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Conserved domains on  [gi|1124574266|ref|WP_074856684|]
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ParA family protein [Ectopseudomonas oleovorans]

Protein Classification

ParA family protein( domain architecture ID 11439703)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-252 2.75e-129

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: 366.11  E-value: 2.75e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YQLLPANRDLTAAEVALLEMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDL 161
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 162 VNSIQRIAQLLNPKLQIEGLLRTMYDPRISLTNDVTAQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIA 241
Cdd:COG1192   161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                         250
                  ....*....|.
gi 1124574266 242 YLALAGELVRR 252
Cdd:COG1192   241 YRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-252 2.75e-129

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: 366.11  E-value: 2.75e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YQLLPANRDLTAAEVALLEMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDL 161
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 162 VNSIQRIAQLLNPKLQIEGLLRTMYDPRISLTNDVTAQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIA 241
Cdd:COG1192   161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                         250
                  ....*....|.
gi 1124574266 242 YLALAGELVRR 252
Cdd:COG1192   241 YRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 4.58e-83

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: 246.34  E-value: 4.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YQLLPANRDLTAAEVALLEMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1124574266 162 VNSIQRIAQLLNPKLQI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 2.63e-48

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: 156.16  E-value: 2.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSgidkhalehsiydvligecdlgqamqfsehggy 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  83 qllpanrdltaaevallemkmkesrlryalapirenYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDLV 162
Cdd:cd02042    48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1124574266 163 NSIQRIAQLLNPKLQIEGLLRTMYDPRISLTNDVTAQLK 201
Cdd:cd02042    92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
4-241 1.74e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 112.65  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATmgsgidkhalehsiydvligecdlgqamQFSEHGGYQ 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL----------------------------DWAAAREDE 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  84 LLPANRDLTAAevallemkmkesRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDLVN 163
Cdd:NF041546   53 RPFPVVGLARP------------TLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124574266 164 SIQRiAQLLNPKLQIEGLL-RTmyDPRISLTNDVTAQLKEhFGDKLYDAVIPRNVRLAEAPSFGMpaLVYDKQSRGAIA 241
Cdd:NF041546  121 LIKE-AREYTPGLKAAFVLnRA--IARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGL--TVFEAEPDGKAA 193
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-219 2.71e-25

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 101.37  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   1 MAKVFAIANQKGGVGKTTTCINLA--ASLVATKRrVLLIDLDPQGNAT--MGSGIDKHALEHSIYDVLIGEcDLgqamqf 76
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAvvASSVFNKK-VLVIDTDLQGNATqfLSKTFNVPNFPQSFMKCVEDG-DL------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  77 sEHGGYQLLPaNRDLTAAEVALLEM------KMKESRLRY-----ALAPIRENYDYILIDCPPSLNMLTINALVAADGVI 145
Cdd:NF041283   73 -EKGIVHLTP-NLDLIAGDYDTRELgdfladKFKSEYDRTfylkkLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124574266 146 IPMQCEYYALEGLSDLVNS-IQRIAQLLNPK--LQIEGLLRTMYDPRISLTNDVTAQLKEHFG-DKLYDAVIPRNVRL 219
Cdd:NF041283  151 VIQETQQFAFEGSKKLILTyLQTLVDDFGDEinVQVAGILPVLLQARRPLQQKIVDETIEYFGkDNVFNNIIKNHARL 228
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-250 4.88e-24

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: 97.11  E-value: 4.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD-PQGNATMGSGIDKhaLEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMED--KPVTLHDVLAGEADIKDAIYEGPFGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YqLLPANRDLTAAevalleMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEyyalegLSDL 161
Cdd:TIGR01969  79 K-VIPAGVSLEGL------RKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE------ISSI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 162 VNSIQRIAQLLNPKLQIEGLLRTMYDpriSLTNDVTAQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIA 241
Cdd:TIGR01969 146 TDALKTKIVAEKLGTAILGVVLNRVT---RDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQA 222


                  ....*....
gi 1124574266 242 YLALAGELV 250
Cdd:TIGR01969 223 FMELAAELA 231
PHA02518 PHA02518
ParA-like protein; Provisional
 3-252 1.65e-20

