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Conserved domains on  [gi|627203010|gb|KCT22431|]
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chromosome partitioning protein ParA [Mycobacterium tuberculosis XTB13-121]

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

Gene Ontology:  GO:0005524
PubMed:  26339031|21963112|22672910|14584729

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 ...
 85-337 5.94e-126

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


:

Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 361.48  E-value: 5.94e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGItDRQSGTPSSYEMLIGEVSLHTALRRSpHSE 164
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL-DPDDLDPTLYDLLLDDAPLEDAIVPT-EIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 RLFCIPATIDLAGAEIELVSMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLAD-DYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 245 QLMRNIEMVKAHLNPQLEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSRGA 324
Cdd:COG1192  159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGA 238

                        250
                 ....*....|...
gi 627203010 325 MSYLDASRELAER 337
Cdd:COG1192  239 KAYRALAEELLER 251
ArsA_halo super family cl49411
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 43-123 6.36e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


The actual alignment was detected with superfamily member NF041417:

Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 38.32  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  43 NPTMNVSRETS--TEFDTPIGAAAERAMRVLhttheplqRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVID 120
Cdd:NF041417 297 EPTVDVAVITEeeTEETSPSETDKEAVMELL--------RPQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVT 368


                 ...
gi 627203010 121 LDP 123
Cdd:NF041417 369 TDP 371
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 85-337 5.94e-126

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 361.48  E-value: 5.94e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGItDRQSGTPSSYEMLIGEVSLHTALRRSpHSE 164
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL-DPDDLDPTLYDLLLDDAPLEDAIVPT-EIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 RLFCIPATIDLAGAEIELVSMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLAD-DYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 245 QLMRNIEMVKAHLNPQLEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSRGA 324
Cdd:COG1192  159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGA 238

                        250
                 ....*....|...
gi 627203010 325 MSYLDASRELAER 337
Cdd:COG1192  239 KAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 85-263 1.16e-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: 243.26  E-value: 1.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGItDRQSGTPSSYEMLIGEVSLHTALRRSPHsE 164
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGI-DKNNVEKTIYELLIGECNIEEAIIKTVI-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  165 RLFCIPATIDLAGAEIELVSMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKD-NYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLS 158

                         170
                  ....*....|....*....
gi 627203010  245 QLMRNIEMVKAHLNPQLEV 263
Cdd:pfam13614 159 QLLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 85-286 5.88e-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: 158.09  E-value: 5.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALgitdrqsgtpssyemligevslhtalrrsphse 164
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 rlfcipatidlagaeielvsmvarenrlrtalaaldnfdFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:cd02042   48 ---------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLA 88

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 627203010 245 QLMRNIEMVKAHLNPQLEVTTVILTMYDGRTKLADQVADEVR 286
Cdd:cd02042   89 KLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
86-335 1.73e-28

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 109.56  E-value: 1.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  86 VLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNAStalgitdrqsgtpssyemligevslHTALRRSphSER 165
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL-------------------------DWAAARE--DER 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 166 LFCipatidlagaeielVSMVARENrLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVSQ 245
Cdd:NF041546  54 PFP--------------VVGLARPT-LHRELPSLAR-DYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASAD 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 246 LmrnIEMVKA--HLNPQLEVTTVIlTMYDGRTKLADQVADEVRQYfGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSrg 323
Cdd:NF041546 118 T---VDLIKEarEYTPGLKAAFVL-NRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG-- 190

                        250
                 ....*....|..
gi 627203010 324 amsylDASRELA 335
Cdd:NF041546 191 -----KAAREIR 197
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 85-335 8.39e-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: 98.26  E-value: 8.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD-PQGNASTALGITDRQsgtPSSYEMLIGEVSLHTALRRSPHS 163
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKP---VTLHDVLAGEADIKDAIYEGPFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  164 ERLfcIPATIDLAGAeielvsMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGV 243
Cdd:TIGR01969  78 VKV--IPAGVSLEGL------RKADPDKLEDVLKEIID-DTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  244 SQLMRNIEMVKahlnpqLEVTTVILTMYdGRTKlADQVADEVRQYFGSKVLrTVIPRSVKVSEAPGYSMTIIDYDPGSRG 323
Cdd:TIGR01969 149 LKTKIVAEKLG------TAILGVVLNRV-TRDK-TELGREEIETILEVPVL-GVVPEDPEVRRAAAFGEPVVIYNPNSPA 219

                         250
                  ....*....|..
gi 627203010  324 AMSYLDASRELA 335
Cdd:TIGR01969 220 AQAFMELAAELA 231
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 77-330 2.51e-23

