|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
41-269 |
3.87e-77 |
|
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: 234.37 E-value: 3.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVDSQGHVGISLGI---EGKRTLYHLMVEGMPLSQCVVAAR-PNLDVLIGDDTLASVEIFLAR 116
Cdd:COG1192 20 VNLAAALARRGKRVLLIDLDPQGNLTSGLGLdpdDLDPTLYDLLLDDAPLEDAIVPTEiPGLDLIPANIDLAGAEIELVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 117 KdEGRDKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNVNQVLLHPISIM 195
Cdd:COG1192 100 R-PGRELRLKRALAPlADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1408134721 196 GILPTFYDMRNNISDESIKTLKGYFHDKVLP-PIRINTRLKEAPRHRQSIFEYAPDSRGASDYQRVVDWVVREHQ 269
Cdd:COG1192 179 GILLTMVDPRTRLSREVLEELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLERLE 253
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
41-184 |
6.04e-38 |
|
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: 131.55 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVDSQGHVGISLGIE---GKRTLYHLMVEGMPLSQCVV-AARPNLDVLIGDDTLASVEIFLAR 116
Cdd:pfam13614 20 VNLAAALAKKGKKVLLIDLDPQGNATSGLGIDknnVEKTIYELLIGECNIEEAIIkTVIENLDLIPSNIDLAGAEIELIG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1408134721 117 KdEGRDKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNV 184
Cdd:pfam13614 100 I-ENRENILKEALEPvKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLNTIKLV 167
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
41-217 |
2.86e-23 |
|
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: 91.83 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVDSQGHVGISLgiegkrtlyhlmvegmplsqcvvaarpnldvligddtlasveiflarkdeg 120
Cdd:cd02042 19 VNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 121 rdkllrkvlhenhdYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNVNQVLLHPISIMGILPT 200
Cdd:cd02042 48 --------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLT 113
|
170
....*....|....*..
gi 1408134721 201 FYDMRNNISDESIKTLK 217
Cdd:cd02042 114 RVDPRTKLAREVLEELK 130
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
25-262 |
2.21e-09 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 57.38 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGHVGISLG------IEGKRTLYHLM---VEGMPLSQCVvaaR 95
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGvlpetdVGANETLYAAIrydDTRRPLRDVI---R 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 96 PN----LDVLIGDDTLASVE---------------IFLARKDEGRDKLlrkvlheNHDYDFILLDCGPSLSLLNMNALTF 156
Cdd:PRK13869 201 PTyfdgLHLVPGNLELMEFEhttpkalsdkgtrdgLFFTRVAQAFDEV-------ADDYDVVVIDCPPQLGFLTLSGLCA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 157 ADHLIVPVSCDFLSLVGVKQVMKTLKNVNQVLLHP-----ISIMGILPTFYDMRNNISDESIKTLKGYFHDKVLP-PIRI 230
Cdd:PRK13869 274 ATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAggnlqYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTnPMVK 353
|
250 260 270
....*....|....*....|....*....|..
gi 1408134721 231 NTRLKEAPRHRQSIFEYAPDSRGASDYQRVVD 262
Cdd:PRK13869 354 SAAVSDAGLTKQTLYEIGRENLTRSTYDRAME 385
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
25-262 |
2.42e-09 |
|
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: 57.30 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGHVGISLGIE------GKRTLYHLM---VEGMPLSQCVVAAR 95
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQpefdvgENETLYGAIrydDERRPISEIIRKTY 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 96 -PNLDVLIGDDTLASVE----IFLARKDEGRDKLLRKV---LHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVS- 165
Cdd:TIGR03453 187 fPGLDLVPGNLELMEFEhetpRALSRGQGGDTIFFARVgeaLAEvEDDYDVVVIDCPPQLGFLTLSALCAATGVLITVHp 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 166 --------CDFLSLVGvkQVMKTLKNVNQVLLHpiSIMGILPTFYDMRNNISDESIKTLKGYFHDKVL-PPIRINTRLKE 236
Cdd:TIGR03453 267 qmldvmsmSQFLLMTG--DLLGVVREAGGNLSY--DFMRYLVTRYEPNDGPQAQMVAFLRSLFGDHVLtNPMLKSTAISD 342
|
250 260
....*....|....*....|....*.