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 86.44  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATmgsgidkhalehsiydvligecdlgQAMQFSEHGGy 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST-------------------------DWAEAREEGE- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  83 QLLPAnrdltaaevalleMKMKESrLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDLV 162
Cdd:PHA02518   55 PLIPV-------------VRMGKS-IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 163 NSIQRiAQLLNPKLQIEGLLRTMYDPRISLTNDVTaQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIAY 242
Cdd:PHA02518  121 ELIKA-RQEVTDGLPKFAFIISRAIKNTQLYREAR-KALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198

                         250
                  ....*....|
gi 1124574266 243 LALAGELVRR 252
Cdd:PHA02518  199 IQLVKELFRG 208
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-252 2.75e-129

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: 366.11  E-value: 2.75e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YQLLPANRDLTAAEVALLEMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDL 161
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 162 VNSIQRIAQLLNPKLQIEGLLRTMYDPRISLTNDVTAQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIA 241
Cdd:COG1192   161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                         250
                  ....*....|.
gi 1124574266 242 YLALAGELVRR 252
Cdd:COG1192   241 YRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 4.58e-83

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: 246.34  E-value: 4.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YQLLPANRDLTAAEVALLEMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 1124574266 162 VNSIQRIAQLLNPKLQI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-228 4.06e-62

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: 194.87  E-value: 4.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   5 FAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATM--GSGIDKHALEHSIYDVLIGECDLGQAMQF--SEHG 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSveGLEGDIAPALQALAEGLKGRVNLDPILLKekSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  81 GYQLLPANRDLTAAEVALLEMKmKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSD 160
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPR-KEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124574266 161 LVNSIQRIAQLLNP-KLQIEGLLRTMYDPRISLTNDVTAQLKEHFGDKLYDaVIPRNVRLAEAPSFGMP 228
Cdd:pfam01656 160 LGGVIAALVGGYALlGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLG-VIPRDEAVAEAPARGLP 227
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 2.63e-48

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: 156.16  E-value: 2.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSgidkhalehsiydvligecdlgqamqfsehggy 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  83 qllpanrdltaaevallemkmkesrlryalapirenYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDLV 162
Cdd:cd02042    48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1124574266 163 NSIQRIAQLLNPKLQIEGLLRTMYDPRISLTNDVTAQLK 201
Cdd:cd02042    92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
4-241 1.74e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 112.65  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATmgsgidkhalehsiydvligecdlgqamQFSEHGGYQ 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL----------------------------DWAAAREDE 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  84 LLPANRDLTAAevallemkmkesRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDLVN 163
Cdd:NF041546   53 RPFPVVGLARP------------TLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124574266 164 SIQRiAQLLNPKLQIEGLL-RTmyDPRISLTNDVTAQLKEhFGDKLYDAVIPRNVRLAEAPSFGMpaLVYDKQSRGAIA 241
Cdd:NF041546  121 LIKE-AREYTPGLKAAFVLnRA--IARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGL--TVFEAEPDGKAA 193
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-256 1.99e-25

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: 99.96  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  18 TTCINLAASLVATKRRVLLIDLDPqGNATMGSGIDKHAlEHSIYDVLIGECDLGQAMQFSEhGGYQLLPANRDLTAAEvA 97
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADL-GLANLDVLLGLEP-KATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELA-E 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  98 LLEmkmkESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSdlvnsiqRIAQLLNPKLQ 177
Cdd:COG0455    77 LDP----EERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAY-------ALLKLLRRRLG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 178 IE--GLLRTMYDPR---ISLTNDVTAQLKEHFGDKL-YDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIAYLALAGELVR 251
Cdd:COG0455   146 VRraGVVVNRVRSEaeaRDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAG 225


                  ....*
gi 1124574266 252 RQRAA 256
Cdd:COG0455   226 WPVPE 230
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-219 2.71e-25