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 99.75  E-value: 2.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  77 PLQRPGRR-RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDRQSgtPSSYEMLIGEVSLHT 155
Cdd:PRK13869 113 PHRRGSEHlQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETD--VGANETLYAAIRYDD 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 156 ALR------RSPHSERLFCIPATIDLAGAE----IELVSMVARENRLRTALA-ALDNF--DFDYVFVDCPPSLGLLTINA 222
Cdd:PRK13869 191 TRRplrdviRPTYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLFFTRVAqAFDEVadDYDVVVIDCPPQLGFLTLSG 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 223 LVAAPEVMIPIQCEYYALEGVSQLM---RNIEMV--KAHLNPQLEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLRTV 297
Cdd:PRK13869 271 LCAATSMVITVHPQMLDIASMSQFLlmtRDLLGVvkEAGGNLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNP 350

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 627203010 298 IPRSVKVSEAPGYSMTIidYDPGSRG--------AMSYLDA 330
Cdd:PRK13869 351 MVKSAAVSDAGLTKQTL--YEIGRENltrstydrAMESLDA 389
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 43-123 6.36e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 38.32  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  43 NPTMNVSRETS--TEFDTPIGAAAERAMRVLhttheplqRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVID 120
Cdd:NF041417 297 EPTVDVAVITEeeTEETSPSETDKEAVMELL--------RPQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVT 368


                 ...
gi 627203010 121 LDP 123
Cdd:NF041417 369 TDP 371
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 85-337 5.94e-126

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 361.48  E-value: 5.94e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGItDRQSGTPSSYEMLIGEVSLHTALRRSpHSE 164
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGL-DPDDLDPTLYDLLLDDAPLEDAIVPT-EIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 RLFCIPATIDLAGAEIELVSMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLAD-DYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 245 QLMRNIEMVKAHLNPQLEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSRGA 324
Cdd:COG1192  159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGA 238

                        250
                 ....*....|...
gi 627203010 325 MSYLDASRELAER 337
Cdd:COG1192  239 KAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 85-263 1.16e-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: 243.26  E-value: 1.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGItDRQSGTPSSYEMLIGEVSLHTALRRSPHsE 164
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGI-DKNNVEKTIYELLIGECNIEEAIIKTVI-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  165 RLFCIPATIDLAGAEIELVSMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKD-NYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLS 158

                         170
                  ....*....|....*....
gi 627203010  245 QLMRNIEMVKAHLNPQLEV 263
Cdd:pfam13614 159 QLLNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 87-314 3.38e-59

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: 190.25  E-value: 3.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   87 LTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGI-TDRQSGTPSSYEMLIGEVSLHTALRRSPHSER 165
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLeGDIAPALQALAEGLKGRVNLDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  166 -LFCIPATIDLAGAEIELVSMvARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:pfam01656  81 gLDLIPGNIDLEKFEKELLGP-RKEERLREALEALKE-DYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAK 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 627203010  245 QLMRNIEMVKAHLNPQ-LEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLrTVIPRSVKVSEAPGYSMTI 314
Cdd:pfam01656 159 RLGGVIAALVGGYALLgLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVL-GVIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 85-286 5.88e-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: 158.09  E-value: 5.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALgitdrqsgtpssyemligevslhtalrrsphse 164
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 rlfcipatidlagaeielvsmvarenrlrtalaaldnfdFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:cd02042   48 ---------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLA 88

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 627203010 245 QLMRNIEMVKAHLNPQLEVTTVILTMYDGRTKLADQVADEVR 286
Cdd:cd02042   89 KLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
86-335 1.73e-28

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 109.56  E-value: 1.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  86 VLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNAStalgitdrqsgtpssyemligevslHTALRRSphSER 165
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL-------------------------DWAAARE--DER 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 166 LFCipatidlagaeielVSMVARENrLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVSQ 245
Cdd:NF041546  54 PFP--------------VVGLARPT-LHRELPSLAR-DYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASAD 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 246 LmrnIEMVKA--HLNPQLEVTTVIlTMYDGRTKLADQVADEVRQYfGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSrg 323
Cdd:NF041546 118 T---VDLIKEarEYTPGLKAAFVL-NRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG-- 190

                        250
                 ....*....|..
gi 627203010 324 amsylDASRELA 335
Cdd:NF041546 191 -----KAAREIR 197
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 100-341 4.77e-26

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: 103.82  E-value: 4.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 100 TTAVNIAAALAVQGLKTLVIDLDPQ-GNASTALGITDRqsgtPSSYEMLIGEVSLHTALRRSPHseRLFCIPATIDLAGA 178
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPK----ATLADVLAGEADLEDAIVQGPG--GLDVLPGGSGPAEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 179 EielvsMVARENRLRTALAALDNFdFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVSQLMRNIEMVKAhln 258
Cdd:COG0455   75 A-----ELDPEERLIRVLEELERF-YDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLG--- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 259 pqLEVTTVILTMYDGRT---KLADQVADEVRQYFGSKV-LRTVIPRSVKVSEAPGYSMTIIDYDPGSRGAMSYLDASREL 334
Cdd:COG0455  146 --VRRAGVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARL 223


