|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
9-223 |
1.16e-44 |
|
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: 151.93 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALldnykskGYEDPSSEinyyseivlpagKTIYK 88
Cdd:COG1192 2 KVIAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQGNLTSGL-------GLDPDDLD------------PTLYD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LFKPQVDMSQAyetpdkeeVIIDLKDNLDILCGDLNLV-----LVNKVSDHTFVKRIRNFVEDNelrkiYDYIIIDCPPT 163
Cdd:COG1192 62 LLLDDAPLEDA--------IVPTEIPGLDLIPANIDLAgaeieLVSRPGRELRLKRALAPLADD-----YDYILIDCPPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 164 LTIYTDSALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERINLKCLGLIYTMVNKN 223
Cdd:COG1192 129 LGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEILGILLTMVDPR 188
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
8-211 |
5.91e-36 |
|
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.
Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 126.93 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 8 GKIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALldnykskGYEDPSSEinyyseivlpagKTIY 87
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGK-KVLLIDLDPQGNATSGL-------GIDKNNVE------------KTIY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 88 KLFKPQVDMSQAYETPDKEeviidlkdNLDILCGDLNLV-----LVNKVSDHTFVKRIRNFVEDNelrkiYDYIIIDCPP 162
Cdd:pfam13614 61 ELLIGECNIEEAIIKTVIE--------NLDLIPSNIDLAgaeieLIGIENRENILKEALEPVKDN-----YDYIIIDCPP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488246763 163 TLTIYTDSALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERINLK 211
Cdd:pfam13614 128 SLGLLTINALTASDSVLIPVQCEYYALEGLSQLLNTIKLVKKRLNPSLE 176
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
9-223 |
4.21e-29 |
|
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: 107.63 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQFNSTQALldnykskgyedpsseinyyseivlpagktiyk 88
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALA-LRGKRVLLIDLDPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 lfkpqvdmsqayetpdkeeviidlkdnldilcgdlnlvlvnkvsdhtfvkrirnfvednelrkiYDYIIIDCPPTLTIYT 168
Cdd:cd02042 48 ----------------------------------------------------------------YDYILIDTPPSLGLLT 63
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488246763 169 DSALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERINLKCLGLIYTMVNKN 223
Cdd:cd02042 64 RNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLTRVDPR 118
|
|
| PrgP |
NF041283 |
ParA superfamily DNA segregation protein PrgP; |
8-236 |
6.44e-18 |
|
ParA superfamily DNA segregation protein PrgP;
Pssm-ID: 469180 [Multi-domain] Cd Length: 297 Bit Score: 81.72 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 8 GKIVSVINMKGGVGKTTLSIGLSDFLSDLNNCKVLLIDADPQFNSTQALldnykskgyedpsseinyyseivlpaGKTIY 87
Cdd:NF041283 2 GYVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFL--------------------------SKTFN 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 88 KLFKPQVDMSqAYETPDKEEVIIDLKDNLDILCGD-----LNLVLVNKVSDHT-----FVKRIrnfvedNELRKIYDYII 157
Cdd:NF041283 56 VPNFPQSFMK-CVEDGDLEKGIVHLTPNLDLIAGDydtreLGDFLADKFKSEYdrtfyLKKLL------DKIKDDYDFIF 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 158 IDCPPTLTIYTDSALMASDFYLIPNRIDRYSIVGIGSL-QKAVQNLIRE--ERINLKCLGLIYTMVNKNLSPKQLKIKES 234
Cdd:NF041283 129 IDVPPSTDIKVDNAMVAADYVIVIQETQQFAFEGSKKLiLTYLQTLVDDfgDEINVQVAGILPVLLQARRPLQQKIVDET 208
|
..
gi 488246763 235 FE 236
Cdd:NF041283 209 IE 210
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
10-181 |
1.88e-15 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 75.79 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 10 IVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQfNSTQALLdnykskGYEdPsseinyysEIVLPAGKTIYKL 89
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLA-LRGYRVLAIDLDPQ-ASLSALF------GYQ-P--------EFDVGENETLYGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 90 FK---PQVDMSqayetpdkeEVIidLK---DNLDILCGDLNL---------VLVNKVSDHT-FVKRIRNF---VEDNelr 150
Cdd:TIGR03453 169 IRyddERRPIS---------EII--RKtyfPGLDLVPGNLELmefehetprALSRGQGGDTiFFARVGEAlaeVEDD--- 234
|
170 180 190
....*....|....*....|....*....|.