gi 1408134721 237 APRHRQSIFEYAPDSRGASDYQRVVD 262
Cdd:TIGR03453 343 AGLTKQTLYEVERSQFTRSTYDRAME 368
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
25-263 |
1.53e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 50.63 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGhvgiSLgiegkRTLYHLMVEGMPLSqcVVA-ARPNLdvlig 103
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG----SA-----LDWAAAREDERPFP--VVGlARPTL----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 104 DDTLASveifLARkdegrdkllrkvlhenhDYDFILLDCGPSLSLLNMNALTFADHLIVPV---------SCDFLSLVGV 174
Cdd:NF041546 66 HRELPS----LAR-----------------DYDFVVIDGPPRAEDLARSAIKAADLVLIPVqpspydlwaSADTVDLIKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 175 KQVMKTlknvnqvllhpisimGILPTFY----DMRNNISDESIKTLKGYfhdkVLP--PIRINTR--LKEAPRHRQSIFE 246
Cdd:NF041546 125 AREYTP---------------GLKAAFVlnraIARTALGREVAEALAEY----GLPvlKTRIGQRvaFAESAAEGLTVFE 185
|
250
....*....|....*..
gi 1408134721 247 YAPDSRGASDYQRVVDW 263
Cdd:NF041546 186 AEPDGKAAREIRALAKE 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
41-269 |
3.87e-77 |
|
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: 234.37 E-value: 3.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVDSQGHVGISLGI---EGKRTLYHLMVEGMPLSQCVVAAR-PNLDVLIGDDTLASVEIFLAR 116
Cdd:COG1192 20 VNLAAALARRGKRVLLIDLDPQGNLTSGLGLdpdDLDPTLYDLLLDDAPLEDAIVPTEiPGLDLIPANIDLAGAEIELVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 117 KdEGRDKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNVNQVLLHPISIM 195
Cdd:COG1192 100 R-PGRELRLKRALAPlADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1408134721 196 GILPTFYDMRNNISDESIKTLKGYFHDKVLP-PIRINTRLKEAPRHRQSIFEYAPDSRGASDYQRVVDWVVREHQ 269
Cdd:COG1192 179 GILLTMVDPRTRLSREVLEELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLERLE 253
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
41-184 |
6.04e-38 |
|
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: 131.55 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVDSQGHVGISLGIE---GKRTLYHLMVEGMPLSQCVV-AARPNLDVLIGDDTLASVEIFLAR 116
Cdd:pfam13614 20 VNLAAALAKKGKKVLLIDLDPQGNATSGLGIDknnVEKTIYELLIGECNIEEAIIkTVIENLDLIPSNIDLAGAEIELIG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1408134721 117 KdEGRDKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNV 184
Cdd:pfam13614 100 I-ENRENILKEALEPvKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLNTIKLV 167
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
25-244 |
2.31e-25 |
|
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: 100.11 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGHVGISLGIEGKR-----TLYHLMVEGMPLSQCVVAARP--- 96
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIapalqALAEGLKGRVNLDPILLKEKSdeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 97 NLDVLIGDDTLASVEIFLARKDEGrdKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVK 175
Cdd:pfam01656 81 GLDLIPGNIDLEKFEKELLGPRKE--ERLREALEAlKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1408134721 176 QVMKTLKNVNQVL-LHPISIMGILPTFYDMRNNIS--DESIKTLKgyFHDKVLPPIRINTRLKEAPRHRQSI 244
Cdd:pfam01656 159 RLGGVIAALVGGYaLLGLKIIGVVLNKVDGDNHGKllKEALEELL--RGLPVLGVIPRDEAVAEAPARGLPV 228
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
41-217 |
2.86e-23 |
|
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: 91.83 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVDSQGHVGISLgiegkrtlyhlmvegmplsqcvvaarpnldvligddtlasveiflarkdeg 120
Cdd:cd02042 19 VNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 121 rdkllrkvlhenhdYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNVNQVLLHPISIMGILPT 200
Cdd:cd02042 48 --------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLT 113
|
170
....*....|....*..
