NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515674926|ref|WP_017107526|]
View 

MULTISPECIES: ParA family protein [Vibrio]

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 ...
 3-254 1.94e-128

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: 363.79  E-value: 1.94e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLVEDSPFDEVVCRSTSGNY 82
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  83 DLIAANGDVTAAEIKLMEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALM 162
Cdd:COG1192   82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 163 DTISKLAAVVNEDLKIEGLLRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:COG1192  162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                        250
                 ....*....|..
gi 515674926 243 LALAGEMLRREE 254
Cdd:COG1192  242 RALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-254 1.94e-128

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: 363.79  E-value: 1.94e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLVEDSPFDEVVCRSTSGNY 82
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  83 DLIAANGDVTAAEIKLMEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALM 162
Cdd:COG1192   82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 163 DTISKLAAVVNEDLKIEGLLRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:COG1192  162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                        250
                 ....*....|..
gi 515674926 243 LALAGEMLRREE 254
Cdd:COG1192  242 RALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 7.25e-80

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: 237.87  E-value: 7.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    2 GRIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLVEDSPFDEVVCRSTSGN 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   82 YDLIAANGDVTAAEIKLMEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTAL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 515674926  162 MDTISKLAAVVNEDLKI 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 7.35e-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: 155.01  E-value: 7.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASgvdkyqveataydllvedspfdevvcrstsgny 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  83 dliaangdvtaaeiklmevfarevrlknalasirsnYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALM 162
Cdd:cd02042   48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515674926 163 DTISKLAAVVNEDLKIEGLLRTMYDPRNRLSNEVSDQLK 201
Cdd:cd02042   92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
4-248 2.47e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 112.26  E-value: 2.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKyqveataydllvEDSPFDEVVCrstsgnyd 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARE------------DERPFPVVGL-------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  84 liaangdvtaaeiklmevfAREvRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALMD 163
Cdd:NF041546  61 -------------------ARP-TLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 164 TIsKLAAVVNEDLKIEGLL-RTmyDPRNRLSNEVSDQLKKhFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:NF041546 121 LI-KEAREYTPGLKAAFVLnRA--IARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREI 196


                 ....*.
gi 515674926 243 LALAGE 248
Cdd:NF041546 197 RALAKE 202
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-219 3.64e-30

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 114.08  E-value: 3.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   1 MGRIVAIANQKGGVGKTTTCVNLAASMAAT-KRKILVVDLDPQGNAT--MASGVDKYQVEATaYDLLVEDSPFDEVVCrS 77
Cdd:NF041283   1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATqfLSKTFNVPNFPQS-FMKCVEDGDLEKGIV-H 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  78 TSGNYDLIAAN------GDVTAAEIKlmEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCE 151
Cdd:NF041283  79 LTPNLDLIAGDydtrelGDFLADKFK--SEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515674926 152 YFALEG-----LTALMDTISKLAAVVNedLKIEGLLRTMYDPRNRLSNEVSDQLKKHFG-NKVYRTVIPRNVRL 219
Cdd:NF041283 157 QFAFEGskkliLTYLQTLVDDFGDEIN--VQVAGILPVLLQARRPLQQKIVDETIEYFGkDNVFNNIIKNHARL 228
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-208 7.50e-27

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: 106.99  E-value: 7.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGvdkYQVE------ATAYDLLVEDS---PFDEVV 74
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFG---YQPEfdvgenETLYGAIRYDDerrPISEII 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   75 CRSTSGNYDLIAANgdvtaaeIKLMEvFAREV----------------RLKNALASIRSNYDFIFIDCPPSLNLLTINAM 138
Cdd:TIGR03453 183 RKTYFPGLDLVPGN-------LELME-FEHETpralsrgqggdtiffaRVGEALAEVEDDYDVVVIDCPPQLGFLTLSAL 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926  139 AAADSVLVP--------MQCEYFaLEGLTALMDTISKLAAVVNED-LKiegLLRTMYDPRNRLSNEVSDQLKKHFGNKV 208
Cdd:TIGR03453 255 CAATGVLITvhpqmldvMSMSQF-LLMTGDLLGVVREAGGNLSYDfMR---YLVTRYEPNDGPQAQMVAFLRSLFGDHV 329
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-222 1.19e-20