                 ....*..
gi 627203010 335 AERDRPP 341
Cdd:COG0455  224 AGWPVPE 230
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 85-335 8.39e-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: 98.26  E-value: 8.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD-PQGNASTALGITDRQsgtPSSYEMLIGEVSLHTALRRSPHS 163
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKP---VTLHDVLAGEADIKDAIYEGPFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  164 ERLfcIPATIDLAGAeielvsMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGV 243
Cdd:TIGR01969  78 VKV--IPAGVSLEGL------RKADPDKLEDVLKEIID-DTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  244 SQLMRNIEMVKahlnpqLEVTTVILTMYdGRTKlADQVADEVRQYFGSKVLrTVIPRSVKVSEAPGYSMTIIDYDPGSRG 323
Cdd:TIGR01969 149 LKTKIVAEKLG------TAILGVVLNRV-TRDK-TELGREEIETILEVPVL-GVVPEDPEVRRAAAFGEPVVIYNPNSPA 219

                         250
                  ....*....|..
gi 627203010  324 AMSYLDASRELA 335
Cdd:TIGR01969 220 AQAFMELAAELA 231
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 81-307 9.37e-24

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: 100.44  E-value: 9.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   81 PGRRR-----VLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITdrqsgtpSSYEMLIGEvSLHT 155
Cdd:TIGR03453  96 PHRRGgehlqVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQ-------PEFDVGENE-TLYG 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  156 ALR----RSPHSE--------RLFCIPATIDLAGAEIELVSMVAREN--------RLRTALAALDNfDFDYVFVDCPPSL 215
Cdd:TIGR03453 168 AIRyddeRRPISEiirktyfpGLDLVPGNLELMEFEHETPRALSRGQggdtiffaRVGEALAEVED-DYDVVVIDCPPQL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  216 GLLTINALVAAPEVMIPIQ---------CEYyaLEGVSQLMRNIEmvKAHLNPQLEVTTVILTMYDGRTKLADQVADEVR 286
Cdd:TIGR03453 247 GFLTLSALCAATGVLITVHpqmldvmsmSQF--LLMTGDLLGVVR--EAGGNLSYDFMRYLVTRYEPNDGPQAQMVAFLR 322

                         250       260
                  ....*....|....*....|.
gi 627203010  287 QYFGSKVLRTVIPRSVKVSEA 307
Cdd:TIGR03453 323 SLFGDHVLTNPMLKSTAISDA 343
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 77-330 2.51e-23

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 99.75  E-value: 2.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  77 PLQRPGRR-RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDRQSgtPSSYEMLIGEVSLHT 155
Cdd:PRK13869 113 PHRRGSEHlQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETD--VGANETLYAAIRYDD 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 156 ALR------RSPHSERLFCIPATIDLAGAE----IELVSMVARENRLRTALA-ALDNF--DFDYVFVDCPPSLGLLTINA 222
Cdd:PRK13869 191 TRRplrdviRPTYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLFFTRVAqAFDEVadDYDVVVIDCPPQLGFLTLSG 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 223 LVAAPEVMIPIQCEYYALEGVSQLM---RNIEMV--KAHLNPQLEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLRTV 297
Cdd:PRK13869 271 LCAATSMVITVHPQMLDIASMSQFLlmtRDLLGVvkEAGGNLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNP 350

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 627203010 298 IPRSVKVSEAPGYSMTIidYDPGSRG--------AMSYLDA 330
Cdd:PRK13869 351 MVKSAAVSDAGLTKQTL--YEIGRENltrstydrAMESLDA 389
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 85-334 2.51e-21

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: 91.11  E-value: 2.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD-PQGNASTALGITDRQSGTPSsyEMLIGEVSLHTALRRSPHS 163
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIVYTLV--DVLEGECRLEQALIKDKRW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 164 ERLFCIPATIDLAGaeielvsMVARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEyyaLEGV 243
Cdd:cd02036   79 ENLYLLPASQTRDK-------DALTPEKLEELVKELKD-SFDFILIDSPAGIESGFINAIAPADEAIIVTNPE---ISSV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 244 SQLMRNIEMVKAHlnpQLEVTTVILTMYD-GRTKLADQVA-DEVRQYFGSKVLrTVIPRSVKVSEAPGYSMTIIDYDPGS 321
Cdd:cd02036  148 RDADRVIGLLESK---GIVNIGLIVNRYRpEMVKSGDMLSvEDIQEILGIPLL-GVIPEDPEVIVATNRGEPLVLYKPNS 223

                        250
                 ....*....|...
gi 627203010 322 RGAMSYLDASREL 334
Cdd:cd02036  224 LAAKAFENIARRL 236
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 37-347 5.97e-19

