|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
78-379 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 540.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 78 LFARLKSGLSKTRENLASGITTLLIGEKKIDDELLEDLETQLLMADVGIDATTHIITDLTKRLDRNELTDTQKAMEALKE 157
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 158 NLSGLLDPCNIPLEIPETKdPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVV 237
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKK-PFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 238 AQHTGADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAE 317
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055718666 318 QFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALFG 379
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFG 301
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
55-379 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 531.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 55 LFGRKKDKIEknnansnsEKKQGLFARLKSGLSKTRENLASGITTLLiGEKKIDDELLEDLETQLLMADVGIDATTHIIT 134
Cdd:PRK10416 1 FFSWLKKKKK--------EKKEGWFERLKKGLSKTRENFGEGINGLF-AKKKIDEDLLEELEELLIEADVGVETTEEIIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 135 DLTKRLDRNELTDTQKAMEALKENLSGLLDPCNIPLEIPETKdPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAG 214
Cdd:PRK10416 72 ELRERVKRKNLKDPEELKELLKEELAEILEPVEKPLNIEEKK-PFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 215 DTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDN 294
Cdd:PRK10416 151 DTFRAAAIEQLQVWGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 295 TAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFI 374
Cdd:PRK10416 231 DAPHEVLLVLDATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFV 310
|
....*
gi 2055718666 375 EALFG 379
Cdd:PRK10416 311 DALLG 315
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
106-378 |
5.75e-138 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 393.93 E-value: 5.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 106 KIDDELLEDLETQLLMADVGIDATTHIITDLTKRLDRNELTDTQKA----MEALKENLSGLLDPCNIPLEIPETKDPFVI 181
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLkeilKEYLKEILKEDLLKNTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 182 LVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAHGY 261
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 262 DILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGV 341
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 2055718666 342 IFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALF 378
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
179-377 |
5.52e-118 |
|
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.
Pssm-ID: 349783 Cd Length: 199 Bit Score: 340.32 E-value: 5.52e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAK 338
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055718666 339 GGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
178-379 |
2.73e-107 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 313.19 E-value: 2.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 178 PFVILVVGVNGAGKTTTIGKLAKYYQTQG-KSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSA 256
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 257 KAHGYDILIADTAGRLHTQSNLMEELKKVKRVlgkvdnTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGT 336
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRV------IKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2055718666 337 AKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALFG 379
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
179-377 |
4.13e-101 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 297.15 E-value: 4.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVlgkvdnTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAK 338
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRV------VAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055718666 339 GGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
7-69 |
4.15e-05 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 44.27 E-value: 4.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055718666 7 ARLKAEEEARLKAEEEARLKAEEEARLKAEEEARRAEESAKK--VKQGGRLFGRKKDKIEKNNAN 69
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAeeLEELKHLLEERKEALEKLRAE 65
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2-50 |
3.31e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 39.06 E-value: 3.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2055718666 2 KKKQEARLKAEEEARLKAEEEARLKAEEEARLKAEEEARRAEESAKKVK 50
Cdd:TIGR02794 135 KAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKA 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2-50 |
7.47e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 38.25 E-value: 7.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2055718666 2 KKKQEARLKAEEEARLKAEEEARLKAEEEARLKAEEEARRAEESAKKVK 50
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
78-379 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 540.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 78 LFARLKSGLSKTRENLASGITTLLIGEKKIDDELLEDLETQLLMADVGIDATTHIITDLTKRLDRNELTDTQKAMEALKE 157
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 158 NLSGLLDPCNIPLEIPETKdPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVV 237
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKK-PFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 238 AQHTGADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAE 317
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055718666 318 QFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALFG 379
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFG 301
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
55-379 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 531.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 55 LFGRKKDKIEknnansnsEKKQGLFARLKSGLSKTRENLASGITTLLiGEKKIDDELLEDLETQLLMADVGIDATTHIIT 134
