|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
13-269 |
2.15e-41 |
|
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: 142.69 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 13 FNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNEkyiNVD 90
Cdd:COG1192 7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLgLDPDDLDPTLYDLLLDdAPLEDAIVPTEIP---GLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 91 LIPSDIQMARFEQELSPLPAREKFLARwYMQNFntLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRGAE 170
Cdd:COG1192 83 LIPANIDLAGAEIELVSRPGRELRLKR-ALAPL--ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE-YLSLEGLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 171 LFKQLWDVDRTYFDKEDNIKSTVLVGFEKKKT---QISDTFDSYLEgfndmrDIMLDTYIRKNEFIEKALLKKLSLTDYt 247
Cdd:COG1192 159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRlsrEVLEELREEFG------DKVLDTVIPRSVALAEAPSAGKPVFEY- 231
|
250 260
....*....|....*....|..
gi 971820185 248 kiTKEHFSRQEFTNMLEELKRK 269
Cdd:COG1192 232 --DPKSKGAKAYRALAEELLER 251
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
7-172 |
2.92e-30 |
|
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: 111.52 E-value: 2.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 7 TKLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSpne 84
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNATSGLgIDKNNVEKTIYELLIGeCNIEEAIIKT--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 85 KYINVDLIPSDIQMARFEQELSPLPAREKFLARwYMQNFNtlSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnIS 164
Cdd:pfam13614 77 VIENLDLIPSNIDLAGAEIELIGIENRENILKE-ALEPVK--DNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE-YY 152
|
....*...
gi 971820185 165 SLRGAELF 172
Cdd:pfam13614 153 ALEGLSQL 160
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
8-182 |
2.18e-13 |
|
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: 65.25 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 8 KLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYVyeinhndnttldilkgisandaivkspnekyi 87
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 88 nvdlipsdiqmarfeqelsplparekflarwymqnfntlseYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKNIsSLR 167
Cdd:cd02042 48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPF-DLD 85
|
170
....*....|....*.
gi 971820185 168 GA-ELFKQLWDVDRTY 182
Cdd:cd02042 86 GLaKLLDTLEELKKQL 101
|
|
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
16-198 |
3.90e-10 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 59.61 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 16 KGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQANLTQY---VYEIN-HNDNTTLDILKGiSANDAIVKSPNEKYINVDL 91
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwVPDLHiHAEDTLLPFYLG-EKDDATYAIKPTCWPGLDI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 92 IPSDIQMARFEQELSP------LPAREKFLARWYMQnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQdkniss 165
Cdd:PRK13705 194 IPSCLALHRIETELMGkfdegkLPTDPHLMLRLAIE--TVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP------ 265
|
170 180 190
....*....|....*....|....*....|....*...
gi 971820185 166 lrgAELFK-----QLWDVDRtyfdkeDNIKSTVLVGFE 198
Cdd:PRK13705 266 ---AELFDytsalQFFDMLR------DLLKNVDLKGFE 294
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
14-158 |
7.52e-06 |
|
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: 46.51 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 14 NIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQ---YVYEINHNDNTTL-------DILKGISandAIVKSPN 83
Cdd:TIGR03453 111 NFKGGSGKTTTAAHLAQYLAL-RGYRVLAIDLDPQASLSAlfgYQPEFDVGENETLygairydDERRPIS---EIIRKTY 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 84 ekYINVDLIPSDIQMARFEQElSPL------PAREKFLARWYMqnfnTLSE----YDYIICDLSPRYDLTAKNVLFLADS 153
Cdd:TIGR03453 187 --FPGLDLVPGNLELMEFEHE-TPRalsrgqGGDTIFFARVGE----ALAEveddYDVVVIDCPPQLGFLTLSALCAATG 259
|
....*
gi 971820185 154 IIIPI 158
Cdd:TIGR03453 260 VLITV 264
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
13-269 |
2.15e-41 |
|
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: 142.69 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 13 FNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNEkyiNVD 90
Cdd:COG1192 7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLgLDPDDLDPTLYDLLLDdAPLEDAIVPTEIP---GLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 91 LIPSDIQMARFEQELSPLPAREKFLARwYMQNFntLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRGAE 170
Cdd:COG1192 83 LIPANIDLAGAEIELVSRPGRELRLKR-ALAPL--ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE-YLSLEGLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 171 LFKQLWDVDRTYFDKEDNIKSTVLVGFEKKKT---QISDTFDSYLEgfndmrDIMLDTYIRKNEFIEKALLKKLSLTDYt 247
Cdd:COG1192 159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRlsrEVLEELREEFG------DKVLDTVIPRSVALAEAPSAGKPVFEY- 231
|
250 260
....*....|....*....|..