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 90.12  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGV---DKYQVEATAYDLLVEDS---PFDEVVCR 76
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlpeTDVGANETLYAAIRYDDtrrPLRDVIRP 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  77 STSGNYDLIAANGDVTAAE----IKLMEVFARE----VRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPM 148
Cdd:PRK13869 202 TYFDGLHLVPGNLELMEFEhttpKALSDKGTRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITV 281

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926 149 QCEYFALEGLTALMDTISKLAAVVNE---DLKIEGL--LRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVIPRNVRLAEA 222
Cdd:PRK13869 282 HPQMLDIASMSQFLLMTRDLLGVVKEaggNLQYDFIryLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDA 360
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-254 1.94e-128

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: 363.79  E-value: 1.94e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLVEDSPFDEVVCRSTSGNY 82
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  83 DLIAANGDVTAAEIKLMEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALM 162
Cdd:COG1192   82 DLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 163 DTISKLAAVVNEDLKIEGLLRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:COG1192  162 ETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAY 241

                        250
                 ....*....|..
gi 515674926 243 LALAGEMLRREE 254
Cdd:COG1192  242 RALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-178 7.25e-80

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: 237.87  E-value: 7.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    2 GRIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLVEDSPFDEVVCRSTSGN 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   82 YDLIAANGDVTAAEIKLMEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTAL 161
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 515674926  162 MDTISKLAAVVNEDLKI 178
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-228 3.60e-58

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: 184.47  E-value: 3.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    5 VAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEA--TAYDLLVEDSPFDEVVC--RSTSG 80
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPAlqALAEGLKGRVNLDPILLkeKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   81 NYDLIAANGDVTAAEIKLMEVFaREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTA 160
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPR-KEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926  161 LMDTISKLAAVVN-EDLKIEGLLRTMYDPRNRLSNEVSDQLKKHFGNKVYrTVIPRNVRLAEAPSHGKP 228
Cdd:pfam01656 160 LGGVIAALVGGYAlLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVL-GVIPRDEAVAEAPARGLP 227
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-201 7.35e-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: 155.01  E-value: 7.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASgvdkyqveataydllvedspfdevvcrstsgny 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  83 dliaangdvtaaeiklmevfarevrlknalasirsnYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALM 162
Cdd:cd02042   48 ------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLL 91

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515674926 163 DTISKLAAVVNEDLKIEGLLRTMYDPRNRLSNEVSDQLK 201
Cdd:cd02042   92 DTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
4-248 2.47e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 112.26  E-value: 2.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKyqveataydllvEDSPFDEVVCrstsgnyd 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARE------------DERPFPVVGL-------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  84 liaangdvtaaeiklmevfAREvRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALMD 163
Cdd:NF041546  61 -------------------ARP-TLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVD 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 164 TIsKLAAVVNEDLKIEGLL-RTmyDPRNRLSNEVSDQLKKhFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:NF041546 121 LI-KEAREYTPGLKAAFVLnRA--IARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREI 196


                 ....*.
gi 515674926 243 LALAGE 248
Cdd:NF041546 197 RALAKE 202
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-219 3.64e-30

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 114.08  E-value: 3.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   1 MGRIVAIANQKGGVGKTTTCVNLAASMAAT-KRKILVVDLDPQGNAT--MASGVDKYQVEATaYDLLVEDSPFDEVVCrS 77
Cdd:NF041283   1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNATqfLSKTFNVPNFPQS-FMKCVEDGDLEKGIV-H 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  78 TSGNYDLIAAN------GDVTAAEIKlmEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCE 151
Cdd:NF041283  79 LTPNLDLIAGDydtrelGDFLADKFK--SEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515674926 152 YFALEG-----LTALMDTISKLAAVVNedLKIEGLLRTMYDPRNRLSNEVSDQLKKHFG-NKVYRTVIPRNVRL 219
Cdd:NF041283 157 QFAFEGskkliLTYLQTLVDDFGDEIN--VQVAGILPVLLQARRPLQQKIVDETIEYFGkDNVFNNIIKNHARL 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-253 2.43e-27

