2.36e-23

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 94.15  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVkqdiydvlvnelpiaeativtehenln 83
Cdd:PHA02518    2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE--------------------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ivpatlqlagaeiELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQ---CEYYALEGLSQ 160
Cdd:PHA02518   55 -------------PLIPVVRMGKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQpspFDIWAAPDLVE 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 161 LLNTVRLVqkhfNPDLEIAGVLLTMYDARTNLGTEvVEEVRKYFREKVYDTIIPRNVRLSEAPSHGLPIIDYDPRSRGAE 240
Cdd:PHA02518  122 LIKARQEV----TDGLPKFAFIISRAIKNTQLYRE-ARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAE 196

                         250
                  ....*....|..
gi 1055941243 241 VYQALAKEVVDR 252
Cdd:PHA02518  197 EIIQLVKELFRG 208
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-146 2.49e-23

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: 94.17  E-value: 2.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD-AQGNATSGVGVRkpdVKQDIYDVLVNELPIAEATIVTEhEN 81
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLA---PKKTLGDVLKGRVSLEDIIVEGP-EG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055941243  82 LNIVPATlqlAGAE--IELTSMmaRESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILI 146
Cdd:cd02038    77 LDIIPGG---SGMEelANLDPE--QKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-189 1.94e-22

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: 93.33  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgvgVRKPDV--------KQDIYDVLVNELPIAEA 73
Cdd:COG0489    92 LEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDAD----------LRGPSLhrmlglenRPGLSDVLAGEASLEDV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  74 TIVTEHENLNIVPatlqlAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLG--HLTINSfTASDAILIPVQCE 151
Cdd:COG0489   162 IQPTEVEGLDVLP-----AGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGvaDATLLA-SLVDGVLLVVRPG 235

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1055941243 152 YYALEGLSQLLNTVRLVqkhfnpDLEIAGVLLTMYDAR 189
Cdd:COG0489   236 KTALDDVRKALEMLEKA------GVPVLGVVLNMVCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-253 5.73e-21

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: 88.55  E-value: 5.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgVGVRKPD--------VKQDIYDVLVNELPIAEA 73
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD--------IGLRNLDlllglenrIVYTLVDVVEGECRLQQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  74 TIVTEH-ENLNIVPAtlqlagAEIELTSMMAREsRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCEY 152
Cdd:TIGR01968  73 LIKDKRlKNLYLLPA------SQTRDKDAVTPE-QMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 153 YALE------GL--SQLLNTVRLVQKHFNPDLEIAGVLLTMYDARTNLGTEVVeevrkyfrekvydTIIPRNVRLSEAPS 224
Cdd:TIGR01968 146 SAVRdadrviGLleAKGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLI-------------GVIPEDEAIIVSTN 212

                         250       260
                  ....*....|....*....|....*....
gi 1055941243 225 HGLPIIdYDPRSRGAEVYQALAKEVVDRE 253
Cdd:TIGR01968 213 KGEPVV-LNDKSRAGKAFENIARRILGEE 240
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-127 2.52e-20

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 87.03  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   1 MAQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgVGVRKPD--------VKQDIYDVLVNELPIAE 72
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD--------IGLRNLDlvmglenrIVYDLVDVIEGECRLKQ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1055941243  73 ATIVTEH-ENLNIVPAtlqlagAEIELTSMMAREsRLKGSLAEVKNQYDYILIDCP 127
Cdd:COG2894    73 ALIKDKRfENLYLLPA------SQTRDKDALTPE-QMKKLVEELKEEFDYILIDSP 121
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-184 1.70e-17

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: 77.61  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   2 AQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgvgVRKPDV--------KQDIYDVLVNELPIAEA 73
Cdd:cd05387    19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD----------LRRPSLhrllglpnEPGLSEVLSGQASLEDV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  74 TIVTEHENLNIVPatlqlAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSF-TASDAILIPVQCEY 152
Cdd:cd05387    89 IQSTNIPNLDVLP-----AGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILaPLVDGVLLVVRAGK 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1055941243 153 YALEGLSQLLNTVRLVQKHfnpdleIAGVLLT 184
Cdd:cd05387   164 TRRREVKEALERLEQAGAK------VLGVVLN 189
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-186 1.82e-17