Cdd:PRK10416 1 FFSWLKKKKK--------EKKEGWFERLKKGLSKTRENFGEGINGLF-AKKKIDEDLLEELEELLIEADVGVETTEEIIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 135 DLTKRLDRNELTDTQKAMEALKENLSGLLDPCNIPLEIPETKdPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAG 214
Cdd:PRK10416 72 ELRERVKRKNLKDPEELKELLKEELAEILEPVEKPLNIEEKK-PFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 215 DTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDN 294
Cdd:PRK10416 151 DTFRAAAIEQLQVWGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 295 TAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFI 374
Cdd:PRK10416 231 DAPHEVLLVLDATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFV 310
|
....*
gi 2055718666 375 EALFG 379
Cdd:PRK10416 311 DALLG 315
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
106-378 |
5.75e-138 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 393.93 E-value: 5.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 106 KIDDELLEDLETQLLMADVGIDATTHIITDLTKRLDRNELTDTQKA----MEALKENLSGLLDPCNIPLEIPETKDPFVI 181
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLkeilKEYLKEILKEDLLKNTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 182 LVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAHGY 261
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 262 DILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGV 341
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 2055718666 342 IFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALF 378
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
179-377 |
5.52e-118 |
|
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.
Pssm-ID: 349783 Cd Length: 199 Bit Score: 340.32 E-value: 5.52e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAK 338
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055718666 339 GGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
178-379 |
2.73e-107 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 313.19 E-value: 2.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 178 PFVILVVGVNGAGKTTTIGKLAKYYQTQG-KSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSA 256
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 257 KAHGYDILIADTAGRLHTQSNLMEELKKVKRVlgkvdnTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGT 336
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRV------IKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2055718666 337 AKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALFG 379
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
179-377 |
4.13e-101 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 297.15 E-value: 4.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVlgkvdnTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAK 338
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRV------VAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055718666 339 GGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
53-379 |
2.62e-94 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 285.33 E-value: 2.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 53 GRLFGRKKDKIEKNNANSNSEKKQGLFARLKSGlSKTRENLASGITTLLIGEKKIDDeLLEDLETQLLMADVGIDATTHI 132
Cdd:PRK14974 10 SKFVEKVEEKIEEEEEEEAPEAEEEEEEEDEEE-KKEKPGFFDKAKITEIKEKDIED-LLEELELELLESDVALEVAEEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 133 ITDLTKRLD---RNELTDTQKA-MEALKENLSGLLDP---CNIPLEIPETKDPFVILVVGVNGAGKTTTIGKLAKYYQTQ 205
Cdd:PRK14974 88 LESLKEKLVgkkVKRGEDVEEIvKNALKEALLEVLSVgdlFDLIEEIKSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 206 GKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKV 285
Cdd:PRK14974 168 GFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 286 KRVlgkvdnTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDL 365
Cdd:PRK14974 248 VRV------TKPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDL 321
|
330
....*....|....
gi 2055718666 366 RPFKSDEFIEALFG 379
Cdd:PRK14974 322 IPFDPDWFVDKLLG 335
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
179-377 |
3.14e-89 |
|
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: 266.93 E-value: 3.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVlgkvdnTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAK 338
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055718666 339 GGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
79-374 |
4.58e-78 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 246.47 E-value: 4.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 79 FARLKSGLSKTRENLAsgittlliGEKKID----DELLEDLETQLLMADVGIDatthIITDLTKRLdrneltdTQKAMEA 154
Cdd:COG0541 2 FENLSERLQGAFKKLR--------GKGRLTeeniKEALREVRRALLEADVNLK----VVKDFIERV-------KERALGE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 155 ---------------LKENLSGLLDPCNIPLEIPETKdPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRA 219
Cdd:COG0541 63 evlksltpgqqvikiVHDELVELLGGENEELNLAKKP-PTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 220 AAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKRVLgkvdntAPHE 299
Cdd:COG0541 142 AAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAV------NPDE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055718666 300 VLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFI 374
Cdd:COG0541 216 TLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMA 290
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
180-371 |
1.93e-73 |
|
GTPase domain of signal recognition particle protein; 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 cognated 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: 349786 Cd Length: 193 Bit Score: 226.71 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKAH 259
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 260 GYDILIADTAGRLHTQSNLMEELKKVKRVLGkvdntaPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKG 339
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|..