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: 104.97  E-value: 2.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  18 TTCVNLAASMAATKRKILVVDLDPQ-GNATMASGVDkyqVEATAYDLLVEDSPFDEVVCRsTSGNYDLIAANGDVTAaei 96
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLE---PKATLADVLAGEADLEDAIVQ-GPGGLDVLPGGSGPAE--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  97 klMEVFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALMdtisKLAAVVNEDL 176
Cdd:COG0455   74 --LAELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALL----KLLRRRLGVR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 177 KIeGLLRTMYDPRN---RLSNEVSDQLKKHFGNKV-YRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAYLALAGEMLRR 252
Cdd:COG0455  148 RA-GVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226


                 .
gi 515674926 253 E 253
Cdd:COG0455  227 P 227
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-208 7.50e-27

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: 106.99  E-value: 7.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGvdkYQVE------ATAYDLLVEDS---PFDEVV 74
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFG---YQPEfdvgenETLYGAIRYDDerrPISEII 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   75 CRSTSGNYDLIAANgdvtaaeIKLMEvFAREV----------------RLKNALASIRSNYDFIFIDCPPSLNLLTINAM 138
Cdd:TIGR03453 183 RKTYFPGLDLVPGN-------LELME-FEHETpralsrgqggdtiffaRVGEALAEVEDDYDVVVIDCPPQLGFLTLSAL 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926  139 AAADSVLVP--------MQCEYFaLEGLTALMDTISKLAAVVNED-LKiegLLRTMYDPRNRLSNEVSDQLKKHFGNKV 208
Cdd:TIGR03453 255 CAATGVLITvhpqmldvMSMSQF-LLMTGDLLGVVREAGGNLSYDfMR---YLVTRYEPNDGPQAQMVAFLRSLFGDHV 329
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-249 3.30e-21

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: 89.40  E-value: 3.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDldpqGNATMAS-----GVDKYQVeaTAYDLLVEDSPFDEVVCRS 77
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALD----ADITMANlelilGMEDKPV--TLHDVLAGEADIKDAIYEG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   78 TSGNYdliaangdVTAAEIKLMEVF-AREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALE 156
Cdd:TIGR01969  75 PFGVK--------VIPAGVSLEGLRkADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  157 -----GLTALMDTISKLAAVVNedlkiegllRTMYDPRNRLSNEVSDQLKkhfgNKVYrTVIPRNVRLAEAPSHGKPAMY 231
Cdd:TIGR01969 147 dalktKIVAEKLGTAILGVVLN---------RVTRDKTELGREEIETILE----VPVL-GVVPEDPEVRRAAAFGEPVVI 212

                         250
                  ....*....|....*...
gi 515674926  232 YDKYSAGAKAYLALAGEM 249
Cdd:TIGR01969 213 YNPNSPAAQAFMELAAEL 230
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-254 6.46e-21

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: 90.17  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   2 GRIVAIANQKGGVGKTTTCVNLAASMAA-TKRKILVVDLDPQ-GNATMASGVDKYQveaTAYDLLVEDSPFDEVVCRST- 78
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQfGDVALYLDLEPRR---GLADALRNPDRLDETLLDRAl 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  79 ---SGNYDLIAANGDVTAAEiklmEVFAREV-RLKNALasiRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFA 154
Cdd:COG4963  179 trhSSGLSVLAAPADLERAE----EVSPEAVeRLLDLL---RRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPS 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 155 LEGLTALMDTISKLAAvvnEDLKIEgLLRTMYDPRNRLSnevSDQLKKHFGNKVYrTVIPRNVR-LAEAPSHGKPAMYYD 233
Cdd:COG4963  252 LRNAKRLLDLLRELGL---PDDKVR-LVLNRVPKRGEIS---AKDIEEALGLPVA-AVLPNDPKaVAEAANQGRPLAEVA 323

                        250       260
                 ....*....|....*....|.
gi 515674926 234 KYSAGAKAYLALAGEMLRREE 254
Cdd:COG4963  324 PKSPLAKAIRKLAARLTGRPA 344
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-222 1.19e-20

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 90.12  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGV---DKYQVEATAYDLLVEDS---PFDEVVCR 76
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlpeTDVGANETLYAAIRYDDtrrPLRDVIRP 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  77 STSGNYDLIAANGDVTAAE----IKLMEVFARE----VRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPM 148
Cdd:PRK13869 202 TYFDGLHLVPGNLELMEFEhttpKALSDKGTRDglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITV 281