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 80.79  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVD-MDAQGNATSGVGVrKPDVKQDIYDVLvneLPI--------AEAT 74
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGW-VPDLHIHAEDTL---LPFylgekddaTYAI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  75 IVTEHENLNIVPATLQLAGAEIELTSM-------MARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIP 147
Cdd:PRK13705  184 KPTCWPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVP 263

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1055941243 148 VQCEYYALEGLSQLLNTVRLVQKH-----FNPDLEIagvLLTMY 186
Cdd:PRK13705  264 TPAELFDYTSALQFFDMLRDLLKNvdlkgFEPDVRI---LLTKY 304
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-199 4.22e-16

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 76.97  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVD-MDAQGNATSGVGVrKPDVKQDIYDVLV----NELPIAEATIV-T 77
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGY-VPDLHIHADDTLLpfylGERDNAEYAIKpT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  78 EHENLNIVPATLQLAGAEIELTSMMARES-------RLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQC 150
Cdd:PHA02519  187 CWPGLDIIPSCLALHRIETDLMQYHDAGKlphpphlMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPA 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1055941243 151 EYY----ALEGLSQLLNTVRLVQ-KHFNPDLEiagVLLTMYDARTNLGTEVVEE 199
Cdd:PHA02519  267 ELFdyvsVLQFFTMLLDLLATVDlGGFEPVVR---LLLTKYSLTVGNQSRWMEE 317
minD CHL00175
septum-site determining protein; Validated
 1-146 4.71e-14

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 70.18  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   1 MAQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgVGVRKPDV-----KQDIY---DVLVNELPIAE 72
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD--------IGLRNLDLllgleNRVLYtamDVLEGECRLDQ 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055941243  73 ATIVTEH-ENLNIVPATLQLAGAEIELTSMMARESRLKgslaevKNQYDYILIDCPPSLGHLTINSF-TASDAILI 146
Cdd:CHL00175   86 ALIRDKRwKNLSLLAISKNRQRYNVTRKNMNMLVDSLK------NRGYDYILIDCPAGIDVGFINAIaPAQEAIVV 155
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-246 4.78e-14

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: 69.23  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGK-KVLLVDMD-AQGNATSGVGVRKpdvKQDIYDVL--VNEL-PIAEATIVT 77
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDlPFGDLGLYLNLRP---DYDLADVIqnLDRLdRTLLDSAVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  78 EHEN-LNIVPATLQLAGAEIeltsmmARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQceyyalE 156
Cdd:cd03111    78 RHSSgLSLLPAPQELEDLEA------LGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQ------Q 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 157 GLSQLLNTVRLVQ--KHFNPDLEIAGVLLTMYDARTNLGTEVVEEVrkyFREKVYDTIIPRNVRLSEAPSHGLPIIDYDP 234
Cdd:cd03111   146 DLPSLRNARRLLDslRELEGSSDRLRLVLNRYDKKSEISPKDIEEA---LGLEVFATLPNDYKAVSESANTGRPLVEVAP 222

                         250
                  ....*....|..
gi 1055941243 235 RSRGAEVYQALA 246
Cdd:cd03111   223 RSALVRALQDLA 234
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 4-246 1.24e-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: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRkPDVKQDIYDVLVNELPIAEATivteHENLN 83
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMD-WSVRDGWARALLNGADWAAAA----YRSPD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ---IVP-ATLQLAGAEIeltsMMARESR-LKGSLAEVK-NQYDYILIDCPPSLGHLTINSFTASDAILIPVQCE---YYA 154
Cdd:TIGR03371  78 gvlFLPyGDLSADEREA----YQAHDAGwLARLLQQLDlAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADaacYAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 155 LEGLSQLL--NTVRLVQKHFnpdleiagvLLTMYDARTNLGTEVVEEVRKYFREKVYDTIIPRNVRLSEAPSHGLPIIDY 232
Cdd:TIGR03371 154 LHQLALALfaGSGPRDGPRF---------LINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNY 224