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 101.37  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   1 MAKVFAIANQKGGVGKTTTCINLA--ASLVATKRrVLLIDLDPQGNAT--MGSGIDKHALEHSIYDVLIGEcDLgqamqf 76
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAvvASSVFNKK-VLVIDTDLQGNATqfLSKTFNVPNFPQSFMKCVEDG-DL------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  77 sEHGGYQLLPaNRDLTAAEVALLEM------KMKESRLRY-----ALAPIRENYDYILIDCPPSLNMLTINALVAADGVI 145
Cdd:NF041283   73 -EKGIVHLTP-NLDLIAGDYDTRELgdfladKFKSEYDRTfylkkLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124574266 146 IPMQCEYYALEGLSDLVNS-IQRIAQLLNPK--LQIEGLLRTMYDPRISLTNDVTAQLKEHFG-DKLYDAVIPRNVRL 219
Cdd:NF041283  151 VIQETQQFAFEGSKKLILTyLQTLVDDFGDEinVQVAGILPVLLQARRPLQQKIVDETIEYFGkDNVFNNIIKNHARL 228
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-250 4.88e-24

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: 97.11  E-value: 4.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD-PQGNATMGSGIDKhaLEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMED--KPVTLHDVLAGEADIKDAIYEGPFGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YqLLPANRDLTAAevalleMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEyyalegLSDL 161
Cdd:TIGR01969  79 K-VIPAGVSLEGL------RKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE------ISSI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 162 VNSIQRIAQLLNPKLQIEGLLRTMYDpriSLTNDVTAQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIA 241
Cdd:TIGR01969 146 TDALKTKIVAEKLGTAILGVVLNRVT---RDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQA 222


                  ....*....
gi 1124574266 242 YLALAGELV 250
Cdd:TIGR01969 223 FMELAAELA 231
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-249 5.50e-24

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: 96.50  E-value: 5.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDpqgnATMgSGIDKH-ALEHSI----YDVLIGECDLGQAM--- 74
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD----IGL-RNLDLIlGLENRIvytlVDVLEGECRLEQALikd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  75 QFSEhgGYQLLPANRDLTaaevallEMKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYA 154
Cdd:cd02036    76 KRWE--NLYLLPASQTRD-------KDALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 155 LEGlSDlvnsiqRIAQLLNPK-LQIEGLLRTMYDP-RISLTNDVTAQ-LKEHFGDKLYdAVIPRNVRLAEAPSFGMPALV 231
Cdd:cd02036   147 VRD-AD------RVIGLLESKgIVNIGLIVNRYRPeMVKSGDMLSVEdIQEILGIPLL-GVIPEDPEVIVATNRGEPLVL 218

                         250
                  ....*....|....*...
gi 1124574266 232 YDKQSRGAIAYLALAGEL 249
Cdd:cd02036   219 YKPNSLAAKAFENIARRL 236
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-196 1.44e-22

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: 95.43  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSG----IDKHALEhSIYDVLIGE---CDLGQAMQF 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGyqpeFDVGENE-TLYGAIRYDderRPISEIIRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  77 SEHGGYQLLPANRDLTAAE----VALLE----MKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPM 148
Cdd:TIGR03453 185 TYFPGLDLVPGNLELMEFEhetpRALSRgqggDTIFFARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLITV 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124574266 149 Q---------CEYyaLEGLSDLVNSIQRIAQLLN----------------PKLQIEGLLRTMYDPRIsLTNDV 196
Cdd:TIGR03453 265 HpqmldvmsmSQF--LLMTGDLLGVVREAGGNLSydfmrylvtryepndgPQAQMVAFLRSLFGDHV-LTNPM 334
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-262 4.53e-22

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: 93.64  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASL-VATKRRVLLIDLDPQ-GNATMGSGIDKhalEHSIYDVL--IGECD---LGQAM 74
Cdd:COG4963   102 GRVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQfGDVALYLDLEP---RRGLADALrnPDRLDetlLDRAL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  75 QfSEHGGYQLLPANRDLTAAE-------VALLEMkmkesrlryalapIRENYDYILIDCPPSLNMLTINALVAADGVIIP 147
Cdd:COG4963   179 T-RHSSGLSVLAAPADLERAEevspeavERLLDL-------------LRRHFDYVVVDLPRGLNPWTLAALEAADEVVLV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 148 MQCEyyaLEGLSDLVNSIQRIAQLLNPKLQIEgLLRTMYDPRISLTndvTAQLKEHFGDKLyDAVIPRNVR-LAEAPSFG 226
Cdd:COG4963   245 TEPD---LPSLRNAKRLLDLLRELGLPDDKVR-LVLNRVPKRGEIS---AKDIEEALGLPV-AAVLPNDPKaVAEAANQG 316