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: 86.71  E-value: 5.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  37 TPEAAHNPTMNVSRETSTEFDTPIGAAAERAMRVLHTTHEPLQRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQ-GLK 115
Cdd:COG4963   55 LSAPTPNLILLEALSESAALLADVLPLSPDELRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALAREsGRR 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 116 TLVIDLDPQ-GNASTALGITDRQsgtpSSYEML-----IGEVSLHTALrrSPHSERLFCIPATIDLagAEIELVSmvarE 189
Cdd:COG4963  135 VLLVDLDLQfGDVALYLDLEPRR----GLADALrnpdrLDETLLDRAL--TRHSSGLSVLAAPADL--ERAEEVS----P 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 190 NRLRTALAALDNFdFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVSQLMRNIEMvkahLNPQLEVTTVILT 269
Cdd:COG4963  203 EAVERLLDLLRRH-FDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRE----LGLPDDKVRLVLN 277

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 627203010 270 MYDGRTKLAdqvADEVRQYFGSKVLrTVIPRSVK-VSEAPGYSMTIIDYDPGSRGAMSYLDASRELAERDRPPSAKGRP 347
Cdd:COG4963  278 RVPKRGEIS---AKDIEEALGLPVA-AVLPNDPKaVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKAGG 352
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 60-229 6.85e-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: 6.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  60 IGAAAERAMRVLHTTHEPLQRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQG-NASTALGITDRqs 138
Cdd:COG0489   68 GLLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGpSLHRMLGLENR-- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 139 gtPSSYEMLIGEVSLHTALRRSPHsERLFCIPATiDLAGAEIELVSMvareNRLRTALAALDNfDFDYVFVDCPPslGLL 218
Cdd:COG0489  146 --PGLSDVLAGEASLEDVIQPTEV-EGLDVLPAG-PLPPNPSELLAS----KRLKQLLEELRG-RYDYVIIDTPP--GLG 214

                        170
                 ....*....|.
gi 627203010 219 TINALVAAPEV 229
Cdd:COG0489  215 VADATLLASLV 225
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 85-307 2.51e-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: 76.84  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD-PQGNASTALGITDRQsgtpSSYEMLIGEVSLHTALRRSPhs 163
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPKK----TLGDVLKGRVSLEDIIVEGP-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 164 ERLFCIPATIDLAG-AEIELVSMvareNRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEG 242
Cdd:cd02038   75 EGLDIIPGGSGMEElANLDPEQK----AKLIEELSSLES-NYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITD 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 627203010 243 VSQLMRNIEMVKAHLNPQLEVTTViLTMYDGRtKLADQVADEVRQYFGSKV-LRTVIPRSVKVSEA 307
Cdd:cd02038  150 AYALIKVLSRRGGKKNFRLIVNMA-RSPKEGR-ATFERLKKVAKRFLDINLdFVGFIPYDQSVRRA 213
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 67-227 4.12e-16

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


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 75.30  E-value: 4.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  67 AMRVLHTTHEPLQRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDP-QGNASTALGITDRQSGTpssyE 145
Cdd:cd05387    2 AFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNEPGLS----E 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 146 MLIGEVSLHTALRRSPhSERLFCIPA-TIDLAGAeiELVSmvarENRLRTALAALDNfDFDYVFVDCPPSLGLltINALV 224
Cdd:cd05387   78 VLSGQASLEDVIQSTN-IPNLDVLPAgTVPPNPS--ELLS----SPRFAELLEELKE-QYDYVIIDTPPVLAV--ADALI 147


                 ...
gi 627203010 225 AAP 227
Cdd:cd05387  148 LAP 150
PHA02518 PHA02518
ParA-like protein; Provisional
 85-337 4.25e-16

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 76.04  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTAlgITDRQSGTPssyemLIGEVSLHTALRRSPHSE 164
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW--AEAREEGEP-----LIPVVRMGKSIRADLPKV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 RLfcipatidlagaeielvsmvarenrlrtalaaldnfDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVS 244
Cdd:PHA02518  74 AS------------------------------------GYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAP 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 245 QLMRNIEMVKAhLNPQLEVTTVILTMYDGRTKLADQVADEVrQYFGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSRGA 324
Cdd:PHA02518 118 DLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYREARKAL-AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAA 195

                        250
                 ....*....|...
gi 627203010 325 MSYLDASRELAER 337
Cdd:PHA02518 196 EEIIQLVKELFRG 208
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 77-298 6.59e-15

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 75.05  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  77 PLQRPGRRR--VLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVID-LDPQGNASTalgitdrqsgtpssYEMLIGEVSL 153
Cdd:PHA02519  97 PNQRPDDKNpvVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASM--------------YHGYVPDLHI 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 154 HTALRRSPH--SER--------------LFCIPATIDLAGAEIELVSMVAREN-------RLRTALAAL-DNFDFdyVFV 209
Cdd:PHA02519 163 HADDTLLPFylGERdnaeyaikptcwpgLDIIPSCLALHRIETDLMQYHDAGKlphpphlMLRAAIESVwDNYDI--IVI 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 210 DCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVSQ---LMRNIeMVKAHLNPQLEVTTVILTMYDGRTKLADQ-VADEV 285
Cdd:PHA02519 241 DSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQfftMLLDL-LATVDLGGFEPVVRLLLTKYSLTVGNQSRwMEEQI 319

