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Conserved domains on  [gi|849138834|ref|WP_047997795|]
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plasmid partitioning protein RepA [Puniceibacterium sp. IMCC21224]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
partition_RepA super family cl30270
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 9-394 0e+00

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]


The actual alignment was detected with superfamily member TIGR03453:

Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 551.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834    9 DQKIQTMATRLSKSLDVNMRKSFLPDERKSLRRFSSTEVAQILGVSQDFLRKMFFEDKLDlgEIETDARGRRFYTAEQID 88
Cdd:TIGR03453   1 DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGP--EPETLSNGRRSYTLEQIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834   89 IARHEIARSSTKFQHIVPRRRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEID 168
Cdd:TIGR03453  79 ELRRHLAQRGREARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  169 FPEAGTVYDALRYED-PIPFRDVVRKTYFHNLDLAAAGLLLSEFETETAHAL--RNNIRPPFYQRLALCINEVETDYDIV 245
Cdd:TIGR03453 159 VGENETLYGAIRYDDeRRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRALsrGQGGDTIFFARVGEALAEVEDDYDVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  246 VIDCPPQLGFTTLSALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDWDFMRFLITRFEPNDGPQTQMA 325
Cdd:TIGR03453 239 VIDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMV 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849138834  326 AFLRTMFTDDVLTQPFLKSSAVSDAGLTQQTLFEIARTDFHRQTYDRAIESINGVVAEVEGLIKTAWGR 394
Cdd:TIGR03453 319 AFLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR 387
 
Name Accession Description Interval E-value
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 9-394 0e+00

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: 551.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834    9 DQKIQTMATRLSKSLDVNMRKSFLPDERKSLRRFSSTEVAQILGVSQDFLRKMFFEDKLDlgEIETDARGRRFYTAEQID 88
Cdd:TIGR03453   1 DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGP--EPETLSNGRRSYTLEQIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834   89 IARHEIARSSTKFQHIVPRRRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEID 168
Cdd:TIGR03453  79 ELRRHLAQRGREARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  169 FPEAGTVYDALRYED-PIPFRDVVRKTYFHNLDLAAAGLLLSEFETETAHAL--RNNIRPPFYQRLALCINEVETDYDIV 245
Cdd:TIGR03453 159 VGENETLYGAIRYDDeRRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRALsrGQGGDTIFFARVGEALAEVEDDYDVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  246 VIDCPPQLGFTTLSALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDWDFMRFLITRFEPNDGPQTQMA 325
Cdd:TIGR03453 239 VIDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMV 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849138834  326 AFLRTMFTDDVLTQPFLKSSAVSDAGLTQQTLFEIARTDFHRQTYDRAIESINGVVAEVEGLIKTAWGR 394
Cdd:TIGR03453 319 AFLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR 387
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-394 1.10e-143

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 414.46  E-value: 1.10e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834   5 RIRMDQKIQTMATRLSKSLDVNMRKSFLPDERKSLRRFSSTEVAQILGVSQDFLRKMFFEdkldlGE---IETDARGRRF 81
Cdd:PRK13869  12 RPSVDVTIGEHAEQLSSQLQAMSEALFPPTSHKSLRKFTSGEAARLMKISDSTLRKMTLA-----GEgpqPELASNGRRF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  82 YTAEQIDIARHEIARSSTKFQHI--VPRRRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTT 159
Cdd:PRK13869  87 YTLGQINEIRQMLAGSTRGRESIdfVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 160 MFGFRPEIDFPEAGTVYDALRYEDPI-PFRDVVRKTYFHNLDLAAAGLLLSEFETETAHAL--RNNIRPPFYQRLALCIN 236
Cdd:PRK13869 167 LLGVLPETDVGANETLYAAIRYDDTRrPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALsdKGTRDGLFFTRVAQAFD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 237 EVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDWDFMRFLITRFEP 316
Cdd:PRK13869 247 EVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFIRYLLTRYEP 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 849138834 317 NDGPQTQMAAFLRTMFTDDVLTQPFLKSSAVSDAGLTQQTLFEIARTDFHRQTYDRAIESINGVVAEVEGLIKTAWGR 394
Cdd:PRK13869 327 QDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEALIKMAWGR 404
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 115-377 9.50e-68