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1124574266 227 MPALVYDKQSRGAIAYLALAGELVRRQRAAAKTATA 262
Cdd:COG4963   317 RPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKAGG 352
PHA02518 PHA02518
ParA-like protein; Provisional
 3-252 1.65e-20

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 86.44  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATmgsgidkhalehsiydvligecdlgQAMQFSEHGGy 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST-------------------------DWAEAREEGE- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  83 QLLPAnrdltaaevalleMKMKESrLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYALEGLSDLV 162
Cdd:PHA02518   55 PLIPV-------------VRMGKS-IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 163 NSIQRiAQLLNPKLQIEGLLRTMYDPRISLTNDVTaQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIAY 242
Cdd:PHA02518  121 ELIKA-RQEVTDGLPKFAFIISRAIKNTQLYREAR-KALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198

                         250
                  ....*....|
gi 1124574266 243 LALAGELVRR 252
Cdd:PHA02518  199 IQLVKELFRG 208
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-246 1.04e-18

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: 82.77  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDpQG--NATMGSGIDKHALeHSIYDVLIGECDLGQAMQFSEH 79
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-IGlrNLDLLLGLENRIV-YTLVDVVEGECRLQQALIKDKR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  80 -GGYQLLPA--NRDLTaaevALLEMKMKEsrlryALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYAle 156
Cdd:TIGR01968  79 lKNLYLLPAsqTRDKD----AVTPEQMKK-----LVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSA-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 157 glsdlVNSIQRIAQLLNPKlQIE--GLLRTMYDPRISLTNDV--TAQLKEHFGDKLYdAVIPRNVRLAEAPSFGMPaLVY 232
Cdd:TIGR01968 148 -----VRDADRVIGLLEAK-GIEkiHLIVNRLRPEMVKKGDMlsVDDVLEILSIPLI-GVIPEDEAIIVSTNKGEP-VVL 219

                         250
                  ....*....|....
gi 1124574266 233 DKQSRGAIAYLALA 246
Cdd:TIGR01968 220 NDKSRAGKAFENIA 233
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 4-146 1.70e-18

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: 82.54  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGnATMGS--GIDKhalEHSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRG-PSLHRmlGLEN---RPGLSDVLAGEASLEDVIQPTEVEG 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124574266  82 YQLLPANRdLTAAEVALLEMKmkesRLRYALAPIRENYDYILIDCPPSLnmLTINALVAA---DGVII 146
Cdd:COG0489   170 LDVLPAGP-LPPNPSELLASK----RLKQLLEELRGRYDYVIIDTPPGL--GVADATLLAslvDGVLL 230
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-206 6.25e-18

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 82.42  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGI----DKHALEhSIYDVLIGECD---LGQAMQ 75
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlpetDVGANE-TLYAAIRYDDTrrpLRDVIR 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  76 FSEHGGYQLLPANRDLTAAE----VALLEMKMKE----SRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIP 147
Cdd:PRK13869  201 PTYFDGLHLVPGNLELMEFEhttpKALSDKGTRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVIT 280

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124574266 148 MQCEYYALEGLS-------DLVNSIQRIAQllNPKLQIEGLLRTMYDPRISLTNDVTAQLKEHFGD 206
Cdd:PRK13869  281 VHPQMLDIASMSqfllmtrDLLGVVKEAGG--NLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFED 344
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-146 7.57e-17

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 77.40  E-value: 7.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   1 MAKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLID-------LDpqgnATMGsgidkhaLEHSI-YD---VLIGECD 69
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDadiglrnLD----LVMG-------LENRIvYDlvdVIEGECR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  70 LGQAM----QFSehgGYQLLPA--NRDLTaaevALLEMKMKEsrlryALAPIRENYDYILIDCPPSLNMLTINALVAADG 143
Cdd:COG2894    70 LKQALikdkRFE---NLYLLPAsqTRDKD----ALTPEQMKK-----LVEELKEEFDYILIDSPAGIEQGFKNAIAGADE 137


                  ...
gi 1124574266 144 VII 146
Cdd:COG2894   138 AIV 140
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-146 1.58e-16