                         250
                  ....*....|....
gi 1055941243 233 DPRSRGAEVYQALA 246
Cdd:TIGR03371 225 APHSQAAHDIRTLA 238
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-151 1.70e-12

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: 64.38  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVgVRKPDVKQDIYDVLVNELPIAEATIVTEHENL 82
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGT-FKSQNKITGLTNFLSGTTDLSDAICDTNIENL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055941243  83 NIVPatlqlAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPslghltINSFTasDAILIPVQCE 151
Cdd:TIGR01007  97 DVIT-----AGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPP------IGTVT--DAAIIARACD 152
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-252 2.96e-10

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: 58.92  E-value: 2.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGV--GVRKPDVKQDIYDVLVNELPIAEATIVTEHENLNIV--- 85
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLtgGKVPPTIDEMLTEDGTAEELRREDLLFSGFNGVDCVeag 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  86 --PATLQLAGAEIELTSMMARESRLKgslaevKNQYDYILIDCppsLGHLTINSFTA------SDAILIPVQCEYYALEG 157
Cdd:cd02117    88 gpEPGVGCGGRGIGTMLELLEEHGLL------DDDYDVVIFDV---LGDVVCGGFAAplrrgfAQKVVIVVSEELMSLYA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 158 LSqllNTVRLVQKHFNPDLEIAGVLLtmyDARTNLGTEVVEEVRKYFREKVYdTIIPRNVRLSEAPSHGLPIIDYDPRSR 237
Cdd:cd02117   159 AN---NIVKAVENYSKNGVRLAGLVA---NLRDPAGTEEIQAFAAAVGTKIL-AVIPRDPAVRRAELARVTVFEHDPVSP 231

                         250
                  ....*....|....*
gi 1055941243 238 GAEVYQALAKEVVDR 252
Cdd:cd02117   232 AASEFARLAAKIADA 246
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 4-40 1.09e-09

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 57.08  E-value: 1.09e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD 40
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-170 1.52e-09

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: 57.08  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDA-QGNATSGVGVRKPDVKQDIYDvlvneLPIaeativTEHENL 82
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATADRTGLS-----LPT------PEHLNL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  83 NIVPATLQLAGAEIELTSMMAresrlkgSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIP-------------VQ 149
Cdd:pfam09140  71 PDNDVAEVPDGENIDDARLEE-------AFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPlndsfvdfdllgqVD 143

                         170       180
                  ....*....|....*....|.
gi 1055941243 150 CEYYALEGLSQLLNTVRLVQK 170
Cdd:pfam09140 144 PETFKVKRPSFYAEMVWEARK 164
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 3-190 1.80e-09

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: 57.81  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDA-QGNATSGVGvrkPDVKQDIYDVLVNELPIAEATIVTEHEN 81
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIrKGGLHQMFG---KAPKPGLLDLLAGEASIEAGIHRDQRPG 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  82 LNIVPATlqLAGAEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTA-SDAILIPVQCEYYALEGLSQ 160
Cdd:TIGR01005 631 LAFIAAG--GASHFPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAAlADGILFVTEFERSPLGEIRD 708

                         170       180       190
                  ....*....|....*....|....*....|
gi 1055941243 161 LLNTVRLVqkhfnpDLEIAGVLLTMYDART 190
Cdd:TIGR01005 709 LIHQEPHA------NSDVLGVIFNALDMNE 732
PRK10818 PRK10818
septum site-determining protein MinD;
1-252 2.09e-09