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: 214.72  E-value: 9.50e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEidfPEAGTVYDALRyeDPIPFRDVVRKT 194
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD---DLDPTLYDLLL--DDAPLEDAIVPT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 195 YFHNLDLAAAGLLLSEFETETAHalrnniRPPFYQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPS 274
Cdd:COG1192   77 EIPGLDLIPANIDLAGAEIELVS------RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 275 MLDVASMAQFLQLTSSLMATIadvgaSPDWDFMRFLITRFEPNDGPQTQMAAFLRTMFTDDVLTQPFLKSSAVSDAGLTQ 354
Cdd:COG1192  151 YLSLEGLAQLLETIEEVREDL-----NPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAG 225

                        250       260
                 ....*....|....*....|...
gi 849138834 355 QTLFEIARTDFHRQTYDRAIESI 377
Cdd:COG1192  226 KPVFEYDPKSKGAKAYRALAEEL 248
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 117-357 7.19e-49

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: 165.21  E-value: 7.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  117 ISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEIDfPEAGTVYDALRYEDPI-PFRDVVRKTY 195
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIA-PALQALAEGLKGRVNLdPILLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  196 fHNLDLAAAGLLLSEFETETahalrnnIRPPFYQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:pfam01656  80 -GGLDLIPGNIDLEKFEKEL-------LGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  276 LDVASMAQFLQLTSSLMATIADVGAspdwDFMRFLITRFEPNDGPQTQMAAFLRTMFTDDVLtQPFLKSSAVSDAGLTQQ 355
Cdd:pfam01656 152 ILVEDAKRLGGVIAALVGGYALLGL----KIIGVVLNKVDGDNHGKLLKEALEELLRGLPVL-GVIPRDEAVAEAPARGL 226


                  ..
gi 849138834  356 TL 357
Cdd:pfam01656 227 PV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 116-329 1.01e-33

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: 122.26  E-value: 1.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFgfrpeidfpeagtvydalryedpipfrdvvrkty 195
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 196 fhnldlaaaglllsefetetahalrnnirppfyqrlalcinevetdYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:cd02042   48 ----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSP 81

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 849138834 276 LDVASMAQFLQLTSSLMATIadvgaSPDWDFMRFLITRFEPNDGPQTQMAAFLR 329
Cdd:cd02042   82 FDLDGLAKLLDTLEELKKQL-----NPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
116-287 1.18e-24

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 99.93  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEidfpeagtvydalryEDPIPFRDVVRkty 195
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARED---------------ERPFPVVGLAR--- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 196 fhnldlaaaglllsefetETAHALrnnirppfyqrlalcINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:NF041546  63 ------------------PTLHRE---------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSP 109

                        170
                 ....*....|..
gi 849138834 276 LDVASMAQFLQL 287
Cdd:NF041546 110 YDLWASADTVDL 121
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 68-162 4.64e-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: 39.09  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  68 DLGEIETDARGRRFYTAEQIDIARHEIARSSTKFQHIVPRRRDGEHIQIISIANfKGGAGKTTTAIHLAQKLALDGYRVL 147
Cdd:NF041417 287 DVGEVLYEGKEPTVDVAVITEEETEETSPSETDKEAVMELLRPQKDTRYLFFTG-KGGVGKSTIASTTATYLAEEGYETL 365

                         90
                 ....*....|....*
gi 849138834 148 AIDLDPQASMTTMFG 162
Cdd:NF041417 366 IVTTDPASHLQDIFG 380
 
Name Accession Description Interval E-value
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 9-394 0e+00

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: 551.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834    9 DQKIQTMATRLSKSLDVNMRKSFLPDERKSLRRFSSTEVAQILGVSQDFLRKMFFEDKLDlgEIETDARGRRFYTAEQID 88
Cdd:TIGR03453   1 DALIAAQARELSEQLQALRERLFPPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGP--EPETLSNGRRSYTLEQIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834   89 IARHEIARSSTKFQHIVPRRRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEID 168
Cdd:TIGR03453  79 ELRRHLAQRGREARRYLPHRRGGEHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  169 FPEAGTVYDALRYED-PIPFRDVVRKTYFHNLDLAAAGLLLSEFETETAHAL--RNNIRPPFYQRLALCINEVETDYDIV 245
Cdd:TIGR03453 159 VGENETLYGAIRYDDeRRPISEIIRKTYFPGLDLVPGNLELMEFEHETPRALsrGQGGDTIFFARVGEALAEVEDDYDVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  246 VIDCPPQLGFTTLSALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDWDFMRFLITRFEPNDGPQTQMA 325
Cdd:TIGR03453 239 VIDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSYDFMRYLVTRYEPNDGPQAQMV 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849138834  326 AFLRTMFTDDVLTQPFLKSSAVSDAGLTQQTLFEIARTDFHRQTYDRAIESINGVVAEVEGLIKTAWGR 394
Cdd:TIGR03453 319 AFLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEGLIKKAWGR 387
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-394 1.10e-143