gi 971820185 248 kiTKEHFSRQEFTNMLEELKRK 269
Cdd:COG1192 232 --DPKSKGAKAYRALAEELLER 251
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
7-172 |
2.92e-30 |
|
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: 111.52 E-value: 2.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 7 TKLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSpne 84
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNATSGLgIDKNNVEKTIYELLIGeCNIEEAIIKT--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 85 KYINVDLIPSDIQMARFEQELSPLPAREKFLARwYMQNFNtlSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnIS 164
Cdd:pfam13614 77 VIENLDLIPSNIDLAGAEIELIGIENRENILKE-ALEPVK--DNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE-YY 152
|
....*...
gi 971820185 165 SLRGAELF 172
Cdd:pfam13614 153 ALEGLSQL 160
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
14-194 |
3.01e-18 |
|
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: 81.24 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 14 NIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQY---VYEINHNDNTTLDILKG-ISANDAIVKsPNEKYINV 89
Cdd:pfam01656 5 GTKGGVGKTTLAANLARALAR-RGLRVLLIDLDPQSNNSSVeglEGDIAPALQALAEGLKGrVNLDPILLK-EKSDEGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 90 DLIPSDIQMARFEQELSPLPAREKFLArwymqNFNTLSE-YDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRG 168
Cdd:pfam01656 83 DLIPGNIDLEKFEKELLGPRKEERLRE-----ALEALKEdYDYVIIDGAPGLGELLRNALIAADYVIIPLEPE-VILVED 156
|
170 180
....*....|....*....|....*..
gi 971820185 169 AELFKQLW-DVDRTYFDKEDNIKSTVL 194
Cdd:pfam01656 157 AKRLGGVIaALVGGYALLGLKIIGVVL 183
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
8-182 |
2.18e-13 |
|
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: 65.25 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 8 KLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYVyeinhndnttldilkgisandaivkspnekyi 87
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 88 nvdlipsdiqmarfeqelsplparekflarwymqnfntlseYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKNIsSLR 167
Cdd:cd02042 48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPF-DLD 85
|
170
....*....|....*.
gi 971820185 168 GA-ELFKQLWDVDRTY 182
Cdd:cd02042 86 GLaKLLDTLEELKKQL 101
|
|
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
16-198 |
3.90e-10 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 59.61 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 16 KGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQANLTQY---VYEIN-HNDNTTLDILKGiSANDAIVKSPNEKYINVDL 91
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwVPDLHiHAEDTLLPFYLG-EKDDATYAIKPTCWPGLDI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 92 IPSDIQMARFEQELSP------LPAREKFLARWYMQnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQdkniss 165
Cdd:PRK13705 194 IPSCLALHRIETELMGkfdegkLPTDPHLMLRLAIE--TVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP------ 265
|
170 180 190
....*....|....*....|....*....|....*...
gi 971820185 166 lrgAELFK-----QLWDVDRtyfdkeDNIKSTVLVGFE 198
Cdd:PRK13705 266 ---AELFDytsalQFFDMLR------DLLKNVDLKGFE 294
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
23-169 |
5.15e-10 |
|
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: 57.98 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 23 TTSIMTAYELAKdKDKKILLWDLDVQ-ANLTQYvyeINHNDNTTL-DILKG-ISANDAIVKSPNekyiNVDLIPSDIQMA 99
Cdd:COG0455 1 TVAVNLAAALAR-LGKRVLLVDADLGlANLDVL---LGLEPKATLaDVLAGeADLEDAIVQGPG----GLDVLPGGSGPA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971820185 100 RFEqELSPlparekflARWYMQNFNTLSE-YDYIICDLSPryDLTAKNVLFL--ADSIIIPIQDkNISSLRGA 169
Cdd:COG0455 73 ELA-ELDP--------EERLIRVLEELERfYDVVLVDTGA--GISDSVLLFLaaADEVVVVTTP-EPTSITDA 133
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
6-157 |
1.09e-09 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 58.10 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 6 NTKLLTYFNIKGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQANLTQ---YVYEIN-HNDNTTLDILKGISANDAIVKS 81
Cdd:PHA02519 105 NPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMyhgYVPDLHiHADDTLLPFYLGERDNAEYAIK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 82 PNeKYINVDLIPSDIQMARFEQELSPLPAREKF------LARWYMQnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSII 155
Cdd:PHA02519 185 PT-CWPGLDIIPSCLALHRIETDLMQYHDAGKLphpphlMLRAAIE--SVWDNYDIIVIDSAPNLGTGTINVVCAADVIV 261
|
..
