|
Name |
Accession |
Description |
Interval |
E-value |
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
3-216 |
1.89e-21 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 87.98 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLseIPYFECYTDIPAMARKLAARFD 82
Cdd:PHA02518 1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518 79 YVVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 435048952 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
4-215 |
3.68e-20 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 84.14 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 4 IITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLS--EIPYFECYTDIPAMARklaaRF 81
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELPSLAR----DY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 82 DYVFVDTPGMKSPAFVKALSCADILFTFIEPgAGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546 77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 435048952 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
3-164 |
1.61e-16 |
|
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: 72.96 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIkdfieerktndrlseipyfecytdipamarkLAARFD 82
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSL-------------------------------TSWLYD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAGVNPS-MKAWIVLNKCSTNPsdSEASELR 161
Cdd:cd02042 50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSP-FDLDGLAKLLDTLEELKKQLNPPlLILGILLTRVDPRT--KLAREVL 126
|
...
gi 435048952 162 RQL 164
Cdd:cd02042 127 EEL 129
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
3-215 |
2.03e-16 |
|
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: 75.28 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQG---------------SIKDFIEERKTNDRL---SEIPYF 64
Cdd:COG1192 2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnltsglgldpddldpTLYDLLLDDAPLEDAivpTEIPGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 65 ECytdIPA--------------------MARKLAA---RFDYVFVDTPGMKSPAFVKALSCADILFTFIEPGAGiEINTL 121
Cdd:COG1192 82 DL---IPAnidlagaeielvsrpgrelrLKRALAPladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL-SLEGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 122 GRLVFDIKTAQAGVNPSMK-AWIVLNKC--STNPSDSEASELRRQLNDdpdwlPVPRQRIYMRTAHKKAYNGGMGVHEYD 198
Cdd:COG1192 158 AQLLETIEEVREDLNPKLEiLGILLTMVdpRTRLSREVLEELREEFGD-----KVLDTVIPRSVALAEAPSAGKPVFEYD 232
|
250
....*....|....*..
gi 435048952 199 dkRGNKARGEIELLLKE 215
Cdd:COG1192 233 --PKSKGAKAYRALAEE 247
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-147 |
1.92e-08 |
|
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: 52.73 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 5 ITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGS---------------------------IKDFI-EERKTND 56
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssveglegdiapalqalaeglkgrvnLDPILlKEKSDEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 57 RLSEIP-------------YFECYTDIPAMARKLAARFDYVFVDTPGmkSPAF--VKALSCADILFTFIEPGAgIEINTL 121
Cdd:pfam01656 81 GLDLIPgnidlekfekellGPRKEERLREALEALKEDYDYVIIDGAP--GLGEllRNALIAADYVIIPLEPEV-ILVEDA 157
|
170 180
....*....|....*....|....*...
gi 435048952 122 GRLVFDIKTAQAGVNPS--MKAWIVLNK 147
Cdd:pfam01656 158 KRLGGVIAALVGGYALLglKIIGVVLNK 185
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
3-216 |
1.89e-21 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 87.98 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLseIPYFECYTDIPAMARKLAARFD 82
Cdd:PHA02518 1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518 79 YVVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 435048952 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
4-215 |
3.68e-20 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 84.14 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 4 IITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLS--EIPYFECYTDIPAMARklaaRF 81
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELPSLAR----DY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 82 DYVFVDTPGMKSPAFVKALSCADILFTFIEPgAGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546 77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 435048952 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
3-164 |
1.61e-16 |
|
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: 72.96 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIkdfieerktndrlseipyfecytdipamarkLAARFD 82
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSL-------------------------------TSWLYD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAGVNPS-MKAWIVLNKCSTNPsdSEASELR 161
Cdd:cd02042 50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSP-FDLDGLAKLLDTLEELKKQLNPPlLILGILLTRVDPRT--KLAREVL 126
|
...
gi 435048952 162 RQL 164
Cdd:cd02042 127 EEL 129
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
3-215 |
2.03e-16 |
|
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: 75.28 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQG---------------SIKDFIEERKTNDRL---SEIPYF 64
Cdd:COG1192 2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnltsglgldpddldpTLYDLLLDDAPLEDAivpTEIPGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 65 ECytdIPA--------------------MARKLAA---RFDYVFVDTPGMKSPAFVKALSCADILFTFIEPGAGiEINTL 121
Cdd:COG1192 82 DL---IPAnidlagaeielvsrpgrelrLKRALAPladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL-SLEGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 122 GRLVFDIKTAQAGVNPSMK-AWIVLNKC--STNPSDSEASELRRQLNDdpdwlPVPRQRIYMRTAHKKAYNGGMGVHEYD 198
Cdd:COG1192 158 AQLLETIEEVREDLNPKLEiLGILLTMVdpRTRLSREVLEELREEFGD-----KVLDTVIPRSVALAEAPSAGKPVFEYD 232
|
250
....*....|....*..
gi 435048952 199 dkRGNKARGEIELLLKE 215
Cdd:COG1192 233 --PKSKGAKAYRALAEE 247
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-147 |
1.92e-08 |
|
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: 52.73 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 5 ITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGS---------------------------IKDFI-EERKTND 56
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssveglegdiapalqalaeglkgrvnLDPILlKEKSDEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 57 RLSEIP-------------YFECYTDIPAMARKLAARFDYVFVDTPGmkSPAF--VKALSCADILFTFIEPGAgIEINTL 121
Cdd:pfam01656 81 GLDLIPgnidlekfekellGPRKEERLREALEALKEDYDYVIIDGAP--GLGEllRNALIAADYVIIPLEPEV-ILVEDA 157
|
170 180
....*....|....*....|....*...
gi 435048952 122 GRLVFDIKTAQAGVNPS--MKAWIVLNK 147
Cdd:pfam01656 158 KRLGGVIAALVGGYALLglKIIGVVLNK 185
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
4-187 |
2.06e-07 |
|
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.