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 56.49  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   1 MAQIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDaqgnatsgVGVRKPD--------VKQDIYDVLVNELPIAE 72
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD--------IGLRNLDlimgcerrVVYDFVNVIQGDATLNQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  73 ATIVTEH-ENLNIVPATlqlagaEIELTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIPVQCE 151
Cdd:PRK10818   73 ALIKDKRtENLYILPAS------QTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 152 YYALEGLSQLLNTV----RLVQKHFNPDLEiaGVLLTMYD-ARTNLGTEV-VEEVRKYFREKVYDtIIPRNVRLSEAPSH 225
Cdd:PRK10818  147 VSSVRDSDRILGILasksRRAENGEEPIKE--HLLLTRYNpGRVSRGDMLsMEDVLEILRIKLVG-VIPEDQSVLRASNQ 223

                         250       260
                  ....*....|....*....|....*..
gi 1055941243 226 GLPIIdYDPRSRGAEVYqalaKEVVDR 252
Cdd:PRK10818  224 GEPVI-LDIEADAGKAY----ADTVDR 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 4-146 7.36e-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: 54.43  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGnatsgvgvrkPDVKQdiydvlvnELPIAEATIVTEHEnlN 83
Cdd:cd02037     2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYG----------PSIPR--------LLGVEGKPLHQSEE--G 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 IVPATLQlagaEIELTSM--MARESR------------LKGSLAEVK-NQYDYILIDCPPSLG--HLTINSFTASDAILI 146
Cdd:cd02037    62 IVPVEVG----GIKVMSIgfLLPEDDaviwrgpmksgaIKQFLKDVDwGELDYLIIDLPPGTGdeHLSLVQLIPIDGAVV 137
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 4-246 1.02e-08

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: 54.31  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDM---------------DAQGNATSGVGVRkpDVKQDIYDVLvnel 68
Cdd:pfam06564   3 ILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLspdnllrlhfnvpfeHRQGWARAELDGA--DWRDAALEYT---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  69 piaeativtehENLNIVPATlQLAGAEIE-LTSMMARESRLKGSLAEVKNQYDYILIDCPPSLGHLTINSFTASDAILIP 147
Cdd:pfam06564  77 -----------PGLDLLPFG-RLSVEEQEnLQQLQPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 148 VQCEYYAleglsqllnTVRLVQKhfnpDLEIAGVLL-TMYDARTNLGTEVVEEVRKYFReKVYDTIIPRNVRLSEAPSHG 226
Cdd:pfam06564 145 VNPDANC---------HVLLHQQ----PLPDADHLLiNDFRPASQLQQDLLQLWRQSQR-RLLPLVIHRDEALAEALAAK 210

                         250       260
                  ....*....|....*....|
gi 1055941243 227 LPIIDYDPRSRGAEVYQALA 246
Cdd:pfam06564 211 QPLGEYRPDSLAAEEVLTLA 230
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 5.22e-08

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: 49.74  E-value: 5.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD 40
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-132 8.84e-07

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: 48.66  E-value: 8.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNAtsgvgvrkpdvkQDIYDV-LVNELPIAEA---------TIVTEHE 80
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSL------------SDAFGQkLGGETPVKGApnlwameidPEEALEE 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055941243  81 NLNIVPATLQLAGAEIELTSMMARE-SRLKG-----SLAEV-----KNQYDYILIDCPPSlGH 132
Cdd:cd02035    76 YWEEVKELLAQYLRLPGLDEVYAEElLSLPGmdeaaAFDELreyveSGEYDVIVFDTAPT-GH 137
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-43 2.91e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 47.73  E-value: 2.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQG 43
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYG 148
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
13-130 2.95e-06

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 47.84  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  13 GVGKTTTTVNLGACLASLGKKVLLVDMDA-QGNATSGVGVRKPDvkqDIYDVLVNELPIAEATIVTEHENLNIVPATlQL 91
Cdd:PRK11519  537 SIGKTFVCANLAAVISQTNKRVLLIDCDMrKGYTHELLGTNNVN---GLSDILIGQGDITTAAKPTSIANFDLIPRG-QV 612