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 414.46  E-value: 1.10e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834   5 RIRMDQKIQTMATRLSKSLDVNMRKSFLPDERKSLRRFSSTEVAQILGVSQDFLRKMFFEdkldlGE---IETDARGRRF 81
Cdd:PRK13869  12 RPSVDVTIGEHAEQLSSQLQAMSEALFPPTSHKSLRKFTSGEAARLMKISDSTLRKMTLA-----GEgpqPELASNGRRF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  82 YTAEQIDIARHEIARSSTKFQHI--VPRRRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTT 159
Cdd:PRK13869  87 YTLGQINEIRQMLAGSTRGRESIdfVPHRRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 160 MFGFRPEIDFPEAGTVYDALRYEDPI-PFRDVVRKTYFHNLDLAAAGLLLSEFETETAHAL--RNNIRPPFYQRLALCIN 236
Cdd:PRK13869 167 LLGVLPETDVGANETLYAAIRYDDTRrPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALsdKGTRDGLFFTRVAQAFD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 237 EVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDWDFMRFLITRFEP 316
Cdd:PRK13869 247 EVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFIRYLLTRYEP 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 849138834 317 NDGPQTQMAAFLRTMFTDDVLTQPFLKSSAVSDAGLTQQTLFEIARTDFHRQTYDRAIESINGVVAEVEGLIKTAWGR 394
Cdd:PRK13869 327 QDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEALIKMAWGR 404
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 115-377 9.50e-68

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: 214.72  E-value: 9.50e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEidfPEAGTVYDALRyeDPIPFRDVVRKT 194
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD---DLDPTLYDLLL--DDAPLEDAIVPT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 195 YFHNLDLAAAGLLLSEFETETAHalrnniRPPFYQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPS 274
Cdd:COG1192   77 EIPGLDLIPANIDLAGAEIELVS------RPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 275 MLDVASMAQFLQLTSSLMATIadvgaSPDWDFMRFLITRFEPNDGPQTQMAAFLRTMFTDDVLTQPFLKSSAVSDAGLTQ 354
Cdd:COG1192  151 YLSLEGLAQLLETIEEVREDL-----NPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAG 225

                        250       260
                 ....*....|....*....|...
gi 849138834 355 QTLFEIARTDFHRQTYDRAIESI 377
Cdd:COG1192  226 KPVFEYDPKSKGAKAYRALAEEL 248
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 117-357 7.19e-49

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: 165.21  E-value: 7.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  117 ISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEIDfPEAGTVYDALRYEDPI-PFRDVVRKTY 195
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIA-PALQALAEGLKGRVNLdPILLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  196 fHNLDLAAAGLLLSEFETETahalrnnIRPPFYQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:pfam01656  80 -GGLDLIPGNIDLEKFEKEL-------LGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  276 LDVASMAQFLQLTSSLMATIADVGAspdwDFMRFLITRFEPNDGPQTQMAAFLRTMFTDDVLtQPFLKSSAVSDAGLTQQ 355
Cdd:pfam01656 152 ILVEDAKRLGGVIAALVGGYALLGL----KIIGVVLNKVDGDNHGKLLKEALEELLRGLPVL-GVIPRDEAVAEAPARGL 226


                  ..
gi 849138834  356 TL 357
Cdd:pfam01656 227 PV 228
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 115-285 2.05e-36

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: 130.78  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFrpeIDFPEAGTVYDALRYEDPIpfRDVVRKT 194
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGI---DKNNVEKTIYELLIGECNI--EEAIIKT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  195 YFHNLDLAAAGLLLSEFETETAHALRNNIrppfyqRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPS 274
Cdd:pfam13614  77 VIENLDLIPSNIDLAGAEIELIGIENREN------ILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150

                         170
                  ....*....|.
gi 849138834  275 MLDVASMAQFL 285
Cdd:pfam13614 151 YYALEGLSQLL 161
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 33-392 3.57e-36