Pssm-ID: 401181 [Multi-domain] Cd Length: 262 Bit Score: 50.15 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 4 IITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDS-QGSIKDFIEERKTNDRLSEI----PYFECYTDIP------- 71
Cdd:pfam09140 2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATADRTGLslptPEHLNLPDNDvaevpdg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 72 ---------AMARKLAARFDYVFVDTPGMKSPAFVKALSCADILFTFIEpGAGIEINTLGRL---VFDIKtaqagvNPSM 139
Cdd:pfam09140 82 eniddarleEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLN-DSFVDFDLLGQVdpeTFKVK------RPSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 435048952 140 KAWIVLnkcstnpsdsEASELRRQLNDDP-DWLpVPRQRIYMRTAHKKA 187
Cdd:pfam09140 155 YAEMVW----------EARKKRAKADRAPmDWI-VLRNRLGTLEARNKR 192
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
3-114 |
1.53e-06 |
|
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: 47.18 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETD-------------SQGSIKDFIEERKT-NDRLSEIPY----- 63
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSlEDIIVEGPEgldii 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 435048952 64 -----FECYTDIPAMARK--------LAARFDYVFVDTPGMKSPAFVKALSCAD--ILFTFIEPGA 114
Cdd:cd02038 81 pggsgMEELANLDPEQKAklieelssLESNYDYLLIDTGAGISRNVLDFLLAADevIVVTTPEPTS 146
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
2-172 |
3.13e-06 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 47.03 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 2 GKIITVAGHKGGIGKSTVLCSLCV---------CVII-----KGKTACFLETDSQGSIKDFIEERKTNDR---------- 57
Cdd:COG4963 102 GRVIAVVGAKGGVGATTLAVNLAWalaresgrrVLLVdldlqFGDVALYLDLEPRRGLADALRNPDRLDEtlldraltrh 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 58 ------LSEIPYFECYTDIPAMA-----RKLAARFDYVFVDTPGMKSPAFVKALSCADILFTFIEPgagiEINTLGRLVF 126
Cdd:COG4963 182 ssglsvLAAPADLERAEEVSPEAverllDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP----DLPSLRNAKR 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 435048952 127 DIKT-AQAGVNPSmKAWIVLNKCSTNPsDSEASELRRQLNDDPDW-LP 172
Cdd:COG4963 258 LLDLlRELGLPDD-KVRLVLNRVPKRG-EISAKDIEEALGLPVAAvLP 303
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
3-90 |
1.08e-04 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 41.59 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGgIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKdfIEERKTNDRLSEIPYFECYT-----DIpAMARKL 77
Cdd:cd03115 1 NVILLVGLQG-SGKTTTLAKLARYYQEKGKKVLLIAADTFRAAA--VEQLKTLAEKLGVPVFESYTgtdpaSI-AQEAVE 76
|
90
....*....|....*.
gi 435048952 78 AAR---FDYVFVDTPG 90
Cdd:cd03115 77 KAKlegYDVLLVDTAG 92
|
|
| VirC1 |
pfam07015 |
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ... |
3-93 |
2.82e-04 |
|
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.
Pssm-ID: 148565 [Multi-domain] Cd Length: 231 Bit Score: 40.63 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSI---KDFIEERKTNDRLSEI------PYFEcytdiPAM 73
Cdd:pfam07015 2 QLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLtkwRENALRKGTWDPACEIfnadelPLLE-----QAY 76
|
90 100
....*....|....*....|
gi 435048952 74 ARKLAARFDYVFVDTPGMKS 93
Cdd:pfam07015 77 EHAEGSGFDYALADTHGGSS 96
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
2-75 |
7.20e-04 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 39.26 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 2 GKIITVAGHKGgIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIK--------DFIEERKTNDRLSEIPYFECYTDIPAM 73
Cdd:cd01393 1 GKITEIYGPPG-SGKTQLALQLAANALLLGGGVVWIDTEGAFPPSrlvqileaSPSSELELAEALSRLLYFRPPDTLAHL 79
|
..
gi 435048952 74 AR 75
Cdd:cd01393 80 LA 81
|
|
| PRK13849 |
PRK13849 |
conjugal transfer ATPase VirC1; |
3-93 |
1.57e-03 |
|
conjugal transfer ATPase VirC1;
Pssm-ID: 139909 Cd Length: 231 Bit Score: 38.28 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSI---KDFIEERKTNDRLSEI------PYFEcytdiPAM 73
Cdd:PRK13849 2 KLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLtrwKENALRSNTWDPACEVyaadelPLLE-----AAY 76
|
90 100
....*....|....*....|
gi 435048952 74 ARKLAARFDYVFVDTPGMKS 93
Cdd:PRK13849 77 EDAELQGFDYALADTHGGSS 96
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
3-67 |
6.20e-03 |
|
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Pssm-ID: 396792 Cd Length: 302 Bit Score: 36.94 E-value: 6.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 435048952 3 KIITVAGhKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFI------EERKTNDRLS--EI-PYFECY 67
Cdd:pfam02374 2 RWIFFGG-KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFnqkfghEPTKVKENLSamEIdPNMELE 74
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
2-43 |
8.76e-03 |
|
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: 35.64 E-value: 8.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 435048952 2 GKIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQG 43
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG 42
|
|
|