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926 149 QCEYFALEGLTALMDTISKLAAVVNE---DLKIEGL--LRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVIPRNVRLAEA 222
Cdd:PRK13869 282 HPQMLDIASMSQFLLMTRDLLGVVKEaggNLQYDFIryLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDA 360
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-246 1.08e-19

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: 84.95  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDpqgnATMAS-----GVDKyQVEATAYDLLVEDSPFDEVVCRS 77
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD----IGLRNldlilGLEN-RIVYTLVDVLEGECRLEQALIKD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  78 TSG-NYDLIAANgdVTAAEIKLmevfaREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEyfale 156
Cdd:cd02036   76 KRWeNLYLLPAS--QTRDKDAL-----TPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPE----- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 157 gLTALMDTISKLAAVVNEDLKIEGLLRTMYDP-RNRLSNEVS-DQLKKHFGNKVYrTVIPRNVRLAEAPSHGKPAMYYDK 234
Cdd:cd02036  144 -ISSVRDADRVIGLLESKGIVNIGLIVNRYRPeMVKSGDMLSvEDIQEILGIPLL-GVIPEDPEVIVATNRGEPLVLYKP 221

                        250
                 ....*....|..
gi 515674926 235 YSAGAKAYLALA 246
Cdd:cd02036  222 NSLAAKAFENIA 233
PHA02518 PHA02518
ParA-like protein; Provisional
 3-252 2.93e-19

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 82.98  E-value: 2.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASgvdkyqvEATAydllvEDSPFDEVVCRSTSgny 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWA-------EARE-----EGEPLIPVVRMGKS--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  83 dliaangdvtaaeiklmevfarevrLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLTALM 162
Cdd:PHA02518  66 -------------------------IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLV 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 163 DTIsKLAAVVNEDLKIEGLLRTMYDPRNRLSNEVSDQLkKHFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:PHA02518 121 ELI-KARQEVTDGLPKFAFIISRAIKNTQLYREARKAL-AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198

                        250
                 ....*....|
gi 515674926 243 LALAGEMLRR 252
Cdd:PHA02518 199 IQLVKELFRG 208
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-146 9.28e-18

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: 79.54  E-value: 9.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD-PQGNATMASGVdkyQVEATAYDLLVEDSPFDEVVCRSTSGN 81
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGL---APKKTLGDVLKGRVSLEDIIVEGPEGL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515674926  82 YDLIAANGDVTAAEIKlmevFAREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLV 146
Cdd:cd02038   78 DIIPGGSGMEELANLD----PEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-191 1.29e-16

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: 77.53  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQG-NATMASGVDKyqvEATAYDLLVEDSPFDEVVCRSTSGN 81
Cdd:COG0489   93 EVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGpSLHRMLGLEN---RPGLSDVLAGEASLEDVIQPTEVEG 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  82 YDLIAANGDVTAAeiklMEVFAREvRLKNALASIRSNYDFIFIDCPPSLNL--LTINAMAAADSVLVpmqceyfALEGLT 159
Cdd:COG0489  170 LDVLPAGPLPPNP----SELLASK-RLKQLLEELRGRYDYVIIDTPPGLGVadATLLASLVDGVLLV-------VRPGKT 237

                        170       180       190
                 ....*....|....*....|....*....|..
gi 515674926 160 ALMDTISKLAAVVNEDLKIEGLLRTMYDPRNR 191
Cdd:COG0489  238 ALDDVRKALEMLEKAGVPVLGVVLNMVCPKGE 269
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-213 1.48e-15

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 75.40  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVD-LDPQGNATMASG-VDKYQVEATayDLLV-------EDSPFdeVV 74
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGwVPDLHIHAE--DTLLpfylgekDDATY--AI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  75 CRSTSGNYDLIAANGDVTAAEIKLMEVF-------AREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVP 147
Cdd:PRK13705 184 KPTCWPGLDIIPSCLALHRIETELMGKFdegklptDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVP 263

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515674926 148 MQCEYF----ALEGLTALMDTISklaavvNEDLK-----IEGLLRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVI 213
Cdd:PRK13705 264 TPAELFdytsALQFFDMLRDLLK------NVDLKgfepdVRILLTKYSNSNGSQSPWMEEQIRDAWGSMVLKNVV 332
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-146 5.49e-15