gi 1408134721 201 FYDMRNNISDESIKTLK 217
Cdd:cd02042 114 RVDPRTKLAREVLEELK 130
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
41-271 |
1.52e-22 |
|
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: 92.65 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVD-SQGHVGISLGIEGKRTLYHLMVEGMPLSQCVVAARPNLDVLIGDDTLASVEIFLARKDe 119
Cdd:COG0455 4 VNLAAALARLGKRVLLVDADlGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAELDPEER- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 120 grdklLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNVnqvllHPISIMGIL 198
Cdd:COG0455 83 -----LIRVLEElERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRR-----LGVRRAGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 199 -------PTFYDMRNNISDESIKTLKGyfHDKVLPPIRINTRLKEAPRHRQSIFEYAPDSRGASDYQRVVDWVVREHQRR 271
Cdd:COG0455 153 vnrvrseAEARDVFERLEQVAERFLGV--RLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGWPVPE 230
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
41-162 |
1.86e-10 |
|
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: 59.51 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALA--GHRVLIIDVD-SQGHVGISLGIEGKRTLYHLMVEGMPLSQCVVAARPNLDVLIGDdtlASVEIFLARK 117
Cdd:cd02038 17 VSANLALALSklGKRVLLLDADlGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGPEGLDIIPGG---SGMEELANLD 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1408134721 118 DEGRDKLLRKVLHENHDYDFILLDCGPSLSllnMNALTF---ADHLIV 162
Cdd:cd02038 94 PEQKAKLIEELSSLESNYDYLLIDTGAGIS---RNVLDFllaADEVIV 138
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
41-182 |
3.96e-10 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 59.36 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALA---GHRVLIIDVDSQ-GHVGISLGIEGKRTLYHLM-----VEGMPLSQCVVAARPNLDVLIGDDTLASVE 111
Cdd:COG4963 119 LAVNLAWALAresGRRVLLVDLDLQfGDVALYLDLEPRRGLADALrnpdrLDETLLDRALTRHSSGLSVLAAPADLERAE 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1408134721 112 IFlarKDEGRDKLLRKVLHEnhdYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLK 182
Cdd:COG4963 199 EV---SPEAVERLLDLLRRH---FDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLR 263
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
41-197 |
8.54e-10 |
|
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: 58.27 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVD-SQGHVGISLGIEGKRTLYHLMVEGMPLSQCVVA-ARPNLDVL-IGDDTLASVEIFLARK 117
Cdd:COG0489 111 ANLALALAQSGKRVLLIDADlRGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPtEVEGLDVLpAGPLPPNPSELLASKR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 118 degrdklLRKVLHE-NHDYDFILLDCGPSLSLLNMNAL-TFADHLIVPVSCDFLSLVGVKQVMKTLKNVNqvllhpISIM 195
Cdd:COG0489 191 -------LKQLLEElRGRYDYVIIDTPPGLGVADATLLaSLVDGVLLVVRPGKTALDDVRKALEMLEKAG------VPVL 257
|
..
gi 1408134721 196 GI 197
Cdd:COG0489 258 GV 259
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
25-262 |
2.21e-09 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 57.38 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGHVGISLG------IEGKRTLYHLM---VEGMPLSQCVvaaR 95
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGvlpetdVGANETLYAAIrydDTRRPLRDVI---R 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 96 PN----LDVLIGDDTLASVE---------------IFLARKDEGRDKLlrkvlheNHDYDFILLDCGPSLSLLNMNALTF 156
Cdd:PRK13869 201 PTyfdgLHLVPGNLELMEFEhttpkalsdkgtrdgLFFTRVAQAFDEV-------ADDYDVVVIDCPPQLGFLTLSGLCA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 157 ADHLIVPVSCDFLSLVGVKQVMKTLKNVNQVLLHP-----ISIMGILPTFYDMRNNISDESIKTLKGYFHDKVLP-PIRI 230
Cdd:PRK13869 274 ATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAggnlqYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTnPMVK 353
|
250 260 270
....*....|....*....|....*....|..
gi 1408134721 231 NTRLKEAPRHRQSIFEYAPDSRGASDYQRVVD 262
Cdd:PRK13869 354 SAAVSDAGLTKQTLYEIGRENLTRSTYDRAME 385
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
25-262 |
2.42e-09 |
|
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: 57.30 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGHVGISLGIE------GKRTLYHLM---VEGMPLSQCVVAAR 95
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQpefdvgENETLYGAIrydDERRPISEIIRKTY 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 96 -PNLDVLIGDDTLASVE----IFLARKDEGRDKLLRKV---LHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPVS- 165
Cdd:TIGR03453 187 fPGLDLVPGNLELMEFEhetpRALSRGQGGDTIFFARVgeaLAEvEDDYDVVVIDCPPQLGFLTLSALCAATGVLITVHp 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 166 --------CDFLSLVGvkQVMKTLKNVNQVLLHpiSIMGILPTFYDMRNNISDESIKTLKGYFHDKVL-PPIRINTRLKE 236
Cdd:TIGR03453 267 qmldvmsmSQFLLMTG--DLLGVVREAGGNLSY--DFMRYLVTRYEPNDGPQAQMVAFLRSLFGDHVLtNPMLKSTAISD 342
|
250 260
....*....|....*....|....*.