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: 76.07  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDpqgnatMGSGiDKHAL-----EHSIYDVLIGECDLGQAMQFS 77
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD------LGLA-NLDILlglapKKTLGDVLKGRVSLEDIIVEG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124574266  78 EhGGYQLLPANRDLtaAEVALLEmKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVII 146
Cdd:cd02038    74 P-EGLDIIPGGSGM--EELANLD-PEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-146 6.47e-16

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


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 73.76  E-value: 6.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD---PQGNATMGSGiDKHALEhsiyDVLIGECDLGQAMQFSE 78
Cdd:cd05387    19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlrrPSLHRLLGLP-NEPGLS----EVLSGQASLEDVIQSTN 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124574266  79 HGGYQLLPANRDL-TAAEvaLLEmkmkESRLRYALAPIRENYDYILIDCPPSLNmLTINALVA--ADGVII 146
Cdd:cd05387    94 IPNLDVLPAGTVPpNPSE--LLS----SPRFAELLEELKEQYDYVIIDTPPVLA-VADALILAplVDGVLL 157
minD CHL00175
septum-site determining protein; Validated
 1-253 2.36e-15

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 73.65  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   1 MAKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD-PQGNATMGSGIDKHALeHSIYDVLIGECDLGQAM-QFSE 78
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRVL-YTAMDVLEGECRLDQALiRDKR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  79 HGGYQLLPANRDLTAAEVALLEMKMKESRLRyalapiRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYAlegl 158
Cdd:CHL00175   93 WKNLSLLAISKNRQRYNVTRKNMNMLVDSLK------NRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITA---- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 159 sdlVNSIQRIAQLL--NPKLQIEgLLRTMYDPRISLTNDV--TAQLKEHFGDKLYdAVIPRNVRLAEAPSFGMPALVYDK 234
Cdd:CHL00175  163 ---IRDADRVAGLLeaNGIYNVK-LLVNRVRPDMIQANDMmsVRDVQEMLGIPLL-GAIPEDENVIISTNRGEPLVLNKK 237

                         250
                  ....*....|....*....
gi 1124574266 235 QSRGAIAYLALAGELVRRQ 253
Cdd:CHL00175  238 LTLSGIAFENAARRLVGKQ 256
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-221 2.93e-15

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 74.66  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLID-LDPQGNATMGSGI--DKHALE-HSIYDVLIGECDLGQ-AMQFSE 78
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYvpDLHIHAdDTLLPFYLGERDNAEyAIKPTC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  79 HGGYQLLPANRDLTAAEVALLEMKMKES-------RLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCE 151
Cdd:PHA02519  188 WPGLDIIPSCLALHRIETDLMQYHDAGKlphpphlMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 152 YYaleglsDLVNSIQRIAQLLNpklqiegLLRTM----YDP-------RISLTNDVTAQ-LKEHFGDKLYDAVIPRNVRL 219
Cdd:PHA02519  268 LF------DYVSVLQFFTMLLD-------LLATVdlggFEPvvrllltKYSLTVGNQSRwMEEQIRNTWGSMVLRQVVRV 334


                  ..
gi 1124574266 220 AE 221
Cdd:PHA02519  335 TD 336
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-167 6.11e-15

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: 71.93  E-value: 6.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVA-TKRRVLLIDLD-PQGNATMGSGIDKHaleHSIYDVL-----IGECDLGQAMq 75
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDlPFGDLGLYLNLRPD---YDLADVIqnldrLDRTLLDSAV- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  76 FSEHGGYQLLPANRDLTAAEvallemKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYYAL 155
Cdd:cd03111    77 TRHSSGLSLLPAPQELEDLE------ALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSL 150

                         170
                  ....*....|..
gi 1124574266 156 EGLSDLVNSIQR 167
Cdd:cd03111   151 RNARRLLDSLRE 162
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-166 1.10e-14

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 72.70  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLID-LDPQGNATMGSG----IDKHAlEHSIYDVLIGEC-DLGQAMQFS 77
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGwvpdLHIHA-EDTLLPFYLGEKdDATYAIKPT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  78 EHGGYQLLPANRDLTAAEVALL----EMKMKES---RLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQC 150
Cdd:PRK13705  187 CWPGLDIIPSCLALHRIETELMgkfdEGKLPTDphlMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPA 266

                         170
                  ....*....|....*.
gi 1124574266 151 EYYaleglsDLVNSIQ 166
Cdd:PRK13705  267 ELF------DYTSALQ 276
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 2-250 4.25e-14