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: 71.06  E-value: 5.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDP-QGNATMASGVDKyqvEATAYDLLVEDSPFDEVVCRSTSGN 81
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPN---EPGLSEVLSGQASLEDVIQSTNIPN 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515674926  82 YDLIAANGDVTAAeiklMEVFAREvRLKNALASIRSNYDFIFIDCPPSLNLL-TINAMAAADSVLV 146
Cdd:cd05387   97 LDVLPAGTVPPNP----SELLSSP-RFAELLEELKEQYDYVIIDTPPVLAVAdALILAPLVDGVLL 157
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 4-247 1.53e-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: 70.84  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLvEDSPFDEVVCRSTSGnyD 83
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALL-NGADWAAAAYRSPDG--V 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   84 LIAANGDVTAAEiklmevfaREVR-------LKNALASI-RSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFAL 155
Cdd:TIGR03371  80 LFLPYGDLSADE--------REAYqahdagwLARLLQQLdLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAACY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  156 EGLTALMDTISKLAAVVNEdlkiEGLLRTMYDPRNRLSNEVSDQLKKHFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKY 235
Cdd:TIGR03371 152 ATLHQLALALFAGSGPRDG----PRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPH 227

                         250
                  ....*....|..
gi 515674926  236 SAGAKAYLALAG 247
Cdd:TIGR03371 228 SQAAHDIRTLAG 239
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-173 1.68e-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: 70.77  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAA-TKRKILVVDLD-PQGNATM-ASGVDKYQVEATAYDLLVEDSPFDEVVCRSTS 79
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDlPFGDLGLyLNLRPDYDLADVIQNLDRLDRTLLDSAVTRHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  80 GNYDLIAANGDVTAAEIKlmevfaREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFALEGLT 159
Cdd:cd03111   81 SGLSLLPAPQELEDLEAL------GAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNAR 154

                        170       180
                 ....*....|....*....|.
gi 515674926 160 ALMDTI-------SKLAAVVN 173
Cdd:cd03111  155 RLLDSLrelegssDRLRLVLN 175
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-230 2.22e-14

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 71.97  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVD-LDPQGNATMASG-VDKYQVEATAYDL---LVEDSPFDEVVCRST 78
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGyVPDLHIHADDTLLpfyLGERDNAEYAIKPTC 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  79 SGNYDLIAANGDVTAAEIKLMEVFARE-------VRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCE 151
Cdd:PHA02519 188 WPGLDIIPSCLALHRIETDLMQYHDAGklphpphLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 152 YF----ALEGLTALMDTISKLaavvneDL----KIEGLLRTMYDPRN-RLSNEVSDQLKKHFGNKVYRTViprnVRLAEA 222
Cdd:PHA02519 268 LFdyvsVLQFFTMLLDLLATV------DLggfePVVRLLLTKYSLTVgNQSRWMEEQIRNTWGSMVLRQV----VRVTDE 337


                 ....*...
gi 515674926 223 PSHGKPAM 230
Cdd:PHA02519 338 VGKGQIKM 345
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-256 4.03e-13

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: 66.98  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    2 GRIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDpQG--NATMASG---------VDKYQVEATAYDLLVEDSPF 70
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-IGlrNLDLLLGlenrivytlVDVVEGECRLQQALIKDKRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   71 DevvcrstsgNYDLIAangdvtAAEIKLMEVFAREVrLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQC 150
Cdd:TIGR01968  80 K---------NLYLLP------ASQTRDKDAVTPEQ-MKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  151 EyfalegLTALMDTISKLAAVVNEDLKIEGLLRTMYDPRNRLSNEV--SDQLKKHFGNKVYrTVIPRNVRLAEAPSHGKP 228
Cdd:TIGR01968 144 E------VSAVRDADRVIGLLEAKGIEKIHLIVNRLRPEMVKKGDMlsVDDVLEILSIPLI-GVIPEDEAIIVSTNKGEP 216

                         250       260
                  ....*....|....*....|....*...
gi 515674926  229 AMYYDKYSAGaKAYLALAgEMLRREEIP 256
Cdd:TIGR01968 217 VVLNDKSRAG-KAFENIA-RRILGEEVP 242
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-148 2.28e-10