gi 1408134721 237 APRHRQSIFEYAPDSRGASDYQRVVD 262
Cdd:TIGR03453 343 AGLTKQTLYEVERSQFTRSTYDRAME 368
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
23-266 |
6.55e-08 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 51.77 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 23 MRIAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGHvgiSLGIEGKRTlyhlmvEGMPLSQCVvaarpnldvli 102
Cdd:PHA02518 1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGS---STDWAEARE------EGEPLIPVV----------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 103 gddtlasveiflarkdeGRDKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALTFADHLIVPV---SCDFLSLVGVKQVM 178
Cdd:PHA02518 61 -----------------RMGKSIRADLPKvASGYDYVVVDGAPQDSELARAALRIADMVLIPVqpsPFDIWAAPDLVELI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 179 KTLKNVNQVlLHPISIMGILPTfydMRNNISDESIKTLKGYfhdkVLPPIRINTR----LKEAPRHRQSIFEYAPDSRGA 254
Cdd:PHA02518 124 KARQEVTDG-LPKFAFIISRAI---KNTQLYREARKALAGY----GLPILRNGTTqrvaYADAAEAGGSVLELPEDDKAA 195
|
250
....*....|..
gi 1408134721 255 SDYQRVVDWVVR 266
Cdd:PHA02518 196 EEIIQLVKELFR 207
|
|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
42-265 |
6.85e-08 |
|
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: 51.96 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 42 ALGTGLALAGHRVLIIDVDSQGHVGISLG--IEGKRTLYHLMVEGMPLSQCVVAARPNLDVL-IGDDTLASVEIFLARKD 118
Cdd:TIGR03371 21 NLASALKLLGEPVLAIDLDPQNLLRLHFGmdWSVRDGWARALLNGADWAAAAYRSPDGVLFLpYGDLSADEREAYQAHDA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 119 EGRDKLLRKVLHENHDYdfILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLKNVNQvllHPISImGIL 198
Cdd:TIGR03371 101 GWLARLLQQLDLAARDW--VLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLALALFAGSG---PRDGP-RFL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1408134721 199 PTFYDMRNNISDESIKTLKGYFHDKVLP-PIRINTRLKEAPRHRQSIFEYAPDSRGASDYQRVVDWVV 265
Cdd:TIGR03371 175 INQFDPARQLSRDVRAVLRQTLGSRLLPfVIHRDEAVSEALARGTPVLNYAPHSQAAHDIRTLAGWLL 242
|
|
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
12-255 |
9.85e-08 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 52.29 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 12 RQRRTQDERgPMRIAVLNQKGGTGKTTTTVALGTGLALAGHRVLIID-VDSQGHVGI------SLGIEGKRTL--YHLMV 82
Cdd:PRK13705 97 RLRRAEDVF-PPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMyhgwvpDLHIHAEDTLlpFYLGE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 83 EGMPLSQCVVAARPNLDVLIGDDTLASVEI-FLARKDEGR-----DKLLRKVLHE-NHDYDFILLDCGPSLSLLNMNALT 155
Cdd:PRK13705 176 KDDATYAIKPTCWPGLDIIPSCLALHRIETeLMGKFDEGKlptdpHLMLRLAIETvAHDYDVIVIDSAPNLGIGTINVVC 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 156 FADHLIVPVSCDFLSLVGVKQVMKTLKNvnqvLLHPISIMGILPtfyDMR-------NNIS------DESIKTLKGYFHD 222
Cdd:PRK13705 256 AADVLIVPTPAELFDYTSALQFFDMLRD----LLKNVDLKGFEP---DVRilltkysNSNGsqspwmEEQIRDAWGSMVL 328
|
250 260 270
....*....|....*....|....*....|...