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: 69.68  E-value: 4.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   2 AKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQG--------NATMGSGIDKHALEhsiydvliGECDLGQA 73
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNllrlhfgmDWSVRDGWARALLN--------GADWAAAA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  74 MQFSEhgGYQLLPANrDLTAAEvALLEMKMKESRLRYALAPI-RENYDYILIDCPPSLNMLTINALVAADGVIIPMQCE- 151
Cdd:TIGR03371  73 YRSPD--GVLFLPYG-DLSADE-REAYQAHDAGWLARLLQQLdLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADa 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 152 --YYALEGLSD--LVNSIQRIAqllnpklqiEGLLRTMYDPRISLTNDVTAQLKEHFGDKLYDAVIPRNVRLAEAPSFGM 227
Cdd:TIGR03371 149 acYATLHQLALalFAGSGPRDG---------PRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGT 219

                         250       260
                  ....*....|....*....|...
gi 1124574266 228 PALVYDKQSRGAIAYLALAGELV 250
Cdd:TIGR03371 220 PVLNYAPHSQAAHDIRTLAGWLL 242
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-146 9.17e-11

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: 59.76  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQgNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEHGGY 82
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMR-NSVMSGTFKSQNKITGLTNFLSGTTDLSDAICDTNIENL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124574266  83 QLLPANRdLTAAEVALLEmkmkESRLRYALAPIRENYDYILIDCPPsLNMLTINALVA--ADGVII 146
Cdd:TIGR01007  97 DVITAGP-VPPNPTELLQ----SSNFKTLIETLRKRFDYIIIDTPP-IGTVTDAAIIAraCDASIL 156
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-148 5.13e-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: 55.54  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQgNATMGSGIDKHAlehsiydvligecdlgqamQFSEHGGYQ 83
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFHRYFENRS-------------------ATADRTGLS 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124574266  84 L-LPANRDLTAAEVALLE--MKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPM 148
Cdd:pfam09140  62 LpTPEHLNLPDNDVAEVPdgENIDDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
PRK09841 PRK09841
tyrosine-protein kinase;
15-170 1.35e-08

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 55.30  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  15 GKTTTCINLAASLVATKRRVLLIDLDpqgnatMGSGIdKHAL-----EHSIYDVLIGECDLGQAMQFSEHGGYQLlpanr 89
Cdd:PRK09841  544 GKTFVSSTLAAVIAQSDQKVLFIDAD------LRRGY-SHNLftvsnEHGLSEYLAGKDELNKVIQHFGKGGFDV----- 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  90 dLTAAEVAL--LEMKMKEsRLRYALAPIRENYDYILIDCPPSLNMltINALVAADGVIIPMQCEYYALEGLSDLVNSIQR 167
Cdd:PRK09841  612 -ITRGQVPPnpSELLMRD-RMRQLLEWANDHYDLVIVDTPPMLAV--SDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQR 687


                  ...
gi 1124574266 168 IAQ 170
Cdd:PRK09841  688 LEQ 690
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 3-168 2.07e-08

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: 54.73  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD-PQGNATMGSGIDKHAlehSIYDVLIGECDLGQAMQFSEHGG 81
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFGKAPKP---GLLDLLAGEASIEAGIHRDQRPG 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  82 YQLLPanrdltAAEVALLEMKMKESRLRYALAPIREN----YDYILIDCPPSLNMLTINALVA-ADGVIIPMQCEYYALE 156
Cdd:TIGR01005 631 LAFIA------AGGASHFPHNPNELLANPAMAELIDNarnaFDLVLVDLAALAAVADAAAFAAlADGILFVTEFERSPLG 704

                         170
                  ....*....|..
gi 1124574266 157 GLSDLVNSIQRI 168
Cdd:TIGR01005 705 EIRDLIHQEPHA 716
GPN cd17868
GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small ...
 13-127 2.73e-08

GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small GTPases, Gpn1, 2, and 3. They form heterodimers, interact with RNA polymerase II and may function in nuclear import of RNA polymerase II.


