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Conserved domains on  [gi|148872378|gb|ABR14868|]
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putative plasmid partitioning transcription repressor (plasmid) [Yersinia pestis CA88-4125]

Protein Classification

PRK13705 family protein( domain architecture ID 11486804)

PRK13705 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 1-388 0e+00

plasmid-partitioning protein SopA; Provisional


:

Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 840.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378   1 MDLKSTLDRCIERGQFMTQEIAKSQFGNDSPAARTITRRWRITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVEQRT 80
Cdd:PRK13705   1 MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEMRGRVEQRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  81 GYSIQQINDMRDVFKTRLSKPKGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLYHGYVPDL 160
Cdd:PRK13705  81 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 161 HIHEEDTLLPYYLGQRDDAAYAIKPTCWPNLEVIPSCLAVHRIESEIYGLHDQGKLPVAPHLLLRAAIESVWDSYDVVVL 240
Cdd:PRK13705 161 HIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 241 DSAPNLGIGTINVVCAADVIVVPTPAELYDYVSTLQFFTMLRDLMSNIDLNGFEPDVRVLITKFSNAIGSQSQWMDDQIR 320
Cdd:PRK13705 241 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148872378 321 NAWGGMVLKEVVRVTDEVGKGQVRMRTVFEQAANQRSTPAAWRNAVSIWEPVCAEIFNRLVKPRWENA 388
Cdd:PRK13705 321 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 388
 
Name Accession Description Interval E-value
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 1-388 0e+00

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 840.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378   1 MDLKSTLDRCIERGQFMTQEIAKSQFGNDSPAARTITRRWRITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVEQRT 80
Cdd:PRK13705   1 MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEMRGRVEQRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  81 GYSIQQINDMRDVFKTRLSKPKGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLYHGYVPDL 160
Cdd:PRK13705  81 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 161 HIHEEDTLLPYYLGQRDDAAYAIKPTCWPNLEVIPSCLAVHRIESEIYGLHDQGKLPVAPHLLLRAAIESVWDSYDVVVL 240
Cdd:PRK13705 161 HIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 241 DSAPNLGIGTINVVCAADVIVVPTPAELYDYVSTLQFFTMLRDLMSNIDLNGFEPDVRVLITKFSNAIGSQSQWMDDQIR 320
Cdd:PRK13705 241 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148872378 321 NAWGGMVLKEVVRVTDEVGKGQVRMRTVFEQAANQRSTPAAWRNAVSIWEPVCAEIFNRLVKPRWENA 388
Cdd:PRK13705 321 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 388
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-380 3.37e-48

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: 163.88  E-value: 3.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHGYVPDlhiHEEDTLLPYYLGQRDdAAYAIKPTC 187
Cdd:COG1192    3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDL-DPQGNLTSGLGLDPD---DLDPTLYDLLLDDAP-LEDAIVPTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 188 WPNLEVIPSCLAVHRIESEIYGLHDqgklpvaPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAADVIVVPTPAE 267
Cdd:COG1192   78 IPGLDLIPANIDLAGAEIELVSRPG-------RELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 268 LYDYVSTLQFFTMLRDLMS--NIDLNGfepdVRVLITKFSNAIGSQSQWMdDQIRNAWGGMVLKEVVRVTDEVGKGQVRM 345
Cdd:COG1192  151 YLSLEGLAQLLETIEEVREdlNPKLEI----LGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSVALAEAPSAG 225

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148872378 346 RTVFEQAANQRSTPAawrnavsiWEPVCAEIFNRL 380
Cdd:COG1192  226 KPVFEYDPKSKGAKA--------YRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 109-348 8.04e-42