gi 971820185 156 IP 157
Cdd:PHA02519 262 VA 263
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
16-156 |
9.84e-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: 51.42 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 16 KGGIYKTTTSIMTAYELAKdKDKKILLWDLDV-QANLtqyvyEI---NHNDNTTLDILKG-ISANDAIVKSPNekyiNVD 90
Cdd:cd02038 9 KGGVGKTNVSANLALALSK-LGKRVLLLDADLgLANL-----DIllgLAPKKTLGDVLKGrVSLEDIIVEGPE----GLD 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971820185 91 LIPSDIQMarfeQELSPLPA--REKFLarwymQNFNTL-SEYDYIICDLSPRydlTAKNVLFL---ADSIII 156
Cdd:cd02038 79 IIPGGSGM----EELANLDPeqKAKLI-----EELSSLeSNYDYLLIDTGAG---ISRNVLDFllaADEVIV 138
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
8-175 |
1.04e-07 |
|
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: 52.04 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 8 KLLTYFNIKGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQA-NLTQYVyeiNHNDNTTL-DILKGISAND------AIV 79
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFgDVALYL---DLEPRRGLaDALRNPDRLDetlldrALT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 80 KSPNekyiNVDLIPSDIQMARFEqELSPLPARE--KFLARwymqnfntlsEYDYIICDLSPRYDLTAKNVLFLADSIIIP 157
Cdd:COG4963 180 RHSS----GLSVLAAPADLERAE-EVSPEAVERllDLLRR----------HFDYVVVDLPRGLNPWTLAALEAADEVVLV 244
|
170 180
....*....|....*....|..
gi 971820185 158 IqDKNISSLRGA----ELFKQL 175
Cdd:COG4963 245 T-EPDLPSLRNAkrllDLLREL 265
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
14-158 |
7.52e-06 |
|
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: 46.51 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 14 NIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQ---YVYEINHNDNTTL-------DILKGISandAIVKSPN 83
Cdd:TIGR03453 111 NFKGGSGKTTTAAHLAQYLAL-RGYRVLAIDLDPQASLSAlfgYQPEFDVGENETLygairydDERRPIS---EIIRKTY 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 84 ekYINVDLIPSDIQMARFEQElSPL------PAREKFLARWYMqnfnTLSE----YDYIICDLSPRYDLTAKNVLFLADS 153
Cdd:TIGR03453 187 --FPGLDLVPGNLELMEFEHE-TPRalsrgqGGDTIFFARVGE----ALAEveddYDVVVIDCPPQLGFLTLSALCAATG 259
|
....*
gi 971820185 154 IIIPI 158
Cdd:TIGR03453 260 VLITV 264
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
8-266 |
2.39e-05 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 45.05 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 8 KLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYVYEINHNDNTTLDILKGISANDAIVKSPNE--- 84
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLAL-QGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTRRPLRDvir 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 85 -KYIN-VDLIPSDIQMARFE----QELSPLPAREKFLARWYMQNFNTLSE-YDYIICDLSPRYDLTAKNVLFLADSIIIP 157
Cdd:PRK13869 201 pTYFDgLHLVPGNLELMEFEhttpKALSDKGTRDGLFFTRVAQAFDEVADdYDVVVIDCPPQLGFLTLSGLCAATSMVIT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 158 I--QDKNISSLRGAELF-KQLWDVDRtyfDKEDNIK----STVLVGFEKK---KTQISDTfdsylegfndMRDiMLDTYI 227
Cdd:PRK13869 281 VhpQMLDIASMSQFLLMtRDLLGVVK---EAGGNLQydfiRYLLTRYEPQdapQTKVAAL----------LRN-MFEDHV 346
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 971820185 228 RKNEFIEKALLKKLSLTDYT--KITKEHFSRQEFTNMLEEL 266
Cdd:PRK13869 347 LTNPMVKSAAVSDAGLTKQTlyEIGRENLTRSTYDRAMESL 387
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
16-138 |
4.46e-05 |
|
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: 44.02 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 16 KGGIYKTTTSIMTAYELAKdKDKKILLWDLDV-QANLTQYvYEInHNDNTTLDILKG-ISANDAIVKSPNEkyiNVDLIP 93
Cdd:COG0489 101 KGGEGKSTVAANLALALAQ-SGKRVLLIDADLrGPSLHRM-LGL-ENRPGLSDVLAGeASLEDVIQPTEVE---GLDVLP 174