Pssm-ID: 349777 [Multi-domain]  Cd Length: 198  Bit Score: 52.70  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  13 GVGKTTTCINLAASLVATKRRVLLIDLDPqGNATMGSGIDKHALEHSIYDVLIGECDLGQAMqfsehggyqllpanrdlt 92
Cdd:cd17868    10 GSGKTTFCKNMKEHLRARKRNPYVINLDP-GNINEPLDYDIDIRDLIKYDDIMEELDLGPNG------------------ 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1124574266  93 AAEVALLEMKMKESRLRYALAPIRENYDYILIDCP 127
Cdd:cd17868    71 SIVYSLEYFEKNFDWFEKKLENEDKNPHYILFDCP 105
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
4-170 9.01e-08

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 52.85  E-value: 9.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDpqgnatMGSGIDKHAL----EHSIYDVLIGECDLGQAMQFSEH 79
Cdd:PRK11519  528 VLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCD------MRKGYTHELLgtnnVNGLSDILIGQGDITTAAKPTSI 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  80 GGYQLLPanRDLTAAEVALLEMkmkESRLRYALAPIRENYDYILIDCPPSLNMltINALVAADGVIIPMQCEYYALEGLS 159
Cdd:PRK11519  602 ANFDLIP--RGQVPPNPSELLM---SERFAELVNWASKNYDLVLIDTPPILAV--TDAAIVGRHVGTTLMVARYAVNTLK 674

                         170
                  ....*....|.
gi 1124574266 160 DLVNSIQRIAQ 170
Cdd:PRK11519  675 EVETSLSRFEQ 685
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 3-246 2.05e-07

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: 50.45  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATMGSGIDKHALEHSIYDVLIGECDLGQAMQFSEhgGY 82
Cdd:pfam06564   2 KILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSPDNLLRLHFNVPFEHRQGWARAELDGADWRDAALEYTP--GL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  83 QLLPANRdLTAAEVALLE-MKMKESRLRYALAPIRENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEyyaleglsdl 161
Cdd:pfam06564  80 DLLPFGR-LSVEEQENLQqLQPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 162 VNSIQRIAQLLNPKLQIegLLRTMYDPRISLTNDVTaQLKEHFGDKLYDAVIPRNVRLAEAPSFGMPALVYDKQSRGAIA 241
Cdd:pfam06564 149 ANCHVLLHQQPLPDADH--LLINDFRPASQLQQDLL-QLWRQSQRRLLPLVIHRDEALAEALAAKQPLGEYRPDSLAAEE 225


                  ....*
gi 1124574266 242 YLALA 246
Cdd:pfam06564 226 VLTLA 230
PRK10818 PRK10818
septum site-determining protein MinD;
1-254 1.00e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 48.78  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266   1 MAKVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD-PQGNATMGSGIDKHALeHSIYDVLIGECDLGQAM-QFSE 78
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRVV-YDFVNVIQGDATLNQALiKDKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  79 HGGYQLLPAN--RD---LTAAEVALLEMKMKEsrlryalapirENYDYILIDCPPSLNMLTINALVAADGVIIPMQCEYY 153
Cdd:PRK10818   80 TENLYILPASqtRDkdaLTREGVAKVLDDLKA-----------MDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266 154 ALEG----LSDLVNSIQRIAQLLNPKLqiEGLLRTMYDP-RISLTNDVTAQ-LKEHFGDKLYdAVIPRNVRLAEAPSFGM 227
Cdd:PRK10818  149 SVRDsdriLGILASKSRRAENGEEPIK--EHLLLTRYNPgRVSRGDMLSMEdVLEILRIKLV-GVIPEDQSVLRASNQGE 225

                         250       260
                  ....*....|....*....|....*..
gi 1124574266 228 PaLVYDKQSRGAIAYLALAGELVRRQR 254
Cdd:PRK10818  226 P-VILDIEADAGKAYADTVDRLLGEER 251
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-46 2.22e-06

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 47.65  E-value: 2.22e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1124574266   1 MAKVFAIANqKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT 46
Cdd:PRK13185    1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-51 2.72e-06

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 47.36  E-value: 2.72e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT---MGSGI 51
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTlllTGGKV 51
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 3.54e-06

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 44.73  E-value: 3.54e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD 40
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 5.55e-06

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: 45.96  E-value: 5.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD 40
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-44 1.56e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 45.16  E-value: 1.56e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGN 44
Cdd:COG3640     8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-40 1.91e-05