gi 2055718666 340 GVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSD 371
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
82-379 |
5.36e-63 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 207.75 E-value: 5.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 82 LKSGLSKTRENLASGITtllIGEKKIDdELLEDLETQLLMADVGIDatthIITDLTKRLDRNELT-DTQKAMEA------ 154
Cdd:PRK00771 1 LGESLRDALKKLAGKSR---IDEKTVK-EVVKDIQRALLQADVNVK----LVKELSKSIKERALEeEPPKGLTPrehvik 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 155 -LKENLSGLLDPCNIPLEIPetKDPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERND 233
Cdd:PRK00771 73 iVYEELVKLLGEETEPLVLP--LKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 234 IPVVAQHTGADSASVIFDAHNSAKahGYDILIADTAGRLHTQSNLMEELKKVKRVlgkvdnTAPHEVLLVLDSGTGQNAI 313
Cdd:PRK00771 151 VPFYGDPDNKDAVEIAKEGLEKFK--KADVIIVDTAGRHALEEDLIEEMKEIKEA------VKPDEVLLVIDATIGQQAK 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055718666 314 NQAEQFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALFG 379
Cdd:PRK00771 223 NQAKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLLG 288
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
179-377 |
6.81e-60 |
|
GTPase domain of the signal recognition 54 kDa subunit; 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 cognated 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: 349784 Cd Length: 193 Bit Score: 192.02 E-value: 6.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVLgkvdntAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAK 338
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAV------KPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055718666 339 GGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
87-379 |
1.41e-51 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 177.72 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 87 SKTRENLASgITTLLIGEKKIDDELLEDLETQLLMADVGIDATTHIITDLTKRLDRNELTDT----QKAMEALKENLSGL 162
Cdd:TIGR01425 7 SSLVTALRS-MSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGinkrKLIQDAVFEELCNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 163 LDPcNIPLEIPETKDPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTG 242
Cdd:TIGR01425 86 VDP-GVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 243 ADSASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKrvlgkvDNTAPHEVLLVLDSGTGQNAINQAEQFHQA 322
Cdd:TIGR01425 165 SDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVR------EAIKPDSIIFVMDGSIGQAAFGQAKAFKDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055718666 323 VNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEALFG 379
Cdd:TIGR01425 239 VEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLG 295
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
179-377 |
3.37e-42 |
|
C-terminal domain of signal recognition particle receptor alpha subunit; The signal-recognition particle (SRP) receptor (SR) alpha-subunit (SRalpha) of the eukaryotic SR interacts with the signal-recognition particle (SRP) and is essential for the co-translational membrane targeting of proteins.