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 971820185 94 SDiQMARFEQELSPLPAREKFLARWymqnfntLSEYDYIICDLSP 138
Cdd:COG0489 175 AG-PLPPNPSELLASKRLKQLLEEL-------RGRYDYVIIDTPP 211
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
16-169 |
9.01e-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: 42.57 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 16 KGGIYKTTTSIMTAYELAKdKDKKILLWDLDV-QANLTQYVYEINHNDNTTLDILKG-ISANDAIVKSPNEKyiNVDLIP 93
Cdd:cd02036 9 KGGVGKTTTTANLGVALAK-LGKKVLLIDADIgLRNLDLILGLENRIVYTLVDVLEGeCRLEQALIKDKRWE--NLYLLP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971820185 94 sdIQMARFEQELSPlparEKFLarwymQNFNTLSE-YDYIICDLSPRYDLTAKNVLFLADSIIIpIQDKNISSLRGA 169
Cdd:cd02036 86 --ASQTRDKDALTP----EKLE-----ELVKELKDsFDFILIDSPAGIESGFINAIAPADEAII-VTNPEISSVRDA 150
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
8-161 |
4.30e-04 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 40.60 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 8 KLLTYFNIKGGIYKTTTSIMTAYELAKDkDKKILLWDLDVQANLTQYVYEINHNDnttldilkgisanDAIVKSPNEKYI 87
Cdd:PHA02518 1 KIIAVLNQKGGAGKTTVATNLASWLHAD-GHKVLLVDLDPQGSSTDWAEAREEGE-------------PLIPVVRMGKSI 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971820185 88 NVDLipsdIQMArfeqelsplparekflarwymqnfntlSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDK 161
Cdd:PHA02518 67 RADL----PKVA---------------------------SGYDYVVVDGAPQDSELARAALRIADMVLIPVQPS 109
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
21-156 |
5.61e-04 |
|
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: 39.86 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 21 KTTTSIMTAYELAKDkDKKILLWDLDV-QANLTQYVYEinHNDNTTLDILKGISANDAIVKSPNEKyiNVDLIPSdiqmA 99
Cdd:cd05387 33 KSTVAANLAVALAQS-GKRVLLIDADLrRPSLHRLLGL--PNEPGLSEVLSGQASLEDVIQSTNIP--NLDVLPA----G 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 971820185 100 RFEQELSPLPAREKFLARwymqnFNTLSE-YDYIICDLSPrydltaknVLFLADSIII 156
Cdd:cd05387 104 TVPPNPSELLSSPRFAEL-----LEELKEqYDYVIIDTPP--------VLAVADALIL 148
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
12-138 |
8.66e-04 |
|
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).
Pssm-ID: 275109 [Multi-domain] Cd Length: 566 Bit Score: 40.46 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 12 YFNIKGGIYKTTTSIMTAYELAkDKDKKILLWDLDVQANLTQYVYEINHNDNTTLDILKGISAND----AIVKSPNEKYI 87
Cdd:TIGR04291 7 FFTGKGGVGKTSIACATAINLA-DQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEidpqAAAQAYRARIV 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 971820185 88 NV--DLIPSDIqMARFEQELS-----PLPAREKFLArwYMQNFNTLSEYDYIICDLSP 138
Cdd:TIGR04291 86 DPvrGVLPDDV-VSSIEEQLSgacttEIAAFDEFTG--LLTDAELTQDFDHIIFDTAP 140
|
|
| TadZ-like |
cd17869 |
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ... |
7-178 |
1.92e-03 |
|
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349778 [Multi-domain] Cd Length: 219 Bit Score: 38.67 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 7 TKLLTYFNIKGGIYKTTTSIMTAYELAkDKDKKILLWDLD------------VQANLTQYVYEINHNDNTTLDILkgisa 74
Cdd:cd17869 3 TSVITFHSPCGGSGKSTVAAACAYTLA-EKGKKTLYLNMErlqstdvffgasGRYLMSDHLYTLKSRKANLADKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971820185 75 nDAIVKSPNE--KYINVDLIPSDIQMARFEQElsplpareKFLArwymQNFNTLSEYDYIICDLSPRYDLTAKNVLFLAD 152
Cdd:cd17869 77 -ESCVKQHESgvYYFSPFKSALDILEIKKDDI--------LHMI----TKLVEAHAYDYIIMDLSFEFSSTVCKLLQASH 143
|
170 180
....*....|....*....|....*.
gi 971820185 153 SIIIPIQDKNISSLRGAELFKQLWDV 178
Cdd:cd17869 144 NNVVIALQDANSSYKLNKFLRALEDL 169
|
|
|