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 135.91  E-value: 3.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  33 PDERKSLRRFSSTEVAQILGVSQDFLRKMFFEDKLDLGEIETDAR--GRRFYTAEQIDIARHEIARSStkfqhivpRRRD 110
Cdd:PHA02519  31 PEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDFETRGRveRRAGYTIDQISHMRDHFGNPN--------QRPD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 111 GEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAID-LDPQASMTTMFGFRPEIDFPEAGTVydalryedpIPF-- 187
Cdd:PHA02519 103 DKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLHIHADDTL---------LPFyl 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 188 --RD----VVRKTYFHNLDLAAAGLLLSEFETETA--HALRNNIRPPfYQRLALCINEVETDYDIVVIDCPPQLGFTTLS 259
Cdd:PHA02519 174 geRDnaeyAIKPTCWPGLDIIPSCLALHRIETDLMqyHDAGKLPHPP-HLMLRAAIESVWDNYDIIVIDSAPNLGTGTIN 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 260 ALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDwdfMRFLITRFEPNDGPQTQ-MAAFLRTMFTDDVLT 338
Cdd:PHA02519 253 VVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPV---VRLLLTKYSLTVGNQSRwMEEQIRNTWGSMVLR 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 849138834 339 QPFLKSSAVSDAGLTQQTLFEIARtdFHRQT---YDRAIESINGVVAEV-EGLIKTAW 392
Cdd:PHA02519 330 QVVRVTDEVGKGQIKMRTVFEQAA--NQRSTlnaWRNAVAIWEPVCAEIfNDLIKPRW 385
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 33-392 9.32e-36

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 134.72  E-value: 9.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  33 PDERKSLRRFSSTEVAQILGVSQDFLRKmfFEDKLDLGEIETDARGR----RFYTAEQIDIARHEIARSstkfqhivPRR 108
Cdd:PRK13705  31 PEARKITRRWRIGEAADLVGVSSQAIRD--AEKAGRLPHPDMEMRGRveqrVGYTIEQINHMRDVFGTR--------LRR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 109 RDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAID-LDPQASMTTMFGFRPEIDFPEAGTVydalryedpIPF 187
Cdd:PRK13705 101 AEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHIHAEDTL---------LPF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 188 ----RD----VVRKTYFHNLDLAAAGLLLSEFETETaHALRNNIRPPF--YQRLALCINEVETDYDIVVIDCPPQLGFTT 257
Cdd:PRK13705 172 ylgeKDdatyAIKPTCWPGLDIIPSCLALHRIETEL-MGKFDEGKLPTdpHLMLRLAIETVAHDYDVIVIDSAPNLGIGT 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 258 LSALVASTSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVGASPDwdfMRFLITRFEPNDGPQTQ-MAAFLRTMFTDDV 336
Cdd:PRK13705 251 INVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPD---VRILLTKYSNSNGSQSPwMEEQIRDAWGSMV 327

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 337 LTQPFLKSSAVSDAGLTQQTLFEIARTdfHRQT---YDRAIESINGVVAEV-EGLIKTAW 392
Cdd:PRK13705 328 LKNVVRETDEVGKGQIRMRTVFEQAID--QRSStgaWRNALSIWEPVCNEIfDRLIKPRW 385
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 116-329 1.01e-33

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: 122.26  E-value: 1.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFgfrpeidfpeagtvydalryedpipfrdvvrkty 195
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 196 fhnldlaaaglllsefetetahalrnnirppfyqrlalcinevetdYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:cd02042   48 ----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSP 81

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 849138834 276 LDVASMAQFLQLTSSLMATIadvgaSPDWDFMRFLITRFEPNDGPQTQMAAFLR 329
Cdd:cd02042   82 FDLDGLAKLLDTLEELKKQL-----NPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
116-287 1.18e-24

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 99.93  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEidfpeagtvydalryEDPIPFRDVVRkty 195
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARED---------------ERPFPVVGLAR--- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 196 fhnldlaaaglllsefetETAHALrnnirppfyqrlalcINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:NF041546  63 ------------------PTLHRE---------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSP 109

                        170
                 ....*....|..
gi 849138834 276 LDVASMAQFLQL 287
Cdd:NF041546 110 YDLWASADTVDL 121
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 105-270 3.98e-15

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: 75.22  E-value: 3.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 105 VPRRRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDP-QASMTTMFGFRPEIdfpeagTVYDALRyeD 183
Cdd:COG0489   83 LLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGLENRP------GLSDVLA--G 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 184 PIPFRDVVRKTYFHNldlaaaglllsefetetAHALRNNIRPPFY------QRLALCINEVETDYDIVVIDCPPQLGFT- 256
Cdd:COG0489  155 EASLEDVIQPTEVEG-----------------LDVLPAGPLPPNPsellasKRLKQLLEELRGRYDYVIIDTPPGLGVAd 217

                        170
                 ....*....|....*
gi 849138834 257 -TLSALVASTSLVVT 270
Cdd:COG0489  218 aTLLASLVDGVLLVV 232
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 116-361 1.49e-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: 72.76  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEID-----FPEAGTVYDALRYEDP-----I 185
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRdgwarALLNGADWAAAAYRSPdgvlfL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  186 PFRDVvrktyfhnldlaaAGLLLSEFETETAHALRNNIrppfyQRLALcinEVEtdyDIVVIDCPPQLGFTTLSALvAST 265
Cdd:TIGR03371  83 PYGDL-------------SADEREAYQAHDAGWLARLL-----QQLDL---AAR---DWVLIDLPRGPSPITRQAL-AAA 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  266 SLVVTVIPSmlDVASMAQFLQLTSSLMATIADVGASpdwdfmRFLITRFEPNDGPQTQMAAFLRTMFTDDVLTQPFLKSS 345
Cdd:TIGR03371 138 DLVLVVVNA--DAACYATLHQLALALFAGSGPRDGP------RFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDE 209

                         250
                  ....*....|....*.
gi 849138834  346 AVSDAGLTQQTLFEIA 361
Cdd:TIGR03371 210 AVSEALARGTPVLNYA 225
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 115-285 4.29e-13

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: 67.98  E-value: 4.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD-PQASMTTMFGFRPEIdfpeagTVYDALRYEDPIpFRDVVRK 193
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPKK------TLGDVLKGRVSL-EDIIVEG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 194 TYfhnldLAAAGLLLSEFEtETAHaLRNNIRPPFYQRLalciNEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIP 273
Cdd:cd02038   74 PE-----GLDIIPGGSGME-ELAN-LDPEQKAKLIEEL----SSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTP 142

                        170
                 ....*....|....*
gi 849138834 274 ---SMLDVASMAQFL 285
Cdd:cd02038  143 eptSITDAYALIKVL 157
PHA02518 PHA02518
ParA-like protein; Provisional
 116-287 6.49e-13

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 67.18  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTtmfgfrpeiDFPEAgtvydalRYEDPiPFRDVVRkty 195
Cdd:PHA02518   2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST---------DWAEA-------REEGE-PLIPVVR--- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 196 fhnldlaaaglllsefetetahaLRNNIRPPfyqrlalcINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSM 275
Cdd:PHA02518  62 -----------------------MGKSIRAD--------LPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSP 110

                        170
                 ....*....|..
gi 849138834 276 LDVASMAQFLQL 287
Cdd:PHA02518 111 FDIWAAPDLVEL 122
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 116-275 5.94e-11

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: 62.44  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD-PQASMTTMFGFRpeiDFPEagTVYDALRYEDPIpfRDVVrkt 194
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGME---DKPV--TLHDVLAGEADI--KDAI--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  195 YFHNLDLAAAGLLLSefeteTAHALRNNIRppfyqRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPS 274
Cdd:TIGR01969  72 YEGPFGVKVIPAGVS-----LEGLRKADPD-----KLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE 141


                  .
gi 849138834  275 M 275
Cdd:TIGR01969 142 I 142
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 130-287 7.89e-11

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: 61.44  E-value: 7.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 130 TTAIHLAQKLALDGYRVLAIDLDPQ-ASMTTMFGFRPEidfpeaGTVYDALRyeDPIPFRDVVRKTyfhnldlaaagllL 208
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPK------ATLADVLA--GEADLEDAIVQG-------------P 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 209 SEFE---TETAHALRNNIRPpfYQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIPSMLDVASMAQFL 285
Cdd:COG0455   60 GGLDvlpGGSGPAELAELDP--EERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALL 137


                 ..
gi 849138834 286 QL 287
Cdd:COG0455  138 KL 139
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 115-326 8.83e-10

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: 59.74  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLA-LDGYRVLAIDLDPQA-SMTTMFGFRPEIDFPEAGTVYDALryeDPIPFRDVVR 192
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFgDVALYLDLEPRRGLADALRNPDRL---DETLLDRALT 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 193 KtyfhnldlaaaglllsefETETAHAL--------RNNIRPPFYQRLalcINEVETDYDIVVIDCPPQLGFTTLSALVAS 264
Cdd:COG4963  180 R------------------HSSGLSVLaapadlerAEEVSPEAVERL---LDLLRRHFDYVVVDLPRGLNPWTLAALEAA 238

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 849138834 265 TSLVVTVIPSMLDVASMAQFLQLTSSLMATIADVgaspdwdfmRFLITRFEPNDGPQTQMAA 326
Cdd:COG4963  239 DEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDKV---------RLVLNRVPKRGEISAKDIE 291
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 116-250 3.04e-09

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 57.46  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDP-QASMTTMFGFRPE------IDFPEAGTVYDALRYEDPIPfr 188
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSAtadrtgLSLPTPEHLNLPDNDVAEVP-- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 849138834  189 dvvrktyfhnldlaaaglllsefETETahalrnnirpPFYQRLALCINEVETDYDIVVIDCP 250
Cdd:pfam09140  80 -----------------------DGEN----------IDDARLEEAFADLEARCDFIVIDTP 108
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 115-152 5.71e-09

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: 53.20  E-value: 5.71e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD 152
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 123-171 1.17e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 55.17  E-value: 1.17e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEIDFPE 171
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLIK 56
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 111-269 2.14e-08

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: 53.73  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 111 GEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDP-QASMTTMFGFRPEidfpeaGTVYDALRyeDPIPFRD 189
Cdd:cd05387   16 DAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNE------PGLSEVLS--GQASLED 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 190 VVRKTyfhnldlaaaglllsefETETAHALRNNIRPPF------YQRLALCINEVETDYDIVVIDCPPQLGFTT---LSA 260
Cdd:cd05387   88 VIQST-----------------NIPNLDVLPAGTVPPNpsellsSPRFAELLEELKEQYDYVIIDTPPVLAVADaliLAP 150


                 ....*....
gi 849138834 261 LVASTSLVV 269
Cdd:cd05387  151 LVDGVLLVV 159
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 116-273 1.98e-07

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


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 51.43  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD-PQASMTTMFGFRPEIDFpeagTVYDALryEDPIPFRDVVRKT 194
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIVY----TLVDVL--EGECRLEQALIKD 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849138834 195 YFHNLDLAAAGLLLSEfetetahalRNNIRPpfyQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVIP 273
Cdd:cd02036   76 KRWENLYLLPASQTRD---------KDALTP---EKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNP 142
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 115-291 6.14e-07

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: 49.97  E-value: 6.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLA-LDGYRVLAIDLD-PQASMTTMFGFRPEIDFPEAGTVYDALryeDPIPFRDVVR 192
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDlPFGDLGLYLNLRPDYDLADVIQNLDRL---DRTLLDSAVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 193 KTyfhnldlaaaglllsefeTETAHALrnnirpPFYQRLaLCINEVETD------------YDIVVIDCPPQLGFTTLSA 260
Cdd:cd03111   78 RH------------------SSGLSLL------PAPQEL-EDLEALGAEqvdkllqvlrafYDHIIVDLGHFLDEVTLAV 132

                        170       180       190
                 ....*....|....*....|....*....|.
gi 849138834 261 LVASTSLVVTVIPsmlDVASMAQFLQLTSSL 291
Cdd:cd03111  133 LEAADEILLVTQQ---DLPSLRNARRLLDSL 160
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 117-178 2.63e-06

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: 48.46  E-value: 2.63e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 849138834 117 ISIANfKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEIDfPEAGTVYDA 178
Cdd:cd02034    3 IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKL-PLIKTIGDI 62
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 116-162 3.48e-06

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


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 47.50  E-value: 3.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD---PqaSMTTMFG 162
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADiygP--SIPRLLG 49
HTH_MlrA-like_sg1 cd04764
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ...
 42-106 4.13e-06

Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 1). The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins.


Pssm-ID: 133392  Cd Length: 67  Bit Score: 43.86  E-value: 4.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  42 FSSTEVAQILGVSQDFLRkmFFEDKLDLgEIETDARGRRFYTAEQIDIARH-----EIARSSTKFQHIVP 106
Cdd:cd04764    1 YTIKEVSEIIGVKPHTLR--YYEKEFNL-YIPRTENGRRYYTDEDIELLKKiktllEKGLSIKEIKEILN 67
MerR_1 pfam13411
MerR HTH family regulatory protein;
42-91 5.64e-06

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 43.70  E-value: 5.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 849138834   42 FSSTEVAQILGVSQDFLRkmFFEDKLDLGeIETDARGRRFYTAEQIDIAR 91
Cdd:pfam13411   1 YTISELARLLGVTPRTLR--YWEREGLLP-PPRTERGRRYYTDEDVERLR 47
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 116-337 6.01e-06

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: 47.33  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDpqasmttmFGFRpEIDFP---EAGTVYDALryedpipfrDVVr 192
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD--------IGLR-NLDLLlglENRIVYTLV---------DVV- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  193 ktyfhNLDLAAAGLLLSEFETETAHAL-------RNNIRPPFYQRLalcINEVETDYDIVVIDCPP--QLGFTTlSALVA 263
Cdd:TIGR01968  64 -----EGECRLQQALIKDKRLKNLYLLpasqtrdKDAVTPEQMKKL---VNELKEEFDYVIIDCPAgiESGFRN-AVAPA 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 849138834  264 STSLVVTV--IPSMLDVASMAQFLQLTSslmatIADVgaspdwdfmRFLITRFEPndgpqtQMAAFLRTMFTDDVL 337
Cdd:TIGR01968 135 DEAIVVTTpeVSAVRDADRVIGLLEAKG-----IEKI---------HLIVNRLRP------EMVKKGDMLSVDDVL 190
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
123-338 1.29e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 46.35  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFR----P-EIDFPEagtvYDALRYeDPipfRDVVRktyfh 197
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTElgnePtEVAVPN----LYALEI-DP---EAELE----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 198 nldlaaaglllsEFETETAHALRNNIRPPFYQRLAL---CINEV-----------ETDYDIVVIDCPPqlgfT--TLSAL 261
Cdd:COG0003   78 ------------EYWERVRAPLRGLLPSAGVDELAEslpGTEELaaldellelleEGEYDVIVVDTAP----TghTLRLL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849138834 262 vastSLvvtviPSMLD--VASMAQFLQLTSSLMATIADVGASPDWDFMRFLITRFEpndgpqtqMAAFLRTMFTDDVLT 338
Cdd:COG0003  142 ----SL-----PELLGwwLDRLLKLRRKASGLGRPLAGILGLPDDPVLEGLEELRE--------RLERLRELLRDPERT 203
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 123-162 1.36e-05

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: 45.96  E-value: 1.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFG 162
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFG 47
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 115-152 3.19e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 45.05  E-value: 3.19e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD 152
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 116-162 5.21e-05

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 44.37  E-value: 5.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 849138834  116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD---PqaSMTTMFG 162
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADiygP--SIPRMLG 52
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 123-195 8.58e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 43.99  E-value: 8.58e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRpeidfpEAGTVYDALRYE--DPIPFRDVVRKTY 195
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGE------KIPTVLDVLREKgiDNLGLEDIIYEGF 77
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 123-197 1.68e-04

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: 42.89  E-value: 1.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFGFRPEIDfpeagTVYDALRYEDPIPFRDVVRKTYFH 197
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAIP-----TVLDTLREKGEVEELEDVIKEGFN 77
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 123-195 3.99e-04

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 41.90  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTtmfgfrpeidFPEAG----TVYDALR-----YEDPIPfRDVVRK 193
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDST----------FTLTGflipTVIDVLQsvdfhYEEVWP-EDVIFT 76


                 ..
gi 849138834 194 TY 195
Cdd:cd02032   77 GY 78
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 111-163 4.77e-04

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: 40.88  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 849138834  111 GEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASmtTMFGF 163
Cdd:TIGR01007  14 GAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNS--VMSGT 64
chlL CHL00072
photochlorophyllide reductase subunit L
 123-196 5.91e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 41.26  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMT-TMFGFRpeidFPeagTVYDALR-----YEDPIPfRDVVRKTYF 196
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTfTLTGFL----IP---TIIDTLQskdyhYEDVWP-EDVIYKGYG 79
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
116-162 6.51e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 41.57  E-value: 6.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 849138834 116 IISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD---PqaSMTTMFG 162
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADiygP--SIPTMLG 156
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 123-195 6.52e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 41.10  E-value: 6.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834 123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTtmfgfrpeidFPEAG----TVYDALR-----YEDPIPfRDVVRK 193
Cdd:PRK13185  10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST----------FTLTGklvpTVIDILEevdfhSEELRP-EDFVYE 78


                 ..
gi 849138834 194 TY 195
Cdd:PRK13185  79 GY 80
minD CHL00175
septum-site determining protein; Validated
 115-152 8.37e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.91  E-value: 8.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 849138834 115 QIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD 152
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 118-158 9.33e-04

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: 40.81  E-value: 9.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 849138834 118 SIANF-KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMT 158
Cdd:cd02117    2 SIVVYgKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDST 43
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
123-195 1.45e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 40.12  E-value: 1.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 849138834  123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMT--TMFGFRPEidfpeagTVYDALRYEDP---IPFRDVVRKTY 195
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTrlLLGGKLQP-------TVLDTAREKGYvedVEVEDVVYKGY 78
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
114-152 2.16e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 39.44  E-value: 2.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 849138834 114 IQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD 152
Cdd:PRK13849   1 MKLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEAD 39
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 123-155 2.28e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.07  E-value: 2.28e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 849138834  123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQA 155
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAA 361
HTH_MlrA-like_sg2 cd04765
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ...
 42-91 2.46e-03

Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.


Pssm-ID: 133393  Cd Length: 99  Bit Score: 37.23  E-value: 2.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 849138834  42 FSSTEVAQILGVSQDFLRkmFFEDKLDlgEIE--TDARGRRFYTAEQIDIAR 91
Cdd:cd04765    1 FSIGEVAEILGLPPHVLR--YWETEFP--QLKpvKRAGGRRYYRPKDVELLL 48
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 7-272 2.57e-03

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: 40.09  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834    7 RMDQKIQTMATRLSKSLDVNmrKSFLPDERKSLRRFSSTEVAQILGV----SQDFLRKMFFEDKLDLGEIETDArGRRFY 82
Cdd:TIGR01005 405 DMEQAKLQKAFKIAKARLID--EAAVPEEPSKPKKLMTLALAAVLGMmlggAAAAFLEALEGGFRDEGDIEEHL-GHRSL 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834   83 -----------------TAEQIDIARHEIARSSTKFQHIVPRR-----------------------RDGEHIQIISIANF 122
Cdd:TIGR01005 482 atvplldtqmdkkaqltHAHFGSVKRHDEAVDDTMPFQLLARIvpdaprstfaeafrnaklacdfaLADAENNLIAIAGA 561

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLD-PQASMTTMFGfrPEidfPEAGTVyDALRYEDPIP---FRDVVRKTYFhn 198
Cdd:TIGR01005 562 LPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFG--KA---PKPGLL-DLLAGEASIEagiHRDQRPGLAF-- 633

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 849138834  199 ldlaAAGLLLSEFETETAHALRNnirppfyQRLALCINEVETDYDIVVIDCPPQLGFTTLSALVASTSLVVTVI 272
Cdd:TIGR01005 634 ----IAAGGASHFPHNPNELLAN-------PAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFVT 696
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 123-162 2.74e-03

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: 39.26  E-value: 2.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 849138834  123 KGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTTMFG 162
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFN 48
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 114-152 3.12e-03

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


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 38.71  E-value: 3.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 849138834  114 IQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLD 152
Cdd:pfam07015   1 MQLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEAD 39
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 68-162 4.64e-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: 39.09  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849138834  68 DLGEIETDARGRRFYTAEQIDIARHEIARSSTKFQHIVPRRRDGEHIQIISIANfKGGAGKTTTAIHLAQKLALDGYRVL 147
Cdd:NF041417 287 DVGEVLYEGKEPTVDVAVITEEETEETSPSETDKEAVMELLRPQKDTRYLFFTG-KGGVGKSTIASTTATYLAEEGYETL 365

                         90
                 ....*....|....*
gi 849138834 148 AIDLDPQASMTTMFG 162
Cdd:NF041417 366 IVTTDPASHLQDIFG 380
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
 108-153 8.79e-03

helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.


Pssm-ID: 274798 [Multi-domain]  Cd Length: 322  Bit Score: 37.70  E-value: 8.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 849138834  108 RRDGEHIQIISIANFKGGAGKTTTAIHLAQKLALDGYRVLAIDLDP 153
Cdd:TIGR03815  87 QSPPARGVVVAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADP 132
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 115-162 9.52e-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: 37.89  E-value: 9.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 849138834 115 QIISIANfKGGAGKTTTAIHLAQKLALDGYRVLAIDLDPQASMTT-MFG 162
Cdd:cd02033   32 QIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSlLFG 79
LpxK pfam02606
Tetraacyldisaccharide-1-P 4'-kinase; This family consists of tetraacyldisaccharide-1-P 4 ...
 116-146 9.82e-03

Tetraacyldisaccharide-1-P 4'-kinase; This family consists of tetraacyldisaccharide-1-P 4'-kinase also known as Lipid-A 4'-kinase or Lipid A biosynthesis protein LpxK, EC:2.7.1.130. This enzyme catalyzes the reaction: ATP + 2,3-bis(3-hydroxytetradecanoyl)-D -glucosaminyl-(beta-D-1,6)-2,3-bis(3-hydroxytetradecanoyl)-D-glu cosam inyl beta-phosphate <=> ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D- glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate. This enzyme is involved in the synthesis of lipid A portion of the bacterial lipopolysaccharide layer (LPS). The family contains a P-loop motif at the N terminus.


Pssm-ID: 460616  Cd Length: 319  Bit Score: 37.55  E-value: 9.82e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 849138834  116 IISIANFK-GGAGKTTTAIHLAQKLALDGYRV 146
Cdd:pfam02606  37 VIVVGNITvGGTGKTPLVIALAKLLRARGLRP 68
 
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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