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: 44.75  E-value: 1.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1124574266   3 KVFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD 40
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-191 6.05e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 43.27  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQgnatmgsgidkhaleHSIYDVLigECDLG-----------QAMQ---- 75
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPA---------------HSLGDVL--GTELGneptevavpnlYALEidpe 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  76 ------FSEHGGY--QLLPANRDLTAAEV--------ALLEMkmkesrLRYALapiRENYDYILIDCPPS---LNMLTI- 135
Cdd:COG0003    74 aeleeyWERVRAPlrGLLPSAGVDELAESlpgteelaALDEL------LELLE---EGEYDVIVVDTAPTghtLRLLSLp 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124574266 136 NALVAADGVIIPMQceyyalEGLSDLVNSIQRIAQLLNPKL---------QIEGLLRTMYDPRIS 191
Cdd:COG0003   145 ELLGWWLDRLLKLR------RKASGLGRPLAGILGLPDDPVlegleelreRLERLRELLRDPERT 203
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-62 1.09e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 42.45  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT---MG------------SGIDKHALEHSIYD 62
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTrnlVGekiptvldvlreKGIDNLGLEDIIYE 75
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-135 1.29e-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: 42.11  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQgnatmgsgidkhaleHSIYDVLigECDLG-----------QAMQ---- 75
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPA---------------HSLSDAF--GQKLGgetpvkgapnlWAMEidpe 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  76 --FSEH--------GGYQLLPANRDLTAAE----------VALLEMkmkesrLRYALApirENYDYILIDCPP---SLNM 132
Cdd:cd02035    71 eaLEEYweevkellAQYLRLPGLDEVYAEEllslpgmdeaAAFDEL------REYVES---GEYDVIVFDTAPtghTLRL 141


                  ...
gi 1124574266 133 LTI 135
Cdd:cd02035   142 LSL 144
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-46 2.79e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 41.28  E-value: 2.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT 46
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADST 43
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 3-46 4.43e-04

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: 40.74  E-value: 4.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1124574266   3 KVFAIANqKGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT 46
Cdd:cd02032     1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-40 8.92e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 40.03  E-value: 8.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1124574266   4 VFAIANQKGGVGKTTTCINLAASLVATKRRVLLIDLD 40
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 13-47 2.38e-03

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


Pssm-ID: 406878  Cd Length: 187  Bit Score: 38.01  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1124574266  13 GVGKTTTCINLAASLVATKRRVLLIDLDP-QGNATM 47
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDVgQSEIGP 39
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-44 2.46e-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: 38.92  E-value: 2.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGN 44
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 6-49 5.96e-03

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: 37.29  E-value: 5.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1124574266   6 AIANqKGGVGKTTTCINLAASLVATKRRVLLIDLDPqgNATMGS 49
Cdd:cd02034     4 AVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP--NSNLAE 44
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-46 6.68e-03

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: 37.11  E-value: 6.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT 46
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-100 7.84e-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: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNATmgsgidkHALEHSIYDVLIGECDLGQAMQfsehgGYQ---LLPA 87
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLS-------VTLTGSLNNLQVSRIDPKQETE-----RYRqevLATK 396

                          90
                  ....*....|...
gi 1124574266  88 NRDLTAAEVALLE 100
Cdd:TIGR04291 397 GKELDEDGKAYLE 409
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
 13-127 9.23e-03

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 36.58  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124574266  13 GVGKTTTCINLAASLVATKRRVLLIDLDPqgnatmgsgidkhALEHSIYDVLIGECDLGQAMQFSEHggYQLLPaNRDLT 92
Cdd:pfam03029   6 GSGKTTFVGALSEILPLRGRPVYVVNLDP-------------AAENLPYPADIDIRELITVADVMED--YGLGP-NGALT 69

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1124574266  93 AAevalleMKMKESRLRYALAPIRENYDYILIDCP 127
Cdd:pfam03029  70 VA------MDFGRITLDWLDEELKREDDYYLFDTP 98
chlL CHL00072
photochlorophyllide reductase subunit L
 11-46 9.43e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 36.64  E-value: 9.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1124574266  11 KGGVGKTTTCINLAASLVATKRRVLLIDLDPQGNAT 46
Cdd:CHL00072    8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDST 43
 
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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