Pssm-ID: 349785 Cd Length: 204 Bit Score: 146.61 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSAKA 258
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVkrvlgkVDNTAPHEVLLVLDSGTGQNAINQAEQFHQAV----------NVSGI 328
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKL------IKENNPDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055718666 329 VMTKLDGTA-KGGVIFAIAKKMKLPIRYIGVGEKIDDLRPFKSDEFIEAL 377
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
45-379 |
2.43e-40 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 146.16 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 45 SAKKVKQGGRLFG------------RKKDKIEKNNANSNSEKKQGLFARLKSGLSKTRENLaSGITTLLIGEKKIDDELL 112
Cdd:COG1419 30 STRKVKKGGFLKKvevtaavdedeaEKAPAAAAAPAAASAAAEEEELEELRRELAELKELL-EEQLSGLAGESARLPPEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 113 EDLETQLLmaDVGIDATthIITDLTKRLdrNELTDTQKAMEALKENLSGLLDPCNIPLeipeTKDPFVILVVGVNGAGKT 192
Cdd:COG1419 109 AELLERLL--EAGVSPE--LARELLEKL--PEDLSAEEAWRALLEALARRLPVAEDPL----LDEGGVIALVGPTGVGKT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 193 TTIGKLA-KYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIfdahnsAKAHGYDILIADTAGR 271
Cdd:COG1419 179 TTIAKLAaRFVLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 272 LHTQSNLMEELKKVKRVLGKVdntaphEVLLVLDSGT-GQNAINQAEQFhQAVNVSGIVMTKLDGTAKGGVIFAIAKKMK 350
Cdd:COG1419 253 SPRDPELIEELKALLDAGPPI------EVYLVLSATTkYEDLKEIVEAF-SSLGLDGLILTKLDETASLGSILNLLIRTG 325
|
330 340 350
....*....|....*....|....*....|
gi 2055718666 351 LPIRYIGVGEKI-DDLRPFKSDEFIEALFG 379
Cdd:COG1419 326 LPLSYITNGQRVpEDIEVADPERLARLLLG 355
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
180-377 |
8.11e-32 |
|
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that 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 cognated receptor (SR).
Pssm-ID: 349782 [Multi-domain] Cd Length: 189 Bit Score: 118.81 E-value: 8.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAKYYQ-TQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIfdahnsAKA 258
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADAL------ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 259 HGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVdntaphEVLLVLDSGT-GQNAINQAEQFhQAVNVSGIVMTKLDGTA 337
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKELLGAGEDI------EVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDETT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055718666 338 KGGVIFAIAKKMKLPIRYIGVGEKI-DDLRPFKSDEFIEAL 377
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
2-379 |
2.02e-25 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 106.52 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 2 KKKQEARLKAEEEARLKAEEEARLKAE-EEARLKAEEEARRAEESAKKVKQGGRLFGRKKDKIEKNNANSNSEKKQGLFA 80
Cdd:PRK05703 54 DETPKKNPVLREEKRKPAKSILSLQALlEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 81 RLK---SGLSKTRENLASGIttlliGEKKIDDELLEDLETQLLmaDVGIDAttHIITDLTKRLDRNELTDTQKAMEALKE 157
Cdd:PRK05703 134 ELRdelKELKNLLEDQLSGL-----RQVERIPPEFAELYKRLK--RSGLSP--EIAEKLLKLLLEHMPPRERTAWRYLLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 158 NLSGLLDPCNIPLEIPETkdpfVILVVGVNGAGKTTTIGKLA-KYYQTQG-KSVMLAAGDTFRAAAVEQLQVWGERNDIP 235
Cdd:PRK05703 205 LLANMIPVRVEDILKQGG----VVALVGPTGVGKTTTLAKLAaRYALLYGkKKVALITLDTYRIGAVEQLKTYAKIMGIP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 236 VVAQHTGADSASVIfDAHNSakahgYD-ILIaDTAGRLHTQSNLMEELKKVkrvlgkVDNT-APHEVLLVLdSGTGQN-- 311
Cdd:PRK05703 281 VEVVYDPKELAKAL-EQLRD-----CDvILI-DTAGRSQRDKRLIEELKAL------IEFSgEPIDVYLVL-SATTKYed 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055718666 312 --AInqAEQFhQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKI-DDLRPFKSDEFIEALFG 379
Cdd:PRK05703 347 lkDI--YKHF-SRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLLLG 414
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
90-368 |
3.00e-17 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 82.70 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 90 RENLASGITTLLIGEKkidDELLEDLETQLLMADVGIDATTHIITDLTKRLDRNELTD----TQKAMEALKENLSglLDP 165
Cdd:PRK12724 138 KNSFLESETTIVRKEK---DSPLQRLGERLVREGMSQSYVEEMASKLEERLSPVDQGRnhnvTERAVTYLEERVS--VDS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 166 cNIPLEIPETKDPfVILVVGVNGAGKTTTIGKLA-KYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAqhtgad 244
Cdd:PRK12724 213 -DLFSGTGKNQRK-VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYP------ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 245 sASVIFDAHNSAKAHGYDILIADTAGRLHTQSNLMEELKKVKRVLGKVDNTaphEVLLVLDSGTGQNAINQAEQFHQAVN 324
Cdd:PRK12724 285 -VKDIKKFKETLARDGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSV---ENLLVLSSTSSYHHTLTVLKAYESLN 360
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2055718666 325 VSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIddlrPF 368
Cdd:PRK12724 361 YRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQEV----PF 400
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
12-270 |
5.90e-17 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 80.07 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 12 EEEARLKAEEEARLKAEEEARLKAEEEARRAEEsakkvkqggrlfgRKKDKIEKNNANSNSEKKQGLFARLKSGLSKTRE 91
Cdd:TIGR03499 52 EEEAAAASAEEEASKALEQADPKPLSATAEPLE-------------LPAPQEEPAAPAAQAAEPLLPEEELRKELEALRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 92 NLASGITTLligEKKIDDELLEDLETQLLMAdvGIDATthIITDLTKRLDrnELTDTQKAMEALKENLSGLLDpcNIPLE 171
Cdd:TIGR03499 119 LLERLLAGL---AWLQRPPERAKLYERLLEA--GVSEE--LARELLEKLP--EDADAEDAWRWLREALEGMLP--VKPEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 172 IPETKDPFVILVVGVNGAGKTTTIGKLAKYY--QTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVI 249
Cdd:TIGR03499 188 DPILEQGGVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKELREAL 267
|
250 260
....*....|....*....|.
gi 2055718666 250 fDAHNsakahGYDILIADTAG 270
Cdd:TIGR03499 268 -DRLR-----DKDLILIDTAG 282
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
177-365 |
5.81e-15 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 76.18 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 177 DPF----VILVVGVNGAGKTTTIGKLAKYYQTQ--GKSVMLAAGDTFRAAAVEQLQVWGERNDIPVvaqHTgADSASVIF 250
Cdd:PRK12727 345 DPLerggVIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAESLL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 251 DAHNSAKahGYDILIADTAGRLHTQSNLMEELKKVKrvlgkvdntAPHEV--LLVLDSGTGQNAINQAEQFHQAVNVSGI 328
Cdd:PRK12727 421 DLLERLR--DYKLVLIDTAGMGQRDRALAAQLNWLR---------AARQVtsLLVLPANAHFSDLDEVVRRFAHAKPQGV 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 2055718666 329 VMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKI-DDL 365
Cdd:PRK12727 490 VLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDL 527
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
180-378 |
1.04e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 72.53 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLA-KYYQTQGKS-VMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIfdahnsAK 257
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAaRCVAREGADqLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAADLRFAL------AA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 258 AHGYDILIADTAGRLHTQSNLMEEL-------KKVKRVLgkVDNTAPHevllvldsGTGQNAINQAEQFHQAVNVSGIVM 330
Cdd:PRK14723 261 LGDKHLVLIDTVGMSQRDRNVSEQIamlcgvgRPVRRLL--LLNAASH--------GDTLNEVVHAYRHGAGEDVDGCII 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055718666 331 TKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKI-DDLRPFKSDEFIEALF 378
Cdd:PRK14723 331 TKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
127-362 |
4.74e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 66.85 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 127 DATTHIITDLTKRLDRNELTDTQKAMEALKENLSGLLDPcNIPLEIPETKD--PFVILVVGVNGAGKTTTIGKLAKYY-- 202
Cdd:PRK12723 122 DFSESYIKDINEFIKKEFSLSDLDDYDKVRDSVIIYIAK-TIKCSGSIIDNlkKRVFILVGPTGVGKTTTIAKLAAIYgi 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 203 --QTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNsakahgYDILIADTAGRlhTQSNLMe 280
Cdd:PRK12723 201 nsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQSKD------FDLVLVDTIGK--SPKDFM- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 281 ELKKVKRVLGKVDNTAphEVLLVLDSGTGQNAINqaEQFHQ--AVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGV 358
Cdd:PRK12723 272 KLAEMKELLNACGRDA--EFHLAVSSTTKTSDVK--EIFHQfsPFSYKTVIFTKLDETTCVGNLISLIYEMRKEVSYVTD 347
|
....
gi 2055718666 359 GEKI 362
Cdd:PRK12723 348 GQIV 351
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
180-379 |
1.06e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 65.91 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIfdaHNSAKAH 259
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVATSPAELEEAV---QYMTYVN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 260 GYDILIADTAGRlhtqsNLMEElKKVKRVLGKVDNTAPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTAKG 339
Cdd:PRK12726 285 CVDHILIDTVGR-----NYLAE-ESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTRI 358
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2055718666 340 GVIFAIAKKMKLPIRYIGVGEKIDD--LRPfKSDEFIEALFG 379
Cdd:PRK12726 359 GDLYTVMQETNLPVLYMTDGQNITEniFRP-KSRWLAERFVG 399
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
90-163 |
1.11e-11 |
|
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species.
Pssm-ID: 214941 [Multi-domain] Cd Length: 77 Bit Score: 59.87 E-value: 1.11e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055718666 90 RENLASGITTLLIGEKkIDDELLEDLETQLLMADVGIDATTHIITDLTKRLDR---NELTDTQKAMEALKENLSGLL 163
Cdd:smart00963 2 SKALGKLLGELFLTEK-DDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
180-291 |
2.24e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.24 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVwgerndIPVVAQHTGADSASVIFDAHNSAKAH 259
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALARKL 77
|
90 100 110
....*....|....*....|....*....|..
gi 2055718666 260 GYDILIADTAGRLHTQSNLMEELKKVKRVLGK 291
Cdd:smart00382 78 KPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
180-364 |
9.17e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 62.82 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAK--YYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNSak 257
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAArcVMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLALAELRNK-- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 258 ahgyDILIADTAGRLHTQSNLMEELKkvkrVLGKVDNtaPHEVLLVLDSGTGQNAINQAEQFHQAV---------NVSGI 328
Cdd:PRK14722 217 ----HMVLIDTIGMSQRDRTVSDQIA----MLHGADT--PVQRLLLLNATSHGDTLNEVVQAYRSAagqpkaalpDLAGC 286
|
170 180 190
....*....|....*....|....*....|....*.
gi 2055718666 329 VMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKIDD 364
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
148-362 |
4.41e-10 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 59.76 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 148 TQKAMEALKENLSGLLDPCNIpleipETKDPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQV 227
Cdd:PRK06731 50 TEEVIEYILEDMSSHFNTENV-----FEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 228 WGERNDIPVVAQHTGADSASVIFDAHNSAKAhgyDILIADTAGRLHTQSNLMEELKKvkrVLGKVDntaPHEVLLVLDSG 307
Cdd:PRK06731 125 YVKTIGFEVIAVRDEAAMTRALTYFKEEARV---DYILIDTAGKNYRASETVEEMIE---TMGQVE---PDYICLTLSAS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2055718666 308 TGQNAINQAEQFHQAVNVSGIVMTKLDGTAKGGVIFAIAKKMKLPIRYIGVGEKI 362
Cdd:PRK06731 196 MKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDV 250
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
176-362 |
1.12e-09 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 59.69 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 176 KDPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFRAAAVEQLQVWGERNDIPVVAQHTGADSASVIFDAHNS 255
Cdd:PRK11889 239 KEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 256 AKAhgyDILIADTAGRLHTQSNLMEELKKvkrVLGKVDntaPHEVLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDG 335
Cdd:PRK11889 319 ARV---DYILIDTAGKNYRASETVEEMIE---TMGQVE---PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDE 389
|
170 180
....*....|....*....|....*..