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1055941243  92 AGAEIELtsMMAreSRLKGSLAEVKNQYDYILIDCPPSL 130
Cdd:PRK11519  613 PPNPSEL--LMS--ERFAELVNWASKNYDLVLIDTPPIL 647
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-46 5.26e-06

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 46.49  E-value: 5.26e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1055941243   1 MAQIISVANqKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNAT 46
Cdd:PRK13185    1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-53 5.73e-06

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 46.30  E-value: 5.73e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRK 53
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEK 51
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-56 9.53e-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: 45.58  E-value: 9.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGV--GVRKPDV 56
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLlgGKAIPTV 55
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 4-247 1.04e-05

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


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 45.22  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   4 IISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVL----VNELPIAEATIVTEH 79
Cdd:cd17869     5 VITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLMSDHLYTLksrkANLADKLESCVKQHE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  80 ENLNIVPATlQLAGAEIELTSmmARESRLKGSLAEVkNQYDYILIDCPPSLGHLTINSFTASDAILIPVqceyyaLEGLS 159
Cdd:cd17869    85 SGVYYFSPF-KSALDILEIKK--DDILHMITKLVEA-HAYDYIIMDLSFEFSSTVCKLLQASHNNVVIA------LQDAN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 160 QLLNTVRLVQKHFNPDLEiagvlltmydaRTNLgtevveeVRKYFREKVyDTIIPRNVRLSEAPShglpIIDYDPRSRGA 239
Cdd:cd17869   155 SSYKLNKFLRALEDLFQE-----------NFSY-------IYNKYSNNV-EDSLSTNIEKKIIGG----APRYEHALDVR 211


                  ....*...
gi 1055941243 240 EVYQALAK 247
Cdd:cd17869   212 QIIEALAK 219
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 5-245 1.05e-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: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243   5 ISVANqKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDVLVNELPIAEATIVTEHENLN- 83
Cdd:cd02034     3 IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKTIGDIRERTGAKKGEPPEGMSLNp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  84 ---IVPATLQLAGAEIELTSM----------MARESRLKGSLAE--VKNQYDYILIDCPPSLGHLTINSFTASDAILIPV 148
Cdd:cd02034    82 yvdDIIKEIIVEPDGIDLLVMgrpegggsgcYCPVNALLRELLRhlALKNYEYVVIDMEAGIEHLSRGTIRAVDLLIIVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 149 QCEYYALEGLSQLLNTVRlvqkhfnpDLEIAGVLLTMYDARtnlGTEVVEEVRKYFREKVYDTIIPRNVRLSEAPSHGLP 228
Cdd:cd02034   162 EPSKRSIQTAKRIKELAE--------ELGIKKIYLIVNKVR---NEEEQELIEELLIKLKLIGVIPYDEEIMEADLKGKP 230

                         250
                  ....*....|....*....
gi 1055941243 229 IIDYDPRSRGA--EVYQAL 245
Cdd:cd02034   231 LFDLDSAAVKAieKIVEKL 249
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-47 1.72e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 45.13  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATS 47
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTR 44
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-44 2.07e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 44.39  E-value: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGN 44
Cdd:COG3640     8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 11-46 2.51e-05

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 44.60  E-value: 2.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNAT 46
Cdd:cd02032     8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-132 2.40e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 42.00  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATSGVGVRKPDVKQDIYDV----LVNELPIAEA-----TIVTEHEn 81
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVpglfALEIDPQAAAqayraRIVDPVR- 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055941243  82 lNIVPATL------QLAGA---EI----ELTSMMARESRLkgslaevkNQYDYILIDCPPSlGH 132
Cdd:TIGR04291  90 -GVLPDDVvssieeQLSGActtEIaafdEFTGLLTDAELT--------QDFDHIIFDTAPT-GH 143
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-132 2.91e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.34  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNaTSGV-GVrkpDVKQDIYDVLVNELPIAE---ATIVTEH------- 79
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHS-LGDVlGT---ELGNEPTEVAVPNLYALEidpEAELEEYwervrap 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1055941243  80 -----ENLNIVPATLQLAGAEiELTSMMaresRLKGSLAEvkNQYDYILIDCPPSlGH 132
Cdd:COG0003    87 lrgllPSAGVDELAESLPGTE-ELAALD----ELLELLEE--GEYDVIVVDTAPT-GH 136
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 11-213 3.62e-04