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: 59.39  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQgNATMASGVDKYQ--VEATAYDLlvedsPFDEVVCRSTSG 80
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFHRYFENRSatADRTGLSL-----PTPEHLNLPDND 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515674926   81 NYDliaANGDVTAAEIKLMEVFARevrlknalasIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPM 148
Cdd:pfam09140  75 VAE---VPDGENIDDARLEEAFAD----------LEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-146 2.41e-10

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 59.30  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   1 MGRIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDpqgnatmasgvdkyqVEATAYDLL--VEdspfDEVVcrst 78
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD---------------IGLRNLDLVmgLE----NRIV---- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  79 sgnYDLIaangDVTAAEIKLMEVFAREVRL-------------KNAL---------ASIRSNYDFIFIDCPPSlnlltI- 135
Cdd:COG2894   58 ---YDLV----DVIEGECRLKQALIKDKRFenlyllpasqtrdKDALtpeqmkklvEELKEEFDYILIDSPAG-----Ie 125

                        170
                 ....*....|....*
gi 515674926 136 ----NAMAAADSVLV 146
Cdd:COG2894  126 qgfkNAIAGADEAIV 140
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-252 1.09e-09

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: 57.38  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNAT---MASGVDKYQVEATAYDLLVEDSPFDEVVCRStSGNYDLIAA 87
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTlllTGGKVPPTIDEMLTEDGTAEELRREDLLFSG-FNGVDCVEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  88 NGD---------VTAAEIKLMEvfarEVRLKNalasirSNYDFIFIDCppsLNLLTINAMAA------ADSVLVPMQCEY 152
Cdd:cd02117   87 GGPepgvgcggrGIGTMLELLE----EHGLLD------DDYDVVIFDV---LGDVVCGGFAAplrrgfAQKVVIVVSEEL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 153 ---FALEGLTALMDTISKLAAVVNedlkieGLLRTMYDPRNRlsnEVSDQLKKHFGNKVYrTVIPRNVRLAEAPSHGKPA 229
Cdd:cd02117  154 mslYAANNIVKAVENYSKNGVRLA------GLVANLRDPAGT---EEIQAFAAAVGTKIL-AVIPRDPAVRRAELARVTV 223

                        250       260
                 ....*....|....*....|...
gi 515674926 230 MYYDKYSAGAKAYLALAGEMLRR 252
Cdd:cd02117  224 FEHDPVSPAASEFARLAAKIADA 246
minD CHL00175
septum-site determining protein; Validated
 1-146 1.41e-09

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 57.09  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   1 MGRIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD-PQGNATMASGVDKyQVEATAYDLLVEDSPFDEVVCRSTS 79
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLEN-RVLYTAMDVLEGECRLDQALIRDKR 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926  80 -GNYDLIAangdvtAAEIKLMEVFAREvRLKNALASIRS-NYDFIFIDCPPSLNLLTINAMAAADSVLV 146
Cdd:CHL00175  93 wKNLSLLA------ISKNRQRYNVTRK-NMNMLVDSLKNrGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-146 1.76e-09

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: 55.91  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQgNATMaSGVDKYQVEATAY-DLLVEDSPFDEVVCRSTSGN 81
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMR-NSVM-SGTFKSQNKITGLtNFLSGTTDLSDAICDTNIEN 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515674926   82 YDLIAAnGDVTAAEIKLMEvfarEVRLKNALASIRSNYDFIFIDCPPsLNLLT---INAMAAADSVLV 146
Cdd:TIGR01007  96 LDVITA-GPVPPNPTELLQ----SSNFKTLIETLRKRFDYIIIDTPP-IGTVTdaaIIARACDASILV 157
PRK10818 PRK10818
septum site-determining protein MinD;
1-253 1.69e-08