                        250
                 ....*....|...
gi 627203010 286 RQYFGSKVLRTVI 298
Cdd:PHA02519 320 RNTWGSMVLRQVV 332
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 86-298 6.90e-15

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 75.01  E-value: 6.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  86 VLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVID-LDPQGNASTALG-ITD---RQSGTPSSYEMliGEVSLHTALRRS 160
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGwVPDlhiHAEDTLLPFYL--GEKDDATYAIKP 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 161 PHSERLFCIPATIDLAGAEIELVSM-------VARENRLRTALAALDNfDFDYVFVDCPPSLGLLTINALVAAPEVMIPI 233
Cdd:PRK13705 186 TCWPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAH-DYDVIVIDSAPNLGIGTINVVCAADVLIVPT 264

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 627203010 234 QCEYYALEGVSQ-------LMRNIEMvkAHLNPQLEvttVILTMYDGRTKLADQ-VADEVRQYFGSKVLRTVI 298
Cdd:PRK13705 265 PAELFDYTSALQffdmlrdLLKNVDL--KGFEPDVR---ILLTKYSNSNGSQSPwMEEQIRDAWGSMVLKNVV 332
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 85-231 2.16e-14

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: 71.99  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDpQG--NASTALGITDRQSGTpsSYEMLIGEVSLHTALRRSPH 162
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-IGlrNLDLLLGLENRIVYT--LVDVVEGECRLQQALIKDKR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 627203010  163 SERLFCIPAtidlagAEIELVSMVARENRLRTALAALDnfDFDYVFVDCPPSLGLLTINALVAAPEVMI 231
Cdd:TIGR01968  79 LKNLYLLPA------SQTRDKDAVTPEQMKKLVNELKE--EFDYVIIDCPAGIESGFRNAVAPADEAIV 139
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 86-324 1.16e-13

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: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   86 VLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGI-TDRQSGTpsSYEMLIGEvSLHTALRRSPHSE 164
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMdWSVRDGW--ARALLNGA-DWAAAAYRSPDGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  165 RLfcIP-ATIDLAGAEIelvSMVARENRLRTALAALDNFDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEyyaLEGV 243
Cdd:TIGR03371  80 LF--LPyGDLSADEREA---YQAHDAGWLARLLQQLDLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNAD---AACY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  244 SQLMRNIEMVKAHLNPQLEVTTVIlTMYDGRTKLADQVADEVRQYFGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSRG 323
Cdd:TIGR03371 152 ATLHQLALALFAGSGPRDGPRFLI-NQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQA 230


                  .
gi 627203010  324 A 324
Cdd:TIGR03371 231 A 231
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 85-212 3.06e-13

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 68.55  E-value: 3.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDpQG--NASTALGITDRqsgtpssyemlI---------GEVSL 153
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD-IGlrNLDLVMGLENR-----------IvydlvdvieGECRL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 627203010 154 HTALRRSPHSERLFCIPA--TIDLAGAEIELVSMVAREnrLRTalaaldnfDFDYVFVDCP 212
Cdd:COG2894   71 KQALIKDKRFENLYLLPAsqTRDKDALTPEQMKKLVEE--LKE--------EFDYILIDSP 121
PRK10818 PRK10818
septum site-determining protein MinD;
85-340 5.28e-13

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 68.04  E-value: 5.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD-PQGNASTALGITDRQsgTPSSYEMLIGEVSLHTALRRSPHS 163
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRV--VYDFVNVIQGDATLNQALIKDKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 164 ERLFCIPATidlagaEIELVSMVARENrLRTALAALDNFDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGV 243
Cdd:PRK10818  81 ENLYILPAS------QTRDKDALTREG-VAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 244 SQLM-----------RNIEMVKAHLnpqlevttvILTMYD-GRTKLADQVADEVRQYFGSKVLRTVIPRSVKVSEAPGYS 311
Cdd:PRK10818 154 DRILgilasksrraeNGEEPIKEHL---------LLTRYNpGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQG 224

                        250       260
                 ....*....|....*....|....*....
gi 627203010 312 MTIIdYDPGSRGAMSYLDASRELAERDRP 340
Cdd:PRK10818 225 EPVI-LDIEADAGKAYADTVDRLLGEERP 252
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 85-225 4.09e-12