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: 146.72  E-value: 8.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  109 LAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHGYVPDLHI--HEEDTLLPYYlGQRDDAAYAIKPT 186
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDL-DPQSNNSSVEGLEGDIAPalQALAEGLKGR-VNLDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  187 CWpNLEVIPSCLAVHRIESEIYGlhdqgklpVAPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAADVIVVPTPA 266
Cdd:pfam01656  79 EG-GLDLIPGNIDLEKFEKELLG--------PRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  267 ELYDYVSTLQFFTMLRDLMSNIDLNGFEPdVRVLITKF--SNAIGSQSQWMDDQIRnawGGMVLKEVVRvTDEVGKGQVR 344
Cdd:pfam01656 150 EVILVEDAKRLGGVIAALVGGYALLGLKI-IGVVLNKVdgDNHGKLLKEALEELLR---GLPVLGVIPR-DEAVAEAPAR 224


                  ....
gi 148872378  345 MRTV 348
Cdd:pfam01656 225 GLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 108-316 1.08e-25

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: 100.69  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHgyvpdlhiheedtllpyylgqrddaayaikptc 187
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-DPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 188 wpnlevipsclavhrieseiyglhdqgklpvaphlllraaiesvwdsYDVVVLDSAPNLGIGTINVVCAADVIVVPTPAE 267
Cdd:cd02042   48 -----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPS 80

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148872378 268 LYDYVSTLQFFTMLRDLMSNIDLNGfePDVRVLITKFSNAIGSQSQWMD 316
Cdd:cd02042   81 PFDLDGLAKLLDTLEELKKQLNPPL--LILGILLTRVDPRTKLAREVLE 127
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
40-68 1.79e-05

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 42.12  E-value: 1.79e-05
                           10        20
                   ....*....|....*....|....*....
gi 148872378    40 WRITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPPP 29
CadR-PbrR TIGR02047
Cd(II)/Pb(II)-responsive transcriptional regulator; This model represents the cadmium(II) and ...
 41-71 1.30e-03

Cd(II)/Pb(II)-responsive transcriptional regulator; This model represents the cadmium(II) and/or lead(II) responsive transcriptional activator of the proteobacterial metal efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(6-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix. [Regulatory functions, DNA interactions]


Pssm-ID: 131102  Cd Length: 127  Bit Score: 38.63  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 148872378   41 RITEAAELVGVTPQTIRNYEDSGKLPPPDTA 71
Cdd:TIGR02047   2 KIGELAQKTGVSVETIRFYEKQGLLPPPART 32
 
Name Accession Description Interval E-value
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 1-388 0e+00

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 840.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378   1 MDLKSTLDRCIERGQFMTQEIAKSQFGNDSPAARTITRRWRITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVEQRT 80
Cdd:PRK13705   1 MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEMRGRVEQRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  81 GYSIQQINDMRDVFKTRLSKPKGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLYHGYVPDL 160
Cdd:PRK13705  81 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 161 HIHEEDTLLPYYLGQRDDAAYAIKPTCWPNLEVIPSCLAVHRIESEIYGLHDQGKLPVAPHLLLRAAIESVWDSYDVVVL 240
Cdd:PRK13705 161 HIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 241 DSAPNLGIGTINVVCAADVIVVPTPAELYDYVSTLQFFTMLRDLMSNIDLNGFEPDVRVLITKFSNAIGSQSQWMDDQIR 320
Cdd:PRK13705 241 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148872378 321 NAWGGMVLKEVVRVTDEVGKGQVRMRTVFEQAANQRSTPAAWRNAVSIWEPVCAEIFNRLVKPRWENA 388
Cdd:PRK13705 321 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 388
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 1-387 0e+00

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 742.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378   1 MDLKSTLDRCIERGQFMTQEIAKSQFGNDSPAARTITRRWRITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVEQRT 80
Cdd:PHA02519   1 MSLINLLNSCIERGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDFETRGRVERRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  81 GYSIQQINDMRDVFKTRLSKPKGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLYHGYVPDL 160
Cdd:PHA02519  81 GYTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 161 HIHEEDTLLPYYLGQRDDAAYAIKPTCWPNLEVIPSCLAVHRIESEIYGLHDQGKLPVAPHLLLRAAIESVWDSYDVVVL 240
Cdd:PHA02519 161 HIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKLPHPPHLMLRAAIESVWDNYDIIVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 241 DSAPNLGIGTINVVCAADVIVVPTPAELYDYVSTLQFFTMLRDLMSNIDLNGFEPDVRVLITKFSNAIGSQSQWMDDQIR 320
Cdd:PHA02519 241 DSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPVVRLLLTKYSLTVGNQSRWMEEQIR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148872378 321 NAWGGMVLKEVVRVTDEVGKGQVRMRTVFEQAANQRSTPAAWRNAVSIWEPVCAEIFNRLVKPRWEN 387
Cdd:PHA02519 321 NTWGSMVLRQVVRVTDEVGKGQIKMRTVFEQAANQRSTLNAWRNAVAIWEPVCAEIFNDLIKPRWEN 387
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-380 3.37e-48

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: 163.88  E-value: 3.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHGYVPDlhiHEEDTLLPYYLGQRDdAAYAIKPTC 187
Cdd:COG1192    3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDL-DPQGNLTSGLGLDPD---DLDPTLYDLLLDDAP-LEDAIVPTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 188 WPNLEVIPSCLAVHRIESEIYGLHDqgklpvaPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAADVIVVPTPAE 267
Cdd:COG1192   78 IPGLDLIPANIDLAGAEIELVSRPG-------RELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 268 LYDYVSTLQFFTMLRDLMS--NIDLNGfepdVRVLITKFSNAIGSQSQWMdDQIRNAWGGMVLKEVVRVTDEVGKGQVRM 345
Cdd:COG1192  151 YLSLEGLAQLLETIEEVREdlNPKLEI----LGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSVALAEAPSAG 225

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148872378 346 RTVFEQAANQRSTPAawrnavsiWEPVCAEIFNRL 380
Cdd:COG1192  226 KPVFEYDPKSKGAKA--------YRALAEELLERL 252
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 31-388 1.21e-43

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 156.37  E-value: 1.21e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  31 PAARTITRRWRITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRveqrTGYSIQQINDMRDVF----KTRLS------K 100
Cdd:PRK13869  40 PTSHKSLRKFTSGEAARLMKISDSTLRKMTLAGEGPQPELASNGR----RFYTLGQINEIRQMLagstRGRESidfvphR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 101 PKGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDaTDPQATASLYHGYVPDLHIHEEDTLLP--YYLGQRDD 178
Cdd:PRK13869 116 RGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVD-LDPQASLSALLGVLPETDVGANETLYAaiRYDDTRRP 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 179 AAYAIKPTCWPNLEVIPSCLAVHRIE-SEIYGLHDQGKLPVAPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAA 257
Cdd:PRK13869 195 LRDVIRPTYFDGLHLVPGNLELMEFEhTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAA 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 258 DVIVVPTPAELYDYVSTLQFFTMLRDLMSNIDLNG--FEPD-VRVLITKFSNAIGSQSQwMDDQIRNAWGGMVLKEVVRV 334
Cdd:PRK13869 275 TSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGgnLQYDfIRYLLTRYEPQDAPQTK-VAALLRNMFEDHVLTNPMVK 353

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148872378 335 TDEVGKGQVRMRTVFEqAANQRSTPAAWRNAVSIWEPVCAEIfNRLVKPRWENA 388
Cdd:PRK13869 354 SAAVSDAGLTKQTLYE-IGRENLTRSTYDRAMESLDAVNSEI-EALIKMAWGRA 405
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 109-348 8.04e-42

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: 146.72  E-value: 8.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  109 LAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHGYVPDLHI--HEEDTLLPYYlGQRDDAAYAIKPT 186
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDL-DPQSNNSSVEGLEGDIAPalQALAEGLKGR-VNLDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  187 CWpNLEVIPSCLAVHRIESEIYGlhdqgklpVAPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAADVIVVPTPA 266
Cdd:pfam01656  79 EG-GLDLIPGNIDLEKFEKELLG--------PRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  267 ELYDYVSTLQFFTMLRDLMSNIDLNGFEPdVRVLITKF--SNAIGSQSQWMDDQIRnawGGMVLKEVVRvTDEVGKGQVR 344
Cdd:pfam01656 150 EVILVEDAKRLGGVIAALVGGYALLGLKI-IGVVLNKVdgDNHGKLLKEALEELLR---GLPVLGVIPR-DEAVAEAPAR 224


                  ....
gi 148872378  345 MRTV 348
Cdd:pfam01656 225 GLPV 228
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 108-269 1.02e-27

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: 107.67  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHGYVPDlhiHEEDTLLPYYLGQRDDAAyAIKPTC 187
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDL-DPQGNATSGLGIDKN---NVEKTIYELLIGECNIEE-AIIKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  188 WPNLEVIPSCLAVHRIESEIYGLHDqgklpvaPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAADVIVVPTPAE 267
Cdd:pfam13614  78 IENLDLIPSNIDLAGAEIELIGIEN-------RENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150


                  ..
gi 148872378  268 LY 269
Cdd:pfam13614 151 YY 152
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 108-316 1.08e-25

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: 100.69  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDAtDPQATASLYHgyvpdlhiheedtllpyylgqrddaayaikptc 187
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-DPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 188 wpnlevipsclavhrieseiyglhdqgklpvaphlllraaiesvwdsYDVVVLDSAPNLGIGTINVVCAADVIVVPTPAE 267
Cdd:cd02042   48 -----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPS 80

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148872378 268 LYDYVSTLQFFTMLRDLMSNIDLNGfePDVRVLITKFSNAIGSQSQWMD 316
Cdd:cd02042   81 PFDLDGLAKLLDTLEELKKQLNPPL--LILGILLTRVDPRTKLAREVLE 127
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 106-247 3.37e-13

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: 69.45  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 106 PVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATdpqatasLYHGYVPD-LHIHEEDTLLPYYLGQRDDAAyAIK 184
Cdd:COG0489   92 LEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDAD-------LRGPSLHRmLGLENRPGLSDVLAGEASLED-VIQ 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148872378 185 PTCWPNLEVIPSclavhrieseiyglhdqGKLPVAPHLLL-----RAAIESVWDSYDVVVLDSAPNLG 247
Cdd:COG0489  164 PTEVEGLDVLPA-----------------GPLPPNPSELLaskrlKQLLEELRGRYDYVIIDTPPGLG 214
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 89-309 2.48e-09

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: 58.20  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  89 DMRDVFKTRLSKPKGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQ-GLRVLLIDATDPQATASLYHGYVPDLHIHEedt 167
Cdd:COG4963   85 ELRAALARLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRGLAD--- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 168 LLPyyLGQRDDAAY--AIKPTCWPNLEVIPsclAVHRIESeiyglhdqgklpvaPHLLLRAAIESVWD----SYDVVVLD 241
Cdd:COG4963  162 ALR--NPDRLDETLldRALTRHSSGLSVLA---APADLER--------------AEEVSPEAVERLLDllrrHFDYVVVD 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148872378 242 SAPNLGIGTINVVCAADVIVVPTPAELYDYVSTLQFFTMLRDLMSNID-----LNGFEPDVRVLITKFSNAIG 309
Cdd:COG4963  223 LPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDkvrlvLNRVPKRGEISAKDIEEALG 295
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 122-282 1.91e-08

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: 54.51  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 122 STSVHIAQWMALQGLRVLLIDAtDPQ-ATASLYHGYVPDLHIHEedtllpyYLGQRDDAAYAIKPTcwP-NLEVIPSCLA 199
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDA-DLGlANLDVLLGLEPKATLAD-------VLAGEADLEDAIVQG--PgGLDVLPGGSG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 200 VHRIESeiyglhdqgklpVAPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAADVIVVPTPAELYDYVSTLQFFT 279
Cdd:COG0455   71 PAELAE------------LDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLK 138


                 ...
gi 148872378 280 MLR 282
Cdd:COG0455  139 LLR 141
MerR pfam00376
MerR family regulatory protein;
41-68 9.79e-08

MerR family regulatory protein;


Pssm-ID: 425647 [Multi-domain]  Cd Length: 38  Bit Score: 47.80  E-value: 9.79e-08
                          10        20
                  ....*....|....*....|....*...
gi 148872378   41 RITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:pfam00376   1 TIGEVAKLLGVSPRTLRYYEKIGLLPPP 28
HTH_MerR-SF cd04761
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 40-93 3.90e-07

Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


Pssm-ID: 133389 [Multi-domain]  Cd Length: 49  Bit Score: 46.43  E-value: 3.90e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148872378  40 WRITEAAELVGVTPQTIRNYEDSGKLPPPDTAmigrvEQRTGYSIQQINDMRDV 93
Cdd:cd04761    1 YTIGELAKLTGVSPSTLRYYERIGLLSPARTE-----GGYRLYSDADLERLRLI 49
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 102-262 4.80e-07

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: 49.49  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 102 KGENPVVLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDatdpqatASLYHGYVPD-LHIHEEDTLLPYYLGQRDDAA 180
Cdd:cd05387   15 SDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLID-------ADLRRPSLHRlLGLPNEPGLSEVLSGQASLED 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 181 yAIKPTCWPNLEVIPSclavhrieseiyglhdqGKLPVAPHLLL-----RAAIESVWDSYDVVVLDSAPNLGIGTINVV- 254
Cdd:cd05387   88 -VIQSTNIPNLDVLPA-----------------GTVPPNPSELLssprfAELLEELKEQYDYVIIDTPPVLAVADALILa 149

                        170
                 ....*....|
gi 148872378 255 --CAADVIVV 262
Cdd:cd05387  150 plVDGVLLVV 159
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
42-115 9.55e-07

DNA-binding transcriptional regulator, MerR family [Transcription];


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 46.82  E-value: 9.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  42 ITEAAELVGVTPQTIRNYEDSGKLPPP----------DTAMIGRVE-----QRTGYSIQQIndmrdvfKTRLSKPKGENP 106
Cdd:COG0789    1 IGEVARLTGVSVRTLRYYERIGLLPPPerteggyrlySEEDVERLRfirrlRELGFSLAEI-------RELLDLLDDGEE 73


                 ....*....
gi 148872378 107 VVLAIAAHK 115
Cdd:COG0789   74 EVRELLEEH 82
HTH_HMRTR cd04770
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ...
 41-115 4.28e-06

Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; Helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR): MerR1 (mercury), CueR (copper), CadR (cadmium), PbrR (lead), ZntR (zinc), and other related proteins. These transcription regulators mediate responses to heavy metal stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


Pssm-ID: 133398 [Multi-domain]  Cd Length: 123  Bit Score: 45.63  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378  41 RITEAAELVGVTPQTIRNYEDSGKLPPP----------DTAMIGRVE-----QRTGYSIQQINDMRDVfKTRLSKPKGEn 105
Cdd:cd04770    2 KIGELAKAAGVSPDTIRYYERIGLLPPPqrsengyrlyGEADLARLRfirraQALGFSLAEIRELLSL-RDDGAAPCAE- 79

                         90
                 ....*....|
gi 148872378 106 pvVLAIAAHK 115
Cdd:cd04770   80 --VRALLEEK 87
MerR_1 pfam13411
MerR HTH family regulatory protein;
41-96 6.17e-06

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 43.31  E-value: 6.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148872378   41 RITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVeqrtgYS------IQQINDMRDVFKT 96
Cdd:pfam13411   2 TISELARLLGVTPRTLRYWEREGLLPPPRTERGRRY-----YTdedverLRLIKALLERGLS 58
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 108-265 1.29e-05

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: 46.04  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLYHG----YVPDLH--IHEEDTLlpyylgqrDDAAY 181
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGlenrIVYTLVdvLEGECRL--------EQALI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 182 AIKPtcWPNLEVIPsclavhrieseiyGLHDQGKLPVAPHLLLRaAIESVWDSYDVVVLDSAPNLGIGTINVVCAAD-VI 260
Cdd:cd02036   74 KDKR--WENLYLLP-------------ASQTRDKDALTPEKLEE-LVKELKDSFDFILIDSPAGIESGFINAIAPADeAI 137


                 ....*
gi 148872378 261 VVPTP 265
Cdd:cd02036  138 IVTNP 142
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
40-68 1.79e-05

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 42.12  E-value: 1.79e-05
                           10        20
                   ....*....|....*....|....*....
gi 148872378    40 WRITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPPP 29
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 108-265 3.52e-05

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: 44.48  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLYHGYVPDLHIHEedtllpYYLGQRDDAAYAIKPTc 187
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGD------VLKGRVSLEDIIVEGP- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148872378 188 wPNLEVIPSclavhriESEIYGLHDqgkLPVAPHLLLRAAIESVWDSYDVVVLDSAPNLGIGTINVVCAAD-VIVVPTP 265
Cdd:cd02038   75 -EGLDIIPG-------GSGMEELAN---LDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADeVIVVTTP 142
COG2452 COG2452
Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];
41-67 9.99e-05

Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];


Pssm-ID: 441988 [Multi-domain]  Cd Length: 178  Bit Score: 42.67  E-value: 9.99e-05
                         10        20
                 ....*....|....*....|....*..
gi 148872378  41 RITEAAELVGVTPQTIRNYEDSGKLPP 67
Cdd:COG2452    2 TPGEAAELLGVSPKTLRRWEKEGKLPA 28
HTH_CueR cd01108
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ...
 42-91 1.20e-04

Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.


Pssm-ID: 133383 [Multi-domain]  Cd Length: 127  Bit Score: 41.39  E-value: 1.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148872378  42 ITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIG-RVeqrtgYSIQQINDMR 91
Cdd:cd01108    3 IGEAAKLTGLSAKMIRYYEEIGLIPPPSRSDNGyRV-----YNQRDIEELR 48
HTH_MerR-trunc cd04762
Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family ...
 40-67 1.42e-04

Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family mostly have a truncated helix-turn-helix (HTH) MerR-like domain. They lack a portion of the C-terminal region, called Wing 2 and the long dimerization helix that is typically present in MerR-like proteins. These truncated domains are found in response regulator receiver (REC) domain proteins (i.e., CheY), cytosine-C5 specific DNA methylases, IS607 transposase-like proteins, and RacA, a bacterial protein that anchors chromosomes to cell poles.


Pssm-ID: 133390 [Multi-domain]  Cd Length: 49  Bit Score: 39.10  E-value: 1.42e-04
                         10        20
                 ....*....|....*....|....*...
gi 148872378  40 WRITEAAELVGVTPQTIRNYEDSGKLPP 67
Cdd:cd04762    1 LTTKEAAELLGVSPSTLRRWVKEGKLKA 28
HTH_MerR-like cd00592
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ...
 40-97 1.63e-04

Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


Pssm-ID: 133378 [Multi-domain]  Cd Length: 100  Bit Score: 40.31  E-value: 1.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148872378  40 WRITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVeqrtgYSIQQINDMRDVFKTR 97
Cdd:cd00592    1 YTIGEVAKLLGVSVRTLRYYEEKGLLPPERSENGYRL-----YSEEDLERLRLIRRLR 53
HTH_CadR-PbrR cd04784
Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; ...
 41-68 3.15e-04

Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; Helix-turn-helix (HTH) CadR and PbrR transcription regulators including Pseudomonas aeruginosa CadR and Ralstonia metallidurans PbrR that regulate expression of the cadmium and lead resistance operons, respectively. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines which form a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.


Pssm-ID: 133411  Cd Length: 127  Bit Score: 40.25  E-value: 3.15e-04
                         10        20
                 ....*....|....*....|....*...
gi 148872378  41 RITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:cd04784    2 KIGELAKKTGCSVETIRYYEKEGLLPAP 29
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 115-244 3.31e-04

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 41.72  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 115 KGGAYKTSTSVHIAQWMALQGLRVLLIdATDPQATASlyhgyvpDLhiheedtllpyyLGQRDDAAYAIKPTcwPNLEVI 194
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLV-STDPAHSLS-------DA------------FGQKLGGETPVKGA--PNLWAM 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 195 ---PScLAVHRIESEIYG-----LHDQGKLPVAPHLLLR-------AAIESVWD-----SYDVVVLDSAP 244
Cdd:cd02035   66 eidPE-EALEEYWEEVKEllaqyLRLPGLDEVYAEELLSlpgmdeaAAFDELREyvesgEYDVIVFDTAP 134
HTH_TioE_rpt2 cd04773
Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ...
 41-98 6.16e-04

Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD mainly contains the C-terminal or second repeat (rpt2) of these tandem MerR-like domain proteins.


Pssm-ID: 133400  Cd Length: 108  Bit Score: 38.88  E-value: 6.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148872378  41 RITEAAELVGVTPQTIRNYEDSGKLPPpdtamiGRVEQrTGYSIQQINDMRDVFKTRL 98
Cdd:cd04773    2 TIGELAHLLGVPPSTLRHWEKEGLLSP------DREPE-TGYRVYDPSDVRDARLIHL 52
HTH_HspR-like cd01279
Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix ...
 42-105 6.24e-04

Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix (HTH) transcription regulator HspR and related proteins, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.


Pssm-ID: 133387  Cd Length: 98  Bit Score: 38.73  E-value: 6.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148872378  42 ITEAAELVGVTPQTIRNYEDSGKLPPPDTAMIGRVeqrtgYSIQQINDMRDVfkTRLSKPKGEN 105
Cdd:cd01279    4 ISVAAELLGIHPQTLRVYDRLGLVSPARTNGGGRR-----YSNNDLELLRQV--QRLSQDEGFN 60
HTH_TioE_rpt1 cd04772
First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ...
 40-68 8.50e-04

First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD contains the N-terminal or first repeat (rpt1) of these tandem MerR-like domain proteins.


Pssm-ID: 133399  Cd Length: 99  Bit Score: 38.53  E-value: 8.50e-04
                         10        20
                 ....*....|....*....|....*....
gi 148872378  40 WRITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:cd04772    1 YRTVDLARAIGLSPQTVRNYESLGLIPPA 29
HTH_YyaN cd01109
Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; ...
 42-87 1.03e-03

Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


Pssm-ID: 133384 [Multi-domain]  Cd Length: 113  Bit Score: 38.59  E-value: 1.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148872378  42 ITEAAELVGVTPQTIRNYEDSGKLPPP----------DTAMIGRVE-----QRTGYSIQQI 87
Cdd:cd01109    3 IKEVAEKTGLSADTLRYYEKEGLLPPVkrdengirdfTEEDLEWLEfikclRNTGMSIKDI 63
HTH_MerR2 cd04769
Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix ...
 42-68 1.15e-03

Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MerR2 and related proteins. MerR2 in Bacillus cereus RC607 regulates resistance to organomercurials. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


Pssm-ID: 133397 [Multi-domain]  Cd Length: 116  Bit Score: 38.50  E-value: 1.15e-03
                         10        20
                 ....*....|....*....|....*..
gi 148872378  42 ITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:cd04769    3 IGELAQQTGVTIKAIRLYEEKGLLPSP 29
AlpA COG3311
DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];
34-68 1.19e-03

DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];


Pssm-ID: 442540 [Multi-domain]  Cd Length: 64  Bit Score: 36.83  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 148872378  34 RTITRRWRITEAAELVGVTPQTIRNYEDSGKLPPP 68
Cdd:COG3311    3 LPPDRLLRLKEVAELLGVSRSTIYRLIKKGEFPKP 37
CadR-PbrR TIGR02047
Cd(II)/Pb(II)-responsive transcriptional regulator; This model represents the cadmium(II) and ...
 41-71 1.30e-03

Cd(II)/Pb(II)-responsive transcriptional regulator; This model represents the cadmium(II) and/or lead(II) responsive transcriptional activator of the proteobacterial metal efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(6-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix. [Regulatory functions, DNA interactions]


Pssm-ID: 131102  Cd Length: 127  Bit Score: 38.63  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 148872378   41 RITEAAELVGVTPQTIRNYEDSGKLPPPDTA 71
Cdd:TIGR02047   2 KIGELAQKTGVSVETIRFYEKQGLLPPPART 32
PRK09841 PRK09841
tyrosine-protein kinase;
120-254 3.94e-03

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 39.51  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 120 KTSTSVHIAQWMALQGLRVLLIDAtdpqataSLYHGYVPDLHIHEEDTLLPYYLGQRDDAAYAIKPTCWPNLEVIpSCla 199
Cdd:PRK09841 545 KTFVSSTLAAVIAQSDQKVLFIDA-------DLRRGYSHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVI-TR-- 614

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148872378 200 vhrieseiyglhdqGKLPVAPHLLL-----RAAIESVWDSYDVVVLDSAPNLGIGTINVV 254
Cdd:PRK09841 615 --------------GQVPPNPSELLmrdrmRQLLEWANDHYDLVIVDTPPMLAVSDAAVV 660
HTH_HspR cd04766
Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) ...
 42-105 3.96e-03

Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) transcription regulator HspR, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.


Pssm-ID: 133394 [Multi-domain]  Cd Length: 91  Bit Score: 36.09  E-value: 3.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148872378  42 ITEAAELVGVTPQTIRNYEDSGKLPPpdtamigrveQRTG-----YSIQQINDMRDVfkTRLSKPKGEN 105
Cdd:cd04766    4 ISVAAELSGMHPQTLRLYERLGLLSP----------SRTDggtrrYSERDIERLRRI--QRLTQELGVN 60
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 115-146 4.68e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 38.92  E-value: 4.68e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 148872378  115 KGGAYKTSTSVHIAQWMALQGLRVLLIdATDP 146
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLV-STDP 41
HTH_17 pfam12728
Helix-turn-helix domain; This domain is a DNA-binding helix-turn-helix domain.
 42-67 6.20e-03

Helix-turn-helix domain; This domain is a DNA-binding helix-turn-helix domain.


Pssm-ID: 463684 [Multi-domain]  Cd Length: 51  Bit Score: 34.36  E-value: 6.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 148872378   42 ITEAAELVGVTPQTIRNYEDSGKLPP 67
Cdd:pfam12728   4 VEEAAELLGVSRRTVYRLIRSGELPA 29
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 108-145 6.52e-03

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: 35.87  E-value: 6.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 148872378 108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATD 145
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
HTH_GnyR cd04776
Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR; Putative helix-turn-helix ...
 40-67 7.25e-03

Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR; Putative helix-turn-helix (HTH) regulatory protein, GnyR, and other related proteins. GnyR belongs to the gnyRDBHAL cluster, which is involved in acyclic isoprenoid degradation in Pseudomonas aeruginosa. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.


Pssm-ID: 133403  Cd Length: 118  Bit Score: 35.97  E-value: 7.25e-03
                         10        20
                 ....*....|....*....|....*...
gi 148872378  40 WRITEAAELVGVTPQTIRNYEDSGKLPP 67
Cdd:cd04776    1 YTISELAREFDVTPRTLRFYEDKGLLSP 28
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 108-153 7.65e-03

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: 37.82  E-value: 7.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 148872378  108 VLAIAAHKGGAYKTSTSVHIAQWMALQGLRVLLIDATDPQATASLY 153
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRY 47
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 38-67 9.61e-03

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 34.07  E-value: 9.61e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 148872378  38 RRWRITEAAELVGVTPQTIRNYEdSGKLPP 67
Cdd:cd00093   11 KGLTQEELAEKLGVSRSTISRIE-NGKRNP 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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