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 53.79  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   1 MGRIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD-PQGNATMASGVDKYQVeataYD---LLVEDSPFDEVVCR 76
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRVV----YDfvnVIQGDATLNQALIK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  77 STSGNYDLIaangdVTAAEIKLMEVFARE--VRLKNALASIrsNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEYFA 154
Cdd:PRK10818  77 DKRTENLYI-----LPASQTRDKDALTREgvAKVLDDLKAM--DFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 155 L---EGLTALMDTISKLAAVVNEDLKiEGLLRTMYDPrNRLSNevSDQLKKHFGNKVYRT----VIPRNVRLAEAPSHGK 227
Cdd:PRK10818 150 VrdsDRILGILASKSRRAENGEEPIK-EHLLLTRYNP-GRVSR--GDMLSMEDVLEILRIklvgVIPEDQSVLRASNQGE 225

                        250       260
                 ....*....|....*....|....*.
gi 515674926 228 PAMyYDKYSAGAKAYLALAGEMLRRE 253
Cdd:PRK10818 226 PVI-LDIEADAGKAYADTVDRLLGEE 250
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-40 4.12e-07

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: 49.76  E-value: 4.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 515674926    3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD 40
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 3-145 4.78e-07

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 50.49  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD-PQGNATMASGVDKyqvEATAYDLLVEDSPFDEVVCRSTSGN 81
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFGKAP---KPGLLDLLAGEASIEAGIHRDQRPG 630

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515674926   82 YDLIAAnGDVTAAEIKLMEVFAREvRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAA-ADSVL 145
Cdd:TIGR01005 631 LAFIAA-GGASHFPHNPNELLANP-AMAELIDNARNAFDLVLVDLAALAAVADAAAFAAlADGIL 693
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 6.07e-07

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: 48.65  E-value: 6.07e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD 40
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-52 1.46e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.85  E-value: 1.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVD 52
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLE 49
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 2.19e-06

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 45.11  E-value: 2.19e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515674926   3 RIVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD 40
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
3-89 4.77e-06

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 46.67  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    3 RIVAIANqKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQveATAYDLLVEDSPFDEV----VCRST 78
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQ--PTVLDTAREKGYVEDVevedVVYKG 77

                          90
                  ....*....|.
gi 515674926   79 SGNYDLIAANG 89
Cdd:pfam00142  78 YGGVKCVESGG 88
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-46 1.01e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 45.53  E-value: 1.01e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNAT 46
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCT 44
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 4-246 3.46e-05

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: 43.91  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926    4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATAYDLLvEDSPFDEVVCRSTSGnYD 83
Cdd:pfam06564   3 ILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSPDNLLRLHFNVPFEHRQGWARAEL-DGADWRDAALEYTPG-LD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   84 LIAAnGDVTAAEIKLMEVF-AREVRLKNALASIRSNYDFIFIDCPPSLNLLTINAMAAADSVLVPMQCEyfalegltalM 162
Cdd:pfam06564  81 LLPF-GRLSVEEQENLQQLqPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD----------A 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  163 DTISKLAAVVNEDLKIegLLRTMYDPRNRLSNEVSdQLKKHFGNKVYRTVIPRNVRLAEAPSHGKPAMYYDKYSAGAKAY 242
Cdd:pfam06564 150 NCHVLLHQQPLPDADH--LLINDFRPASQLQQDLL-QLWRQSQRRLLPLVIHRDEALAEALAAKQPLGEYRPDSLAAEEV 226


                  ....
gi 515674926  243 LALA 246
Cdd:pfam06564 227 LTLA 230
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-40 3.91e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 44.26  E-value: 3.91e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 515674926   4 IVAIANQKGGVGKTTTCVNLAASMAATKRKILVVDLD 40
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 3-233 8.75e-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: 42.68  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   3 RIVAIANqKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNATMASGVDKYQVEATA---------------------Y 61
Cdd:cd02034    1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKtigdirertgakkgeppegmsL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  62 DLLVEDSPFDEVVCRstsGNYDLIAAnGDVTAAEIKL---MEVFAREVRLKNALasirSNYDFIFIDCPPSLNLLTINAM 138
Cdd:cd02034   80 NPYVDDIIKEIIVEP---DGIDLLVM-GRPEGGGSGCycpVNALLRELLRHLAL----KNYEYVVIDMEAGIEHLSRGTI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 139 AAADSVLVPMQCEYFALEglTALmdTISKLAavvnEDLKIegllRTMYDPRNRLSNEVSDQLKKHFGNKVYRT-VIPRNV 217
Cdd:cd02034  152 RAVDLLIIVIEPSKRSIQ--TAK--RIKELA----EELGI----KKIYLIVNKVRNEEEQELIEELLIKLKLIgVIPYDE 219

                        250
                 ....*....|....*.
gi 515674926 218 RLAEAPSHGKPAMYYD 233
Cdd:cd02034  220 EIMEADLKGKPLFDLD 235
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-41 1.15e-03

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: 39.41  E-value: 1.15e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDP 41
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP 38
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-46 1.41e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 39.18  E-value: 1.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515674926   1 MGRIVAIANqKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNAT 46
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-188 1.41e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 39.42  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGN-----------------------------ATMASGVDKYQveATAY 61
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSlgdvlgtelgneptevavpnlyaleidpeAELEEYWERVR--APLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  62 DLLveDSPFDEVVCRSTSGnydliaangdvtAAEIKLMEVFAREVRlknalasiRSNYDFIFIDCPPS---LNLLTI-NA 137
Cdd:COG0003   89 GLL--PSAGVDELAESLPG------------TEELAALDELLELLE--------EGEYDVIVVDTAPTghtLRLLSLpEL 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926 138 MAAADSVLVPMQceyfalEGLTALMDTISKLAAVVNEDL---------KIEGLLRTMYDP 188
Cdd:COG0003  147 LGWWLDRLLKLR------RKASGLGRPLAGILGLPDDPVlegleelreRLERLRELLRDP 200
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-46 1.50e-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: 39.03  E-value: 1.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNAT 46
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
nifH PRK13233
nitrogenase iron protein;
1-125 1.52e-03

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 39.03  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926   1 MGRIVAIANqKGGVGKTTTCVNLAASMAA-TKRKILVVDLDPQGNAT--MASGVDKYQV---------EATAYDLLVEdS 68
Cdd:PRK13233   1 MTRKIAIYG-KGGIGKSTTTQNTAAAMAYfHDKKVFIHGCDPKADSTrlILGGKPQTTMmdtlrelgeEKVTPDKVIK-T 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515674926  69 PFDEVVCRSTSGNYDLI--AANGDVTAaeIKLMEvfarevrlknALASIRSNYDFIFID 125
Cdd:PRK13233  79 GFKDIRCVESGGPEPGVgcAGRGVITA--IDLME----------ENGAYTDDLDFVFFD 125
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 11-46 1.80e-03

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: 38.82  E-value: 1.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 515674926  11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNAT 46
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST 43
GPN cd17868
GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small ...
 13-127 3.02e-03

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: 37.68  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  13 GVGKTTTCVNLAASMAATKRKILVVDLDPqGNATmasgvdkyqvEATAYDLLVEDSPF-DEVvcrstSGNYDLiAANGDV 91
Cdd:cd17868   10 GSGKTTFCKNMKEHLRARKRNPYVINLDP-GNIN----------EPLDYDIDIRDLIKyDDI-----MEELDL-GPNGSI 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515674926  92 TAAeiklMEVFAR-EVRLKNALASIRSNYDFIFIDCP 127
Cdd:cd17868   73 VYS----LEYFEKnFDWFEKKLENEDKNPHYILFDCP 105
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-44 4.19e-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: 38.15  E-value: 4.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 515674926   11 KGGVGKTTTCVNLAASMAATKRKILVVDLDPQGN 44
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
13-130 6.65e-03

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 37.44  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515674926  13 GVGKTTTCVNLAASMAATKRKILVVDLDPQGNATM----ASGVDKYQveatayDLLVEDSPFDEVVCRSTSGNYDLIaAN 88
Cdd:PRK11519 537 SIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHellgTNNVNGLS------DILIGQGDITTAAKPTSIANFDLI-PR 609

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515674926  89 GDV--TAAEIKLMEVFAREVrlknALASirSNYDFIFIDCPPSL 130
Cdd:PRK11519 610 GQVppNPSELLMSERFAELV----NWAS--KNYDLVLIDTPPIL 647
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 3-46 8.45e-03

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


Pssm-ID: 349753  Cd Length: 329  Bit Score: 37.12  E-value: 8.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 515674926   3 RIVAIANqKGGVGKTTTCVNLAASMAATKRKILVVDLDPQGNAT 46
Cdd:cd02033   32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTT 74
 
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