gi 1408134721 223 KVLppIRINTRLKEAPRHRQSIFEYAPDSRGAS 255
Cdd:PRK13705 329 KNV--VRETDEVGKGQIRMRTVFEQAIDQRSST 359
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
25-263 |
1.53e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 50.63 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 25 IAVLNQKGGTGKTTTTVALGTGLALAGHRVLIIDVDSQGhvgiSLgiegkRTLYHLMVEGMPLSqcVVA-ARPNLdvlig 103
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQG----SA-----LDWAAAREDERPFP--VVGlARPTL----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 104 DDTLASveifLARkdegrdkllrkvlhenhDYDFILLDCGPSLSLLNMNALTFADHLIVPV---------SCDFLSLVGV 174
Cdd:NF041546 66 HRELPS----LAR-----------------DYDFVVIDGPPRAEDLARSAIKAADLVLIPVqpspydlwaSADTVDLIKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 175 KQVMKTlknvnqvllhpisimGILPTFY----DMRNNISDESIKTLKGYfhdkVLP--PIRINTR--LKEAPRHRQSIFE 246
Cdd:NF041546 125 AREYTP---------------GLKAAFVlnraIARTALGREVAEALAEY----GLPvlKTRIGQRvaFAESAAEGLTVFE 185
|
250
....*....|....*..
gi 1408134721 247 YAPDSRGASDYQRVVDW 263
Cdd:NF041546 186 AEPDGKAAREIRALAKE 202
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
37-257 |
7.90e-07 |
|
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: 48.96 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 37 TTTTVALGTGLALAGHRVLIIDVD-SQGHVGISLGIEGKR-TLYHLMVEGMPLSQCVVAARPNLDVLIGDDTLASVeifl 114
Cdd:TIGR01969 15 TTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPvTLHDVLAGEADIKDAIYEGPFGVKVIPAGVSLEGL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 115 aRKdeGRDKLLRKVLHENH-DYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSL---VGVKQVMKTLKnvnqvllh 190
Cdd:TIGR01969 91 -RK--ADPDKLEDVLKEIIdDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSItdaLKTKIVAEKLG-------- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1408134721 191 pISIMG-ILPTFYDMRNNISDESIKTLkgyFHDKVLPPIRINTRLKEAPRHRQSIFEYAPDSRGASDY 257
Cdd:TIGR01969 160 -TAILGvVLNRVTRDKTELGREEIETI---LEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAF 223
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
41-197 |
3.25e-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: 46.41 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALAGHRVLIIDVD-SQGHVGISLGIEGKRTLYHLMVEGMPLSQCV-VAARPNLDVLIGDDTLASVEIFLARKD 118
Cdd:cd05387 38 ANLAVALAQSGKRVLLIDADlRRPSLHRLLGLPNEPGLSEVLSGQASLEDVIqSTNIPNLDVLPAGTVPPNPSELLSSPR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 119 egrdklLRKVLHE-NHDYDFILLDCGPSLSllnmnaltFADHLIVPVSCDFLSLVgVKQVMKTLKNVNQVL----LHPIS 193
Cdd:cd05387 118 ------FAELLEElKEQYDYVIIDTPPVLA--------VADALILAPLVDGVLLV-VRAGKTRRREVKEALerleQAGAK 182
|
....
gi 1408134721 194 IMGI 197
Cdd:cd05387 183 VLGV 186
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
37-162 |
4.21e-06 |
|
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: 46.81 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 37 TTTTVALGTGLALAGHRVLIIDVDsqghVG-----ISLGIEGkRTLYHLMVegmplsqcVVAARPNL-DVLIGDDTLASV 110
Cdd:cd02036 15 TTTTANLGVALAKLGKKVLLIDAD----IGlrnldLILGLEN-RIVYTLVD--------VLEGECRLeQALIKDKRWENL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1408134721 111 EIFLARKDEGRDKL----LRKVLHENHD-YDFILLDCGPSLSLLNMNALTFADHLIV 162
Cdd:cd02036 82 YLLPASQTRDKDALtpekLEELVKELKDsFDFILIDSPAGIESGFINAIAPADEAII 138
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
18-199 |
1.03e-05 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 46.16 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 18 DERGPMRIAVLNQKGGTGKTTTTVALGTGLALAGHRVLIID-VDSQGHVGI------SLGIEGKRTL--YHLMVEGMPLS 88
Cdd:PHA02519 102 DDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMyhgyvpDLHIHADDTLlpFYLGERDNAEY 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 89 QCVVAARPNLDVLIGDDTLASVEIFLAR-KDEGR-----DKLLRKVLHENHD-YDFILLDCGPSLSLLNMNALTFADHLI 161
Cdd:PHA02519 182 AIKPTCWPGLDIIPSCLALHRIETDLMQyHDAGKlphppHLMLRAAIESVWDnYDIIVIDSAPNLGTGTINVVCAADVIV 261
|
170 180 190
....*....|....*....|....*....|....*...