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 41.18  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATsgvgvrkpdvkqDIYDVLVNELPiaeaTIVTehENLNIVPATLQ 90
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLS------------DSFNQKFGHEP----TKVK--ENLSAMEIDPN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  91 -------LAGAEIELTSMMAREsrLKGSLAE---------------------VKNQYDYILIDCPPSlGH-LTINSFtas 141
Cdd:pfam02374  71 meleeywQEVQKYMNALLGLRM--LEGILAEelaslpgideaasfdefkkymDEGEYDVVVFDTAPT-GHtLRLLSL--- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055941243 142 dailiPVQCEYYaLEGLSQLLNTVRLVQKHFNP--DLEIAGVLLTMYDARtnlgtEVVEEVRKYFREKVYDTII 213
Cdd:pfam02374 145 -----PTVLGWY-LEKIVKLKNQIGPLAKPFLGmgGVSIPEALESLEETK-----ERIERAREILTDPERTSFR 207
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 3-47 4.71e-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: 40.97  E-value: 4.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1055941243   3 QIISVANqKGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNATS 47
Cdd:cd02033    32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTS 75
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 11-254 9.07e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 39.78  E-value: 9.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASlGKKVLLVDMDAQGNAT-SGVGVRKPDVKQDIYDvlvNELPIAEATIVTEHENLNIVPATL 89
Cdd:PRK13231   10 KGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTrTLCGKRIPTVLDTLKD---NRKPELEDIIHEGFNGILCVESGG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243  90 QLAGAEIELTSMMARESRLKgSLAEVKNQYDYILIDCppsLGHLTINSFTA------SDAILIPVQCEYYALEGLSQLLN 163
Cdd:PRK13231   86 PEPGVGCAGRGVIVAMNLLE-NLGVFDEDIDVVIYDV---LGDVVCGGFSVplredyADEVYIVTSGEYMSLYAANNIAR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055941243 164 TVRLVQKhfnpdlEIAGVLLTMYDARTNLgtEVVEEVRKYFREKVYDtIIPRNVRLSEAPSHGLPIIDYDPRSRGAEVYQ 243
Cdd:PRK13231  162 GIKKLKG------KLGGIICNCRGIDNEV--EIVSEFASRIGSRIIG-VIPRSNLVQESELDAKTVVETFPESEQASVYR 232

                         250
                  ....*....|.
gi 1055941243 244 ALAKEVVDREE 254
Cdd:PRK13231  233 KLANNIMNNTE 243
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-40 1.43e-03

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: 38.91  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1055941243   4 IISVANQKGGVGKTTTTvnlgACLASLGKKVLLVDMD 40
Cdd:cd03110     1 IIAVLSGKGGTGKTTIT----ANLAVLLYNVILVDCD 33
chlL CHL00072
photochlorophyllide reductase subunit L
 11-46 3.11e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.18  E-value: 3.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMDAQGNAT 46
Cdd:CHL00072    8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDST 43
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
3-40 6.49e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 37.13  E-value: 6.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD 40
Cdd:PRK13849    2 KLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEAD 39
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-40 8.12e-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: 37.37  E-value: 8.12e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1055941243  11 KGGVGKTTTTVNLGACLASLGKKVLLVDMD 40
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 3-40 9.39e-03

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 36.39  E-value: 9.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1055941243   3 QIISVANQKGGVGKTTTTVNLGACLASLGKKVLLVDMD 40
Cdd:pfam07015   2 QLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEAD 39
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH