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Conserved domains on  [gi|1941065973|ref|WP_196984358|]
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AAA family ATPase, partial [Klebsiella pneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02519 super family cl30938
plasmid partition protein SopA; Reviewed
 1-302 0e+00

plasmid partition protein SopA; Reviewed


The actual alignment was detected with superfamily member PHA02519:

Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 665.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973   1 MSLINLLHECISRGQEMTQAIAIAQFGDDSPEARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRVERRA 80
Cdd:PHA02519    1 MSLINLLNSCIERGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDFETRGRVERRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  81 GYTIDQISHMRSIFGNPNQRPADKNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160
Cdd:PHA02519   81 GYTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 161 HIHAEDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHAQGKLPHPPHLMLRAAIESVWDNYDIIVI 240
Cdd:PHA02519  161 HIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKLPHPPHLMLRAAIESVWDNYDIIVI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1941065973 241 DSAPNLGTGTINVVCAADIIVVATPAELFDYSSVLQFFTMLLDLLKTVDLGGFEPVVRLLLT 302
Cdd:PHA02519  241 DSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPVVRLLLT 302
 
Name Accession Description Interval E-value
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 1-302 0e+00

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 665.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973   1 MSLINLLHECISRGQEMTQAIAIAQFGDDSPEARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRVERRA 80
Cdd:PHA02519    1 MSLINLLNSCIERGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDFETRGRVERRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  81 GYTIDQISHMRSIFGNPNQRPADKNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160
Cdd:PHA02519   81 GYTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 161 HIHAEDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHAQGKLPHPPHLMLRAAIESVWDNYDIIVI 240
Cdd:PHA02519  161 HIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKLPHPPHLMLRAAIESVWDNYDIIVI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1941065973 241 DSAPNLGTGTINVVCAADIIVVATPAELFDYSSVLQFFTMLLDLLKTVDLGGFEPVVRLLLT 302
Cdd:PHA02519  241 DSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPVVRLLLT 302
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-289 2.63e-42

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: 146.16  E-value: 2.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDlhiHAEDTLLPFYLGERDNAEyAIKPTC 187
Cdd:COG1192     3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLID-LDPQGNLTSGLGLDPD---DLDPTLYDLLLDDAPLED-AIVPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 188 WPGLDIIPSCLALHRIETDLMQYHAqgklphpPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVVATPAE 267
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIELVSRPG-------RELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                         170       180
                  ....*....|....*....|..
gi 1941065973 268 LFDYSSVLQFFTMLLDLLKTVD 289
Cdd:COG1192   151 YLSLEGLAQLLETIEEVREDLN 172
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 109-302 1.52e-34

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: 125.15  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 109 LAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLHI--HAEDTLLPfYLGERDNAEYAIKPT 186
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLID-LDPQSNNSSVEGLEGDIAPalQALAEGLK-GRVNLDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 187 CWpGLDIIPSCLALHRIETDLMQYhaqgklphPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVVATPA 266
Cdd:pfam01656  79 EG-GLDLIPGNIDLEKFEKELLGP--------RKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1941065973 267 ELFDYSSVLQFFTMLLDLLKTVDLGGFePVVRLLLT 302
Cdd:pfam01656 150 EVILVEDAKRLGGVIAALVGGYALLGL-KIIGVVLN 184
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 108-302 2.31e-22

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: 89.91  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGnDPQGTASMYHgyvpdlhihaedtllpfylgerdnaeyaikptc 187
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-DPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 188 wpgldiipsclalhrietdlmqyhaqgklphpphlmlraaiesvwdnYDIIVIDSAPNLGTGTINVVCAADIIVVATPAE 267
Cdd:cd02042    48 -----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPS 80

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1941065973 268 LFDYSSVLQFFTMLLDLLKTVDLGGfePVVRLLLT 302
Cdd:cd02042    81 PFDLDGLAKLLDTLEELKKQLNPPL--LILGILLT 113
ParA_partition NF041546
ParA family partition ATPase;
108-262 1.41e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 65.27  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGnDPQGTASMYHgyvpdlHIHAEDTLLPFylgerdnaeyaikptc 187
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDA-DPQGSALDWA------AAREDERPFPV---------------- 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1941065973 188 wpgldiipscLALHRiETdlmqyhaqgklphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVV 262
Cdd:NF041546   58 ----------VGLAR-PT------------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLI 103
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 108-260 1.20e-05

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: 45.12  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNDPQGTASmyhgYVPDLHihAEDTLLPFYLGERDNAEYAIKPTC 187
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMS----GTFKSQ--NKITGLTNFLSGTTDLSDAICDTN 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941065973 188 WPGLDIIPSclalhrietdlmqyhaqGKLPHPPHLMLRAA-----IESVWDNYDIIVIDSAPnlgtgtINVVCAADII 260
Cdd:TIGR01007  93 IENLDVITA-----------------GPVPPNPTELLQSSnfktlIETLRKRFDYIIIDTPP------IGTVTDAAII 147
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
42-93 2.30e-03

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 35.96  E-value: 2.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1941065973   42 ITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRveRRagYTIDQISHMRSI 93
Cdd:smart00422   3 IGEVAKLAGVSVRTLRYYERIGLLPPPIRTEGGY--RL--YSDEDLERLRFI 50
 
Name Accession Description Interval E-value
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 1-302 0e+00

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 665.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973   1 MSLINLLHECISRGQEMTQAIAIAQFGDDSPEARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRVERRA 80
Cdd:PHA02519    1 MSLINLLNSCIERGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDFETRGRVERRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  81 GYTIDQISHMRSIFGNPNQRPADKNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160
Cdd:PHA02519   81 GYTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 161 HIHAEDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHAQGKLPHPPHLMLRAAIESVWDNYDIIVI 240
Cdd:PHA02519  161 HIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKLPHPPHLMLRAAIESVWDNYDIIVI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1941065973 241 DSAPNLGTGTINVVCAADIIVVATPAELFDYSSVLQFFTMLLDLLKTVDLGGFEPVVRLLLT 302
Cdd:PHA02519  241 DSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPVVRLLLT 302
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 1-302 0e+00

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 556.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973   1 MSLINLLHECISRGQEMTQAIAIAQFGDDSPEARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRVERRA 80
Cdd:PRK13705    1 MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEMRGRVEQRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  81 GYTIDQISHMRSIFGNPNQRPADKNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160
Cdd:PRK13705   81 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 161 HIHAEDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHAQGKLPHPPHLMLRAAIESVWDNYDIIVI 240
Cdd:PRK13705  161 HIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1941065973 241 DSAPNLGTGTINVVCAADIIVVATPAELFDYSSVLQFFTMLLDLLKTVDLGGFEPVVRLLLT 302
Cdd:PRK13705  241 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLT 302
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-289 2.63e-42

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: 146.16  E-value: 2.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDlhiHAEDTLLPFYLGERDNAEyAIKPTC 187
Cdd:COG1192     3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLID-LDPQGNLTSGLGLDPD---DLDPTLYDLLLDDAPLED-AIVPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 188 WPGLDIIPSCLALHRIETDLMQYHAqgklphpPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVVATPAE 267
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIELVSRPG-------RELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                         170       180
                  ....*....|....*....|..
gi 1941065973 268 LFDYSSVLQFFTMLLDLLKTVD 289
Cdd:COG1192   151 YLSLEGLAQLLETIEEVREDLN 172
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 19-302 3.36e-41

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 147.13  E-value: 3.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  19 QAIAIAQFgddSPEARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRverrAGYTIDQISHMRSIFGN-- 96
Cdd:PRK13869   31 QAMSEALF---PPTSHKSLRKFTSGEAARLMKISDSTLRKMTLAGEGPQPELASNGR----RFYTLGQINEIRQMLAGst 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  97 ---------PNQRPADkNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLHIHAEDT 167
Cdd:PRK13869  104 rgresidfvPHRRGSE-HLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVD-LDPQASLSALLGVLPETDVGANET 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 168 LLPF--YLGERDNAEYAIKPTCWPGLDIIPSCLALHRIE-TDLMQYHAQGKLPHPPHLMLRAAIESVWDNYDIIVIDSAP 244
Cdd:PRK13869  182 LYAAirYDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEhTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVVIDCPP 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1941065973 245 NLGTGTINVVCAADIIVVATPAELFDYSSVLQFFTMLLDLLKTV-DLGG--FEPVVRLLLT 302
Cdd:PRK13869  262 QLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVkEAGGnlQYDFIRYLLT 322
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 109-302 1.52e-34

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: 125.15  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 109 LAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLHI--HAEDTLLPfYLGERDNAEYAIKPT 186
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLID-LDPQSNNSSVEGLEGDIAPalQALAEGLK-GRVNLDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 187 CWpGLDIIPSCLALHRIETDLMQYhaqgklphPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVVATPA 266
Cdd:pfam01656  79 EG-GLDLIPGNIDLEKFEKELLGP--------RKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1941065973 267 ELFDYSSVLQFFTMLLDLLKTVDLGGFePVVRLLLT 302
Cdd:pfam01656 150 EVILVEDAKRLGGVIAALVGGYALLGL-KIIGVVLN 184
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 108-289 4.09e-26

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: 101.51  E-value: 4.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGnDPQGTASMYHGYVPDlhiHAEDTLLPFYLGERDNAEyAIKPTC 187
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDL-DPQGNATSGLGIDKN---NVEKTIYELLIGECNIEE-AIIKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 188 WPGLDIIPSCLALHRIETDLMQYHaqgklphPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVVATPAE 267
Cdd:pfam13614  78 IENLDLIPSNIDLAGAEIELIGIE-------NRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150

                         170       180
                  ....*....|....*....|..
gi 1941065973 268 LFdyssVLQFFTMLLDLLKTVD 289
Cdd:pfam13614 151 YY----ALEGLSQLLNTIKLVK 168
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 108-302 2.31e-22

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: 89.91  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGnDPQGTASMYHgyvpdlhihaedtllpfylgerdnaeyaikptc 187
Cdd:cd02042     2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-DPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 188 wpgldiipsclalhrietdlmqyhaqgklphpphlmlraaiesvwdnYDIIVIDSAPNLGTGTINVVCAADIIVVATPAE 267
Cdd:cd02042    48 -----------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPS 80

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1941065973 268 LFDYSSVLQFFTMLLDLLKTVDLGGfePVVRLLLT 302
Cdd:cd02042    81 PFDLDGLAKLLDTLEELKKQLNPPL--LILGILLT 113
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 102-265 1.41e-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: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 102 ADKNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNdpqgtasMYHGYVPD-LHIHAEDTLLPFYLGERDNAE 180
Cdd:COG0489    88 LRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDAD-------LRGPSLHRmLGLENRPGLSDVLAGEASLED 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 181 yAIKPTCWPGLDIIPSclalhrietdlmqyhaqGKL-PHPPHLM----LRAAIESVWDNYDIIVIDSAPnlGTGTINVVC 255
Cdd:COG0489   161 -VIQPTEVEGLDVLPA-----------------GPLpPNPSELLaskrLKQLLEELRGRYDYVIIDTPP--GLGVADATL 220

                         170
                  ....*....|....
gi 1941065973 256 AAD----IIVVATP 265
Cdd:COG0489   221 LASlvdgVLLVVRP 234
ParA_partition NF041546
ParA family partition ATPase;
108-262 1.41e-12

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 65.27  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGnDPQGTASMYHgyvpdlHIHAEDTLLPFylgerdnaeyaikptc 187
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDA-DPQGSALDWA------AAREDERPFPV---------------- 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1941065973 188 wpgldiipscLALHRiETdlmqyhaqgklphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADIIVV 262
Cdd:NF041546   58 ----------VGLAR-PT------------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLI 103
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 90-263 1.06e-09

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: 56.81  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  90 MRSIFGNPNQRPADKNPAVLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNdpqgtasMYHGYVPD-LHIHAEDTL 168
Cdd:cd05387     3 FRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD-------LRRPSLHRlLGLPNEPGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 169 LPFYLGERDNAEyAIKPTCWPGLDIIPSclalhrietdlmqyhaqGKLPHPPHLML-----RAAIESVWDNYDIIVIDSA 243
Cdd:cd05387    76 SEVLSGQASLED-VIQSTNIPNLDVLPA-----------------GTVPPNPSELLssprfAELLEELKEQYDYVIIDTP 137

                         170       180
                  ....*....|....*....|...
gi 1941065973 244 PNLGTGTINVV---CAADIIVVA 263
Cdd:cd05387   138 PVLAVADALILaplVDGVLLVVR 160
PHA02518 PHA02518
ParA-like protein; Provisional
 108-151 1.38e-09

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 56.78  E-value: 1.38e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGnDPQGTAS 151
Cdd:PHA02518    2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDL-DPQGSST 44
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 108-265 1.50e-08

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: 54.11  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNdpQGTASMyhgyvpD--LHIHAEDTLLPFYLGERDNAEYAIKP 185
Cdd:cd02038     2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD--LGLANL------DilLGLAPKKTLGDVLKGRVSLEDIIVEG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 186 TcwPGLDIIPSclalhriETDLMQYhAQgkLPHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAAD-IIVVAT 264
Cdd:cd02038    74 P--EGLDIIPG-------GSGMEEL-AN--LDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADeVIVVTT 141


                  .
gi 1941065973 265 P 265
Cdd:cd02038   142 P 142
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 131-265 1.00e-07

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: 51.81  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 131 LALQGHRVLLIEGNDPQGTASMYHGYVPDLHIHAedtllpfYLGERDNAEYAIKPTcwP-GLDIIPSCLALHRIEtdlmq 209
Cdd:COG0455    10 LARLGKRVLLVDADLGLANLDVLLGLEPKATLAD-------VLAGEADLEDAIVQG--PgGLDVLPGGSGPAELA----- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1941065973 210 yhaqgklPHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAAD-IIVVATP 265
Cdd:COG0455    76 -------ELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADeVVVVTTP 125
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 28-268 2.24e-06

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: 48.57  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  28 DDSPEARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRVERRAGYTIDQISHMRSIFGNPNQRPADKNPA 107
Cdd:COG4963    24 ALIEAAAEDRRLALAAVAVASGGAAAAAAAYLSAPTPNLILLEALSESAALLADVLPLSPDELRAALARLLDPGAARRGR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQ-GHRVLLIEGNDPQGTASMYHGYVPDLHIhAEDTLLPfylgERDNAEY--AIK 184
Cdd:COG4963   104 VIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRGL-ADALRNP----DRLDETLldRAL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 185 PTCWPGLDIIPSclalhriETDlmqyhaqgklPHPPHLMLRAAIESVWD----NYDIIVIDSAPNLGTGTINVVCAADII 260
Cdd:COG4963   179 TRHSSGLSVLAA-------PAD----------LERAEEVSPEAVERLLDllrrHFDYVVVDLPRGLNPWTLAALEAADEV 241


                  ....*...
gi 1941065973 261 VVATPAEL 268
Cdd:COG4963   242 VLVTEPDL 249
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 108-260 1.20e-05

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: 45.12  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRVLLIEGNDPQGTASmyhgYVPDLHihAEDTLLPFYLGERDNAEYAIKPTC 187
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMS----GTFKSQ--NKITGLTNFLSGTTDLSDAICDTN 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941065973 188 WPGLDIIPSclalhrietdlmqyhaqGKLPHPPHLMLRAA-----IESVWDNYDIIVIDSAPnlgtgtINVVCAADII 260
Cdd:TIGR01007  93 IENLDVITA-----------------GPVPPNPTELLQSSnfktlIETLRKRFDYIIIDTPP------IGTVTDAAII 147
HTH_MerR-SF cd04761
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 42-93 2.68e-05

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: 41.04  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1941065973  42 ITEVADLIGVSPQAIRDAEKNGRLPPpdfelrgrvERRAG----YTIDQISHMRSI 93
Cdd:cd04761     3 IGELAKLTGVSPSTLRYYERIGLLSP---------ARTEGgyrlYSDADLERLRLI 49
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 115-141 5.68e-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: 40.57  E-value: 5.68e-04
                          10        20
                  ....*....|....*....|....*..
gi 1941065973 115 KGGVYKTSSAVHEAQWLALQGHRVLLI 141
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLV 34
MerR pfam00376
MerR family regulatory protein;
42-68 2.07e-03

MerR family regulatory protein;


Pssm-ID: 425647 [Multi-domain]  Cd Length: 38  Bit Score: 35.09  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|....*..
gi 1941065973  42 ITEVADLIGVSPQAIRDAEKNGRLPPP 68
Cdd:pfam00376   2 IGEVAKLLGVSPRTLRYYEKIGLLPPP 28
AlpA COG3311
DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];
37-68 2.16e-03

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


Pssm-ID: 442540 [Multi-domain]  Cd Length: 64  Bit Score: 36.06  E-value: 2.16e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1941065973  37 TRRWGITEVADLIGVSPQAIRDAEKNGRLPPP 68
Cdd:COG3311     6 DRLLRLKEVAELLGVSRSTIYRLIKKGEFPKP 37
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
42-93 2.30e-03

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 35.96  E-value: 2.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1941065973   42 ITEVADLIGVSPQAIRDAEKNGRLPPPDFELRGRveRRagYTIDQISHMRSI 93
Cdd:smart00422   3 IGEVAKLAGVSVRTLRYYERIGLLPPPIRTEGGY--RL--YSDEDLERLRFI 50
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
33-70 3.45e-03

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 35.19  E-value: 3.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1941065973   33 ARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPDF 70
Cdd:smart00530   4 ELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLET 41
HTH_CueR cd01108
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ...
 42-103 3.78e-03

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: 36.77  E-value: 3.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1941065973  42 ITEVADLIGVSPQAIRDAEKNGRLPPPD--------------FELRG-RVERRAGYTIDQISHMRSIFGNPNQRPAD 103
Cdd:cd01108     3 IGEAAKLTGLSAKMIRYYEEIGLIPPPSrsdngyrvynqrdiEELRFiRRARDLGFSLEEIRELLALWRDPSRASAD 79
MerR_1 pfam13411
MerR HTH family regulatory protein;
42-90 4.78e-03

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 34.84  E-value: 4.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1941065973  42 ITEVADLIGVSPQAIRDAEKNGRLPPPDFElRGR-------VER--------RAGYTIDQISHM 90
Cdd:pfam13411   3 ISELARLLGVTPRTLRYWEREGLLPPPRTE-RGRryytdedVERlrlikallERGLSLKEIKEL 65
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 33-69 4.98e-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: 34.84  E-value: 4.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1941065973  33 ARRITRRWGITEVADLIGVSPQAIRDAEKNGRLPPPD 69
Cdd:cd00093     6 ELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLE 42
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 108-138 6.39e-03

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: 37.43  E-value: 6.39e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLALQGHRV 138
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKV 35
HTH_HMRTR cd04770
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ...
 42-115 7.02e-03

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: 36.00  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941065973  42 ITEVADLIGVSPQAIRDAEKNGRLPPP----------DFELRGRVE--RRA---GYTIDQISHMRSIFGNPNQRPADknp 106
Cdd:cd04770     3 IGELAKAAGVSPDTIRYYERIGLLPPPqrsengyrlyGEADLARLRfiRRAqalGFSLAEIRELLSLRDDGAAPCAE--- 79


                  ....*....
gi 1941065973 107 aVLAVMSHK 115
Cdd:cd04770    80 -VRALLEEK 87
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
42-90 7.69e-03

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


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 35.27  E-value: 7.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1941065973  42 ITEVADLIGVSPQAIRDAEKNGRLPPP----------DFELRGRVE-----RRAGYTIDQISHM 90
Cdd:COG0789     1 IGEVARLTGVSVRTLRYYERIGLLPPPerteggyrlySEEDVERLRfirrlRELGFSLAEIREL 64
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 112-146 8.97e-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: 37.33  E-value: 8.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1941065973 112 MSHKGGVYKTSSAVHEAQWLALQGHRVLLIEgNDP 146
Cdd:pfam02374   6 FGGKGGVGKTTVSAATAVQLSELGKKVLLIS-TDP 39
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
33-87 9.48e-03

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 34.05  E-value: 9.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1941065973  33 ARRITRRWGITEVADLIGVSPQAIRDAEKNGRLppPDFELRGRVERRAGYTIDQI 87
Cdd:COG1476    11 ELRKERGLTQEELAELLGVSRQTISAIENGKYN--PSLELALKIARALGVSLEEL 63
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 108-162 9.69e-03

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: 36.87  E-value: 9.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1941065973 108 VLAVMSHKGGVYKTSSAVHEAQWLA-LQGHRVLLIEGNDPQGTASMYHGYVPDLHI 162
Cdd:cd03111     2 VVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDLPFGDLGLYLNLRPDYDL 57
 
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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