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 64.38  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGnaSTALGITDRQSGTPSSYEMLIGEVSLHTALrRSPHSE 164
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRN--SVMSGTFKSQNKITGLTNFLSGTTDLSDAI-CDTNIE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 627203010  165 RLFCIPatidlAGAEIELVSMVARENRLRTALAALDNFdFDYVFVDCPPsLGLLTINALVA 225
Cdd:TIGR01007  95 NLDVIT-----AGPVPPNPTELLQSSNFKTLIETLRKR-FDYIIIDTPP-IGTVTDAAIIA 148
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 85-251 7.60e-12

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 64.22  E-value: 7.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQ-GLKTLVIDLD-PQGNASTALGITDRQS-----GTPSSyemlIGEVSLHTAL 157
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDlPFGDLGLYLNLRPDYDladviQNLDR----LDRTLLDSAV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 158 RRspHSERLFCIPATIDLAGAEIelvsmvARENRLRTALAALDNFdFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEY 237
Cdd:cd03111   77 TR--HSSGLSLLPAPQELEDLEA------LGAEQVDKLLQVLRAF-YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDL 147

                        170
                 ....*....|....
gi 627203010 238 YALEGVSQLMRNIE 251
Cdd:cd03111  148 PSLRNARRLLDSLR 161
minD CHL00175
septum-site determining protein; Validated
 85-231 1.22e-11

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 64.41  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD-PQGNASTALGITDRQSGTpsSYEMLIGEVSLHTALRRSPHS 163
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRVLYT--AMDVLEGECRLDQALIRDKRW 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 627203010 164 ERLFCIPAtidlagAEIELVSMVARENrLRTALAALDNFDFDYVFVDCPPSLGLLTINALVAAPEVMI 231
Cdd:CHL00175  94 KNLSLLAI------SKNRQRYNVTRKN-MNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 93-232 1.21e-10

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: 60.98  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGI----TDRQSGTPSSYEMligEVSLHTALRRspHSERLFc 168
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQklggETPVKGAPNLWAM---EIDPEEALEE--YWEEVK- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 169 ipATIDLAGAEIELVSMVARENrlrTAL------AALDNF-------DFDYVFVDCPP---SLGLLT-----INALVAAP 227
Cdd:cd02035   82 --ELLAQYLRLPGLDEVYAEEL---LSLpgmdeaAAFDELreyvesgEYDVIVFDTAPtghTLRLLSlpleqVRELLRDP 156

                        170
                 ....*....|.
gi 627203010 228 E------VMIP 232
Cdd:cd02035  157 ErttfvlVTIP 167
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 93-347 2.02e-10

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 60.46  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNasTALGITDRQsGTPSSYEMLIGEVSLHTALRRSPHSER---LFCI 169
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHD--STLLLTGGK-VPPTIDEMLTEDGTAEELRREDLLFSGfngVDCV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 170 -----PATIDLAGAEIELVSMVARENRLRtalaaldNFDFDYVFVDCppsLGLLTINALVA------APEVMIPIQCEYY 238
Cdd:cd02117   85 eaggpEPGVGCGGRGIGTMLELLEEHGLL-------DDDYDVVIFDV---LGDVVCGGFAAplrrgfAQKVVIVVSEELM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 239 ALEGVSQLMRnieMVKAHLNPQLEVTTVILTMYD-GRTKLADQVADEVrqyfGSKVLrTVIPRSVKVSEAPGYSMTIIDY 317
Cdd:cd02117  155 SLYAANNIVK---AVENYSKNGVRLAGLVANLRDpAGTEEIQAFAAAV----GTKIL-AVIPRDPAVRRAELARVTVFEH 226

                        250       260       270
                 ....*....|....*....|....*....|
gi 627203010 318 DPGSRGAMSYLDASRELAERdRPPSAKGRP 347
Cdd:cd02117  227 DPVSPAASEFARLAAKIADA-VPPVPGPRP 255
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 84-213 4.64e-10

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 59.00  E-value: 4.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   84 RRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQG-NASTALGITDRQsgtpssyemligevslhtalrrsPH 162
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGpSIPRMLGLEGER-----------------------PE 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 627203010  163 SERLFCIPATIDlagaEIELVSM---VARENrlrTAL--------AALDNF-------DFDYVFVDCPP 213
Cdd:pfam10609  60 QSDGGIIPVEAH----GIKVMSIgflLPDED---DAViwrgpmksGAIKQFltdvdwgELDYLIIDLPP 121
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
93-340 7.36e-10

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 58.99  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNaSTALGITDRQSGTpssyemligevSLHTALRRSPHSER------- 165
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD-STRLLLGGKLQPT-----------VLDTAREKGYVEDVevedvvy 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  166 -----LFCI-----PATIDLAG-AEIELVSMVARenrlrtaLAALDnfDFDYVFVDCppsLGLLTINALVA------APE 228
Cdd:pfam00142  76 kgyggVKCVesggpEPGVGCAGrGVITAINLLEE-------LGAYD--DLDFVLYDV---LGDVVCGGFAMpiregkAQE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  229 VMIPIQCEYYALEGVSQLMRNIEMvKAHLNPqLEVTTVILT--MYDGRTKLADQVADEVrqyfGSKVLRtVIPRSVKVSE 306
Cdd:pfam00142 144 IYIVTSNEMMALYAANNIAKGIQK-YAKSGG-VRLGGIICNsrKVDDERELIDAFAEEL----GTQVLH-FVPRDNIVRK 216

                         250       260       270
                  ....*....|....*....|....*....|....
gi 627203010  307 APGYSMTIIDYDPGSRGAMSYLDASRELAERDRP 340
Cdd:pfam00142 217 AELRKQTVIEYAPDSEQAQEYRELARKILENPKG 250
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
93-230 1.15e-09

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 58.68  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDRQSGTPSSYEMLIG-EVSLHTALRRspHSERLFCIPA 171
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVAVPNLYAlEIDPEAELEE--YWERVRAPLR 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 172 TI-----------DLAGAEiELVSMvareNRLRtalAALDNFDFDYVFVDCPPSLGLLtinALVAAPEVM 230
Cdd:COG0003   89 GLlpsagvdelaeSLPGTE-ELAAL----DELL---ELLEEGEYDVIVVDTAPTGHTL---RLLSLPELL 147
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 93-337 4.34e-09

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: 56.37  E-value: 4.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDRQSGTPSSYEMLIGEVSLHTALRRSPHSerLFCIPAt 172
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIPTVLDTLREKGEVEELEDVIKEGFNG--IKCVES- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 173 idlAGAE----------IELVSMVARenrlrtaLAALDnFDFDYVFVDCppsLGlltinALV----AAP-------EVMI 231
Cdd:cd02040   85 ---GGPEpgvgcagrgiITAINLLEE-------LGAYE-EDLDVVFYDV---LG-----DVVcggfAMPiregyadEVYI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 232 PIQCEYYALEGVSQLMRNIEMvkahLNPQLEVTT--VILTM--YDGRTKLADQVADEVrqyfGSKVLRTViPRSVKVSEA 307
Cdd:cd02040  146 VTSGEMMALYAANNIAKGIVK----YAERGGVRLggLICNSrnVDREEELVEEFAERL----GTQIIHFV-PRSNEVQEA 216

                        250       260       270
                 ....*....|....*....|....*....|
gi 627203010 308 PGYSMTIIDYDPGSRGAMSYldasRELAER 337
Cdd:cd02040  217 ELRGKTVIEYDPDSEQADEY----RELAKK 242
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 85-122 9.72e-09

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 54.81  E-value: 9.72e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD 122
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 85-122 4.28e-08

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 50.51  E-value: 4.28e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLD 122
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 93-135 6.05e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 52.86  E-value: 6.05e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITD 135
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEV 50
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 93-336 9.60e-08

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 52.47  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALG------ITD--RQSGTPSsyeMLIGEVsLHTALrrsphsE 164
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVgekiptVLDvlREKGIDN---LGLEDI-IYEGF------N 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 RLFCIPA-----TIDLAG-AEIELVSMVARenrlrtaLAALDNFDFDYVFVD------C-----PPSLGLltinalvaAP 227
Cdd:PRK13230  79 GIYCVESggpepGYGCAGrGVITAIDLLKK-------LGVFEELGPDVVIYDilgdvvCggfamPLQKGL--------AD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 228 EVMIPIQCEYYALEGVSQLMRNIEMVKAHLNPQLevTTVIltmYDGRTKL-ADQVADEVRQYFGSKVLRTvIPRSVKVSE 306
Cdd:PRK13230 144 DVYIVTTCDPMAIYAANNICKGIKRFAKRGKSAL--GGII---YNGRSVIdAPDIVEEFAKKIGTNVIGK-IPMSNIITE 217

                        250       260       270
                 ....*....|....*....|....*....|
gi 627203010 307 APGYSMTIIDYDPGSRGAMSYldasRELAE 336
Cdd:PRK13230 218 AEIYGKTVIEYAPDSEISNIF----RELAE 243
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 85-233 2.03e-07

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: 51.69  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQgNASTALGITDRqSGTPSSYEMligEVSLHTALRRSPHSE 164
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFHRYFENR-SATADRTGL---SLPTPEHLNLPDNDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 627203010  165 RLFCIPATIDLAGAEiELVSMVAREnrlrtalaaldnfdFDYVFVDCPPSLGLLTINALVAAPEVMIPI 233
Cdd:pfam09140  76 AEVPDGENIDDARLE-EAFADLEAR--------------CDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
82-146 6.98e-07

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 50.43  E-value: 6.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 627203010  82 GRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQG-NASTALGITDRQSGTPSSYEM 146
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGpSIPTMLGAEDQRPTSPDGTHM 170
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 93-230 8.05e-07