gi 1408134721 162 VPVSCDFLSLVGVKQVMKTLKNvnqvLLHPISIMGILP 199
Cdd:PHA02519 262 VATPAELFDYVSVLQFFTMLLD----LLATVDLGGFEP 295
|
|
| CBP_BcsQ |
pfam06564 |
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ... |
38-263 |
2.20e-05 |
|
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.
Pssm-ID: 429004 [Multi-domain] Cd Length: 234 Bit Score: 44.68 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 38 TTTVALGTGLALAGHRVLIIDVDSQGHVGISLG--IEGKRTLYHLMVEGMPLSQCVVAARPNLDVL-IGDDTLASVEIfL 114
Cdd:pfam06564 17 SILAALAWALQRLGERVLLIDLSPDNLLRLHFNvpFEHRQGWARAELDGADWRDAALEYTPGLDLLpFGRLSVEEQEN-L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 115 ARKDEGRDKLLRKVLHENHDYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSlvgvkqvmktlknvnQVLLHPISi 194
Cdd:pfam06564 96 QQLQPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPDANC---------------HVLLHQQP- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1408134721 195 mgiLPTFYDMRNNISD------ESIKTLKGYFHDKVLP-PIRINTRLKEAPRHRQSIFEYAPDSRGASDYQRVVDW 263
Cdd:pfam06564 160 ---LPDADHLLINDFRpasqlqQDLLQLWRQSQRRLLPlVIHRDEALAEALAAKQPLGEYRPDSLAAEEVLTLANW 232
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
37-162 |
2.37e-03 |
|
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: 38.47 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 37 TTTTVALGTGLALAGHRVLIIDVDsqghVG-----ISLGIEgKRTLYHLMVegmplsqcVVAARPNLD-VLIGDDTLASV 110
Cdd:TIGR01968 16 TTTTANLGTALARLGKKVVLIDAD----IGlrnldLLLGLE-NRIVYTLVD--------VVEGECRLQqALIKDKRLKNL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1408134721 111 EIFLARKDEGRDKLLRKVLHE-----NHDYDFILLDCGPSLSLLNMNALTFADHLIV 162
Cdd:TIGR01968 83 YLLPASQTRDKDAVTPEQMKKlvnelKEEFDYVIIDCPAGIESGFRNAVAPADEAIV 139
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
37-162 |
4.94e-03 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 37.83 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 37 TTTTVALGTGLALAGHRVLIIDVDsqghVGIS-----LGIEgKRTLYHLM--VEGmplsQCvvaarpNLD-VLIGDDTLA 108
Cdd:CHL00175 30 TTTTANLGMSIARLGYRVALIDAD----IGLRnldllLGLE-NRVLYTAMdvLEG----EC------RLDqALIRDKRWK 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 109 SVEIFLARKDEGRDKLLRKVLH------ENHDYDFILLDCGPSLSLLNMNALTFADHLIV 162
Cdd:CHL00175 95 NLSLLAISKNRQRYNVTRKNMNmlvdslKNRGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
41-182 |
7.18e-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: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1408134721 41 VALGTGLALA---GHRVLIIDVDSQ-GHVGISLGIEGKRTLYHLM-----VEGMPLSQCVVAARPNLDVLIGDDTLASVE 111
Cdd:cd03111 17 LAVNLAQELAqraKDKVLLIDLDLPfGDLGLYLNLRPDYDLADVIqnldrLDRTLLDSAVTRHSSGLSLLPAPQELEDLE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1408134721 112 IFLArkdEGRDKLLRKVLHEnhdYDFILLDCGPSLSLLNMNALTFADHLIVPVSCDFLSLVGVKQVMKTLK 182
Cdd:cd03111 97 ALGA---EQVDKLLQVLRAF---YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLLDSLR 161
|
|
| |