gi 488246763 151 kiYDYIIIDCPPTLTIYTDSALMASDFYLIP 181
Cdd:TIGR03453 235 --YDVVVIDCPPQLGFLTLSALCAATGVLIT 263
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
10-181 |
2.58e-15 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 72.97 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 10 IVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQfnstQALLDNYKSKGYEDPsseinyySEIVLPAGKTIYKl 89
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGY-RVLLVDADPQ----GSALDWAAAREDERP-------FPVVGLARPTLHR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 90 fkpqvdmsqayetpdkeeviiDLKdnldilcgdlnlvlvnkvsdhtfvkrirnfvednELRKIYDYIIIDCPPTLTIYTD 169
Cdd:NF041546 68 ---------------------ELP----------------------------------SLARDYDFVVIDGPPRAEDLAR 92
|
170
....*....|..
gi 488246763 170 SALMASDFYLIP 181
Cdd:NF041546 93 SAIKAADLVLIP 104
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
9-211 |
6.91e-11 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 62.39 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQfNSTQALLDNYkskgyedPSSEINyyseivlpAGKTIYK 88
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLA-LQGYRVLAVDLDPQ-ASLSALLGVL-------PETDVG--------ANETLYA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LFKpqvdmSQAYETPDKEEVIIDLKDNLDILCGDLNLVLVNK----------VSDHTFVKRIRNFVEdnELRKIYDYIII 158
Cdd:PRK13869 185 AIR-----YDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEHttpkalsdkgTRDGLFFTRVAQAFD--EVADDYDVVVI 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488246763 159 DCPPTLTIYTDSALMASDFYLI---PNRIDRYSIVGIGSLQKAVQNLIREERINLK 211
Cdd:PRK13869 258 DCPPQLGFLTLSGLCAATSMVItvhPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQ 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
9-223 |
1.16e-44 |
|
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: 151.93 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALldnykskGYEDPSSEinyyseivlpagKTIYK 88
Cdd:COG1192 2 KVIAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQGNLTSGL-------GLDPDDLD------------PTLYD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LFKPQVDMSQAyetpdkeeVIIDLKDNLDILCGDLNLV-----LVNKVSDHTFVKRIRNFVEDNelrkiYDYIIIDCPPT 163
Cdd:COG1192 62 LLLDDAPLEDA--------IVPTEIPGLDLIPANIDLAgaeieLVSRPGRELRLKRALAPLADD-----YDYILIDCPPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 164 LTIYTDSALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERINLKCLGLIYTMVNKN 223
Cdd:COG1192 129 LGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEILGILLTMVDPR 188
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
8-211 |
5.91e-36 |
|
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.
Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 126.93 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 8 GKIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALldnykskGYEDPSSEinyyseivlpagKTIY 87
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGK-KVLLIDLDPQGNATSGL-------GIDKNNVE------------KTIY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 88 KLFKPQVDMSQAYETPDKEeviidlkdNLDILCGDLNLV-----LVNKVSDHTFVKRIRNFVEDNelrkiYDYIIIDCPP 162
Cdd:pfam13614 61 ELLIGECNIEEAIIKTVIE--------NLDLIPSNIDLAgaeieLIGIENRENILKEALEPVKDN-----YDYIIIDCPP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488246763 163 TLTIYTDSALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERINLK 211
Cdd:pfam13614 128 SLGLLTINALTASDSVLIPVQCEYYALEGLSQLLNTIKLVKKRLNPSLE 176
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
9-223 |
4.21e-29 |
|
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: 107.63 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQFNSTQALldnykskgyedpsseinyyseivlpagktiyk 88
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALA-LRGKRVLLIDLDPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 lfkpqvdmsqayetpdkeeviidlkdnldilcgdlnlvlvnkvsdhtfvkrirnfvednelrkiYDYIIIDCPPTLTIYT 168
Cdd:cd02042 48 ----------------------------------------------------------------YDYILIDTPPSLGLLT 63
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488246763 169 DSALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERINLKCLGLIYTMVNKN 223
Cdd:cd02042 64 RNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLTRVDPR 118
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
11-230 |
1.40e-27 |
|
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: 106.66 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 11 VSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQAlldnYKSKGYEDPsseinyyseivlpAGKTIYKLF 90
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDPQSNNSSV----EGLEGDIAP-------------ALQALAEGL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 91 KPQVDMSQAYETPDKEEviidlkDNLDILCGDLNLVLVNKVSDHTFVK-RIRNFVEdnELRKIYDYIIIDCPPTLTIYTD 169
Cdd:pfam01656 63 KGRVNLDPILLKEKSDE------GGLDLIPGNIDLEKFEKELLGPRKEeRLREALE--ALKEDYDYVIIDGAPGLGELLR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488246763 170 SALMASDFYLIPNRIDRYSIVGIGSLQKAVQNLIREERI-NLKCLGLIYTMVNKNLSPKQLK 230
Cdd:pfam01656 135 NALIAADYVIIPLEPEVILVEDAKRLGGVIAALVGGYALlGLKIIGVVLNKVDGDNHGKLLK 196
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
4-236 |
2.30e-20 |
|
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: 89.40 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 4 EEKNGKIVSVINMKGGVGKTTLSIGLSDFLSDLNNCKVLLIDADPQFNSTQALLDnykskgyedpsseinyyseivLPAG 83
Cdd:COG4963 98 AARRGRVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLD---------------------LEPR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 84 KTIYklfkpqvDMSQAYETPDK---EEVIIDLKDNLDILCGDLNLVLVNKVSDHTFVKRIrnfvedNELRKIYDYIIIDC 160
Cdd:COG4963 157 RGLA-------DALRNPDRLDEtllDRALTRHSSGLSVLAAPADLERAEEVSPEAVERLL------DLLRRHFDYVVVDL 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488246763 161 PPTLTIYTDSALMASDFYLIPNRIDrysivgIGSLQKAVQ--NLIREERINLKCLGLIYTMVNKNLSPKQLKIKESFE 236
Cdd:COG4963 224 PRGLNPWTLAALEAADEVVLVTEPD------LPSLRNAKRllDLLRELGLPDDKVRLVLNRVPKRGEISAKDIEEALG 295
|
|
| PrgP |
NF041283 |
ParA superfamily DNA segregation protein PrgP; |
8-236 |
6.44e-18 |
|
ParA superfamily DNA segregation protein PrgP;
Pssm-ID: 469180 [Multi-domain] Cd Length: 297 Bit Score: 81.72 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 8 GKIVSVINMKGGVGKTTLSIGLSDFLSDLNNCKVLLIDADPQFNSTQALldnykskgyedpsseinyyseivlpaGKTIY 87
Cdd:NF041283 2 GYVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFL--------------------------SKTFN 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 88 KLFKPQVDMSqAYETPDKEEVIIDLKDNLDILCGD-----LNLVLVNKVSDHT-----FVKRIrnfvedNELRKIYDYII 157
Cdd:NF041283 56 VPNFPQSFMK-CVEDGDLEKGIVHLTPNLDLIAGDydtreLGDFLADKFKSEYdrtfyLKKLL------DKIKDDYDFIF 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 158 IDCPPTLTIYTDSALMASDFYLIPNRIDRYSIVGIGSL-QKAVQNLIRE--ERINLKCLGLIYTMVNKNLSPKQLKIKES 234
Cdd:NF041283 129 IDVPPSTDIKVDNAMVAADYVIVIQETQQFAFEGSKKLiLTYLQTLVDDfgDEINVQVAGILPVLLQARRPLQQKIVDET 208
|
..
gi 488246763 235 FE 236
Cdd:NF041283 209 IE 210
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
10-181 |
1.88e-15 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 75.79 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 10 IVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQfNSTQALLdnykskGYEdPsseinyysEIVLPAGKTIYKL 89
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLA-LRGYRVLAIDLDPQ-ASLSALF------GYQ-P--------EFDVGENETLYGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 90 FK---PQVDMSqayetpdkeEVIidLK---DNLDILCGDLNL---------VLVNKVSDHT-FVKRIRNF---VEDNelr 150
Cdd:TIGR03453 169 IRyddERRPIS---------EII--RKtyfPGLDLVPGNLELmefehetprALSRGQGGDTiFFARVGEAlaeVEDD--- 234
|
170 180 190
....*....|....*....|....*....|.
gi 488246763 151 kiYDYIIIDCPPTLTIYTDSALMASDFYLIP 181
Cdd:TIGR03453 235 --YDVVVIDCPPQLGFLTLSALCAATGVLIT 263
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
10-181 |
2.58e-15 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 72.97 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 10 IVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQfnstQALLDNYKSKGYEDPsseinyySEIVLPAGKTIYKl 89
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGY-RVLLVDADPQ----GSALDWAAAREDERP-------FPVVGLARPTLHR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 90 fkpqvdmsqayetpdkeeviiDLKdnldilcgdlnlvlvnkvsdhtfvkrirnfvednELRKIYDYIIIDCPPTLTIYTD 169
Cdd:NF041546 68 ---------------------ELP----------------------------------SLARDYDFVVIDGPPRAEDLAR 92
|
170
....*....|..
gi 488246763 170 SALMASDFYLIP 181
Cdd:NF041546 93 SAIKAADLVLIP 104
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
17-223 |
3.58e-12 |
|
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: 65.21 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 17 KGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALLDNYKSKGYEDPSSEINYYSEIVLPAGKtiyklfkpqvdm 96
Cdd:COG0489 101 KGGEGKSTVAANLALALAQSGK-RVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEV------------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 97 sqayetpdkeeviidlkDNLDIL-CGDLnlvlVNKVSDHTFVKRIRNFVEdnELRKIYDYIIIDCPPtLTIYTDSALMAS 175
Cdd:COG0489 168 -----------------EGLDVLpAGPL----PPNPSELLASKRLKQLLE--ELRGRYDYVIIDTPP-GLGVADATLLAS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488246763 176 --DFYLI---PNRIDRysivgiGSLQKAVQNLireERINLKCLGLIYTMVNKN 223
Cdd:COG0489 224 lvDGVLLvvrPGKTAL------DDVRKALEML---EKAGVPVLGVVLNMVCPK 267
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
9-211 |
6.91e-11 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 62.39 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQfNSTQALLDNYkskgyedPSSEINyyseivlpAGKTIYK 88
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLA-LQGYRVLAVDLDPQ-ASLSALLGVL-------PETDVG--------ANETLYA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LFKpqvdmSQAYETPDKEEVIIDLKDNLDILCGDLNLVLVNK----------VSDHTFVKRIRNFVEdnELRKIYDYIII 158
Cdd:PRK13869 185 AIR-----YDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEHttpkalsdkgTRDGLFFTRVAQAFD--EVADDYDVVVI 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488246763 159 DCPPTLTIYTDSALMASDFYLI---PNRIDRYSIVGIGSLQKAVQNLIREERINLK 211
Cdd:PRK13869 258 DCPPQLGFLTLSGLCAATSMVItvhPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQ 313
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
24-176 |
7.26e-09 |
|
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: 54.90 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 24 TLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALLDnykskgyedpsseinyyseivLPAGKTIYKLFKPQVDMsqayetp 103
Cdd:COG0455 1 TVAVNLAAALARLGK-RVLLVDADLGLANLDVLLG---------------------LEPKATLADVLAGEADL------- 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488246763 104 dkEEVIIDLKDNLDILCGDLNLVLVNKVSDHTFVKRIRNfvednELRKIYDYIIIDCPPTLTIYTDSALMASD 176
Cdd:COG0455 52 --EDAIVQGPGGLDVLPGGSGPAELAELDPEERLIRVLE-----ELERFYDVVLVDTGAGISDSVLLFLAAAD 117
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
17-160 |
8.09e-09 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 55.17 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 17 KGGVGKTTLSIGLSDFLSDlNNCKVLLIDADPQFNSTQALldnykskGYEDPSSEINYYSEI-------VLPAGKTIYKL 89
Cdd:COG3640 8 KGGVGKTTLSALLARYLAE-KGKPVLAVDADPNANLAEAL-------GLEVEADLIKPLGEMrelikerTGAPGGGMFKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 90 fKPQVDmsqayetpDK-EEVIIDlkdnldilCGDLNLVLVNKVSD---------HTFVKR-IRNFVEDNelrkiYDYIII 158
Cdd:COG3640 80 -NPKVD--------DIpEEYLVE--------GDGVDLLVMGTIEEggsgcycpeNALLRAlLNHLVLGN-----YEYVVV 137
|
..
gi 488246763 159 DC 160
Cdd:COG3640 138 DM 139
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
9-202 |
1.78e-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: 53.73 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALLdNYKSKgyedpsseinyyseivlpagKTIYK 88
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGK-RVLLLDADLGLANLDILL-GLAPK--------------------KTLGD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LFKPQVDMsqayetpdkEEVIIDLKDNLDILCGD---LNLVLVNKVSDHTFVKRIrnfvedNELRKIYDYIIIDCPPTLT 165
Cdd:cd02038 59 VLKGRVSL---------EDIIVEGPEGLDIIPGGsgmEELANLDPEQKAKLIEEL------SSLESNYDYLLIDTGAGIS 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488246763 166 IYTDSALMASDFYLI------PNRIDRYSIVGIGSLQKAVQNL 202
Cdd:cd02038 124 RNVLDFLLAADEVIVvttpepTSITDAYALIKVLSRRGGKKNF 166
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
9-189 |
1.55e-07 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 51.00 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPQFNSTqalldnykskgyeDPSSEINYYSEIVlpagktiyk 88
Cdd:PHA02518 1 KIIAVLNQKGGAGKTTVATNLASWLH-ADGHKVLLVDLDPQGSST-------------DWAEAREEGEPLI--------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 lfkPQVDMSqayetpdkeeviidlkdnldilcgdlnlvlvnkvsdhtfvKRIRNFVEdnELRKIYDYIIIDCPPTLTIYT 168
Cdd:PHA02518 58 ---PVVRMG----------------------------------------KSIRADLP--KVASGYDYVVVDGAPQDSELA 92
|
170 180
....*....|....*....|.
gi 488246763 169 DSALMASDFYLIPNRIDRYSI 189
Cdd:PHA02518 93 RAALRIADMVLIPVQPSPFDI 113
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
9-233 |
1.53e-06 |
|
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: 48.04 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNCKVLLIDADPQFNSTQALLDnykskgyedpsseinyyseivlpaGKTIYK 88
Cdd:cd03111 1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLN------------------------LRPDYD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LfkpqVDMSQAYETPDK---EEVIIDLKDNLDILCGDLNLVLVNKVSDHTFVKRIrnfvedNELRKIYDYIIIDCPPTLT 165
Cdd:cd03111 57 L----ADVIQNLDRLDRtllDSAVTRHSSGLSLLPAPQELEDLEALGAEQVDKLL------QVLRAFYDHIIVDLGHFLD 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488246763 166 IYTDSALMASDFYLIpnrIDRYSIVGIGSLQKAVQNLiREERINLKCLGLIytmVNKNLSPKQLKIKE 233
Cdd:cd03111 127 EVTLAVLEAADEILL---VTQQDLPSLRNARRLLDSL-RELEGSSDRLRLV---LNRYDKKSEISPKD 187
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
5-218 |
3.26e-06 |
|
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: 46.79 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 5 EKNGKIVSVINMKGGVGKTTLSIGLSDFLSdLNNCKVLLIDADPqfnSTQALLDNYKSKGYEDPSSEINYYSEIvlpagk 84
Cdd:cd05387 16 DAGPKVIAVTSASPGEGKSTVAANLAVALA-QSGKRVLLIDADL---RRPSLHRLLGLPNEPGLSEVLSGQASL------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 85 tiyklfkpqvdmsqayetpdkEEVII-DLKDNLDILCgdlnlvlVNKVSDHTFV----KRIRNFVEdnELRKIYDYIIID 159
Cdd:cd05387 86 ---------------------EDVIQsTNIPNLDVLP-------AGTVPPNPSEllssPRFAELLE--ELKEQYDYVIID 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488246763 160 CPPTLTiYTDSALMASdfylipnRID------RYSIVGIGSLQKAVQNLireERINLKCLGLIYT 218
Cdd:cd05387 136 TPPVLA-VADALILAP-------LVDgvllvvRAGKTRRREVKEALERL---EQAGAKVLGVVLN 189
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
9-161 |
2.00e-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: 44.89 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALLdnykskGYEDPsseINYYSEIVLpAGKtiyk 88
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGK-KVLLIDADIGLRNLDLIL------GLENR---IVYTLVDVL-EGE---- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488246763 89 lfkpqVDMSQA-YETPDKEeviidlkdNLDILCGDLNLvlvnkvsDHTFVKR--IRNFVedNELRKIYDYIIIDCP 161
Cdd:cd02036 66 -----CRLEQAlIKDKRWE--------NLYLLPASQTR-------DKDALTPekLEELV--KELKDSFDFILIDSP 119
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
9-216 |
7.76e-05 |
|
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.
Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALLdnykskGYEDPSSeinyyseivlpagkTIYK 88
Cdd:TIGR01969 1 RIITIASGKGGTGKTTITANLGVALAKLGK-KVLALDADITMANLELIL------GMEDKPV--------------TLHD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 LFKPQVDMSQA-YETPDKEEVIIdlkdnldilcGDLNLVLVNKVSdhtfVKRIRNFVedNELRKIYDYIIIDCPPTLTIY 167
Cdd:TIGR01969 60 VLAGEADIKDAiYEGPFGVKVIP----------AGVSLEGLRKAD----PDKLEDVL--KEIIDDTDFLLIDAPAGLERD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488246763 168 TDSALMASDFYLI---PNridrysivgIGSLQKAVQNLIREERINLKCLGLI 216
Cdd:TIGR01969 124 AVTALAAADELLLvvnPE---------ISSITDALKTKIVAEKLGTAILGVV 166
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
17-56 |
1.11e-04 |
|
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.
Pssm-ID: 349754 [Multi-domain] Cd Length: 249 Bit Score: 42.68 E-value: 1.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488246763 17 KGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQAL 56
Cdd:cd02034 8 KGGVGKTTIAALLIRYLAKKGG-KVLAVDADPNSNLAETL 46
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
17-163 |
1.29e-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: 42.49 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 17 KGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQ------FNstQALLDNYKSKGYE-------DPSSEI-NYYSEIVLPa 82
Cdd:cd02035 8 KGGVGKTTIAAATAVRLAEQGK-RVLLVSTDPAhslsdaFG--QKLGGETPVKGAPnlwameiDPEEALeEYWEEVKEL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 83 gktiyklfkpqvdMSQAYETPDKEEVIIDLkdNLDILCGDLNLVLVnkvsdhtfvkRIRNFVEDNElrkiYDYIIIDCPP 162
Cdd:cd02035 84 -------------LAQYLRLPGLDEVYAEE--LLSLPGMDEAAAFD----------ELREYVESGE----YDVIVFDTAP 134
|
.
gi 488246763 163 T 163
Cdd:cd02035 135 T 135
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
9-226 |
1.76e-04 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 41.65 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQfNSTQalldNYKSKGYEDPSSEINYYSeivlpaGKTiyk 88
Cdd:TIGR01007 18 KVLLITSVKPGEGKSTTSANIAIAFAQAGY-KTLLIDGDMR-NSVM----SGTFKSQNKITGLTNFLS------GTT--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 89 lfkpqvDMSQAYETPDKEeviidlkdnldilcgDLNLVLVNKVSDHTFV----KRIRNFVEdnELRKIYDYIIIDCPPtL 164
Cdd:TIGR01007 83 ------DLSDAICDTNIE---------------NLDVITAGPVPPNPTEllqsSNFKTLIE--TLRKRFDYIIIDTPP-I 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488246763 165 TIYTDSALMAS---DFYLI--PNRIDRysivgiGSLQKAVQNLireERINLKCLGLIYTMVNKNLSP 226
Cdd:TIGR01007 139 GTVTDAAIIARacdASILVtdAGKIKK------REVKKAKEQL---EQAGSNFLGVVLNKVDISVSK 196
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
9-47 |
4.38e-04 |
|
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: 38.95 E-value: 4.38e-04
10 20 30
....*....|....*....|....*....|....*....
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDAD 47
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGY-KVLLIDLD 38
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
8-161 |
8.94e-04 |
|
septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]
Pssm-ID: 131023 [Multi-domain] Cd Length: 261 Bit Score: 40.01 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488246763 8 GKIVSVINMKGGVGKTTLSIGLSDFLSDLNNcKVLLIDADPQFNSTQALLdnykskGYEdpsSEINYyseivlpagkTIY 87
Cdd:TIGR01968 1 ARVIVITSGKGGVGKTTTTANLGTALARLGK-KVVLIDADIGLRNLDLLL------GLE---NRIVY----------TLV 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488246763 88 KLFKPQVDMSQAYETPDKEEviidlkdnldilcgdlNLVLV--NKVSDHTFVKR--IRNFVedNELRKIYDYIIIDCP 161
Cdd:TIGR01968 61 DVVEGECRLQQALIKDKRLK----------------NLYLLpaSQTRDKDAVTPeqMKKLV--NELKEEFDYVIIDCP 120
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|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
9-49 |
9.16e-04 |
|
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274549 [Multi-domain] Cd Length: 246 Bit Score: 40.02 E-value: 9.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 488246763 9 KIVSVINMKGGVGKTTLSIGLSDFLSDLNNCkVLLIDADPQ 49
Cdd:TIGR03371 2 KVIAIVSVRGGVGKTTLTANLASALKLLGEP-VLAIDLDPQ 41
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
8-47 |
1.38e-03 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 39.27 E-value: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488246763 8 GKIVSVINMKGGVGKTT----LSIGLSdflsdLNNCKVLLIDAD 47
Cdd:COG2894 2 GKVIVVTSGKGGVGKTTttanLGTALA-----LLGKKVVLIDAD 40
|
|
| |