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 50.04  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010   93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGItdRQSGTPssyemligevslhTALrrsphSERLFCIpaT 172
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQ--KFGHEP-------------TKV-----KENLSAM--E 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  173 IDLAGAEIELVSMVAR-ENRLRTA-------------------LAALDNF-------DFDYVFVDCPP---SLGLLTIna 222
Cdd:pfam02374  67 IDPNMELEEYWQEVQKyMNALLGLrmlegilaeelaslpgideAASFDEFkkymdegEYDVVVFDTAPtghTLRLLSL-- 144


                  ....*...
gi 627203010  223 lvaaPEVM 230
Cdd:pfam02374 145 ----PTVL 148
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 85-271 1.06e-05

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


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 45.99  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  85 RVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDRQsgTPSSYEMLIGE------VSLHTALR 158
Cdd:cd17869    4 SVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRY--LMSDHLYTLKSrkanlaDKLESCVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 159 RspHSERLFCIPATiDLAGAEIELvsMVARENRLRTALAALDNfdFDYVFVDCPPSLGLLTINALVAAPEVMIPIqceyy 238
Cdd:cd17869   82 Q--HESGVYYFSPF-KSALDILEI--KKDDILHMITKLVEAHA--YDYIIMDLSFEFSSTVCKLLQASHNNVVIA----- 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 627203010 239 aLEGVSQLMRNIEMVKAHLNPQLEVTTVILTMY 271
Cdd:cd17869  150 -LQDANSSYKLNKFLRALEDLFQENFSYIYNKY 181
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 93-124 4.10e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.57  E-value: 4.10e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQ 124
Cdd:PRK13185  10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 93-124 6.02e-05

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 44.21  E-value: 6.02e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQ 124
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPK 39
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 93-133 1.17e-04

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 43.07  E-value: 1.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGI 133
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGV 48
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 93-126 1.61e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 43.54  E-value: 1.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 627203010   93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGN 126
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 93-123 3.11e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 42.38  E-value: 3.11e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 627203010   93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDP 123
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP 359
chlL CHL00072
photochlorophyllide reductase subunit L
 93-131 3.65e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 41.65  E-value: 3.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 627203010  93 KGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTAL 131
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTL 46
PRK09841 PRK09841
tyrosine-protein kinase;
57-258 8.87e-04

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 41.05  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  57 DTPIGAAAErAMRVLHTTHEPLQRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDR 136
Cdd:PRK09841 505 DNPADSAVE-AVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSN 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 137 QSGTPssyEMLIGEVSLHTALRRSPHS--ERLFCIPatidLAGAEIELVSmvarENRLRtALAALDNFDFDYVFVDCPPS 214
Cdd:PRK09841 584 EHGLS---EYLAGKDELNKVIQHFGKGgfDVITRGQ----VPPNPSELLM----RDRMR-QLLEWANDHYDLVIVDTPPM 651

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 627203010 215 LGLltINALVAAPEVMIPIQCEYYALEGVSQL---MRNIEMVKAHLN 258
Cdd:PRK09841 652 LAV--SDAAVVGRSVGTSLLVARFGLNTAKEVslsMQRLEQAGVNIK 696
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 93-336 2.72e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 39.01  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  93 KGGVGKTTTAVNIAAALAvQGLKTLVIDLDPQGNASTAL------GITD--RQSGTPSSYEMligevsLHTALRRSPHSE 164
Cdd:PRK13231  10 KGGIGKSTTVSNMAAAYS-NDHRVLVIGCDPKADTTRTLcgkripTVLDtlKDNRKPELEDI------IHEGFNGILCVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 165 RLFCIPAtIDLAGAEIeLVSMVARENrlrtaLAALDNfDFDYVFVDCppsLGLLTINALVA------APEVMIPIQCEYY 238
Cdd:PRK13231  83 SGGPEPG-VGCAGRGV-IVAMNLLEN-----LGVFDE-DIDVVIYDV---LGDVVCGGFSVplredyADEVYIVTSGEYM 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010 239 ALEGVSQLMRNIEMVKAHLNpqlevtTVILTMYDGRTKLadQVADEVRQYFGSKVLrTVIPRSVKVSEAPGYSMTIIDYD 318
Cdd:PRK13231 152 SLYAANNIARGIKKLKGKLG------GIICNCRGIDNEV--EIVSEFASRIGSRII-GVIPRSNLVQESELDAKTVVETF 222

                        250
                 ....*....|....*...
gi 627203010 319 PGSRGAMSYldasRELAE 336
Cdd:PRK13231 223 PESEQASVY----RKLAN 236
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 43-123 6.36e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 38.32  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627203010  43 NPTMNVSRETS--TEFDTPIGAAAERAMRVLhttheplqRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVID 120
Cdd:NF041417 297 EPTVDVAVITEeeTEETSPSETDKEAVMELL--------RPQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVT 368


                 ...
gi 627203010 121 LDP 123
Cdd:NF041417 369 TDP 371
 
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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