gi 2055718666 336 TAKGGVIFAIAKKMKLPIRYIGVGEKI 362
Cdd:PRK11889 390 TASSGELLKIPAVSSAPIVLMTDGQDV 416
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
93-159 |
6.98e-09 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 52.08 E-value: 6.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055718666 93 LASGITTL---LIGEKKIDDELLED----LETQLLMADVGIDATTHIITDLTKR-LDRNELTDTQKAMEALKENL 159
Cdd:pfam02881 1 LGEKLSSLfkgLRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLREKaVGEKKLKPPQEVKKILKEEL 75
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
180-378 |
2.02e-06 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 49.56 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLA-KYYQTQGKS-VMLAAGDTFRAAAVEQLQVWGErndIPVVAQHTGADSASVIFDAHNSAK 257
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAaRAVIRHGADkVALLTTDSYRIGGHEQLRIYGK---LLGVSVRSIKDIADLQLMLHELRG 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 258 AHgydILIADTAGRLHTQSNLMEELKKVKRVLGKVDNtaphevLLVLDSGTGQNAINQAEQFHQAVNVSGIVMTKLDGTA 337
Cdd:PRK14721 270 KH---MVLIDTVGMSQRDQMLAEQIAMLSQCGTQVKH------LLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2055718666 338 KGGVIFAIAKKMKLPIRYIGVGEKI-DDLRPFKSDEFIEALF 378
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
7-69 |
4.15e-05 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 44.27 E-value: 4.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055718666 7 ARLKAEEEARLKAEEEARLKAEEEARLKAEEEARRAEESAKK--VKQGGRLFGRKKDKIEKNNAN 69
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAeeLEELKHLLEERKEALEKLRAE 65
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
180-282 |
1.31e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 43.81 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAA--GdtfRAAAVeqLQvwgERNDIPV--VAQHTGADSASVIFDAHNS 255
Cdd:COG0507 142 VSVLTGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKR--LS---ESTGIEArtIHRLLGLRPDSGRFRHNRD 213
|
90 100
....*....|....*....|....*..
gi 2055718666 256 AKAHGYDILIADTAGRLHTQsnLMEEL 282
Cdd:COG0507 214 NPLTPADLLVVDEASMVDTR--LMAAL 238
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
179-238 |
7.21e-04 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 40.33 E-value: 7.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055718666 179 FVILVVGVNGAGKTTTIGKLAKYYQTQGKSVML--AAGDTFRAAAVEQLQVWGERNDIPVVA 238
Cdd:cd01672 1 MFIVFEGIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
178-218 |
1.14e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 39.22 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2055718666 178 PFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAGDTFR 218
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
175-222 |
2.12e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 38.30 E-value: 2.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2055718666 175 TKDPFVILVvGVNGAGKTTTIGKLAKYYQTQGKSVMLAAgDTFRAAAV 222
Cdd:cd17933 10 LRNRVSVLT-GGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
180-222 |
2.34e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 38.70 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2055718666 180 VILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLAAgDTFRAAAV 222
Cdd:pfam13604 20 VAVLVGPAGTGKTTALKALREAWEAAGYRVIGLA-PTGRAAKV 61
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
173-284 |
2.67e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.50 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055718666 173 PETKDPFVILVVGVNGAGKTTTIGKLAKYYQTQGKSVMLaAGDTFRAAAVEQLQVwgERNDIPVVAQHTGADSASVIFDA 252
Cdd:pfam06414 6 TSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELHPHYREL--QAADPKTASEYTQPDASRWVEKL 82
|
90 100 110
....*....|....*....|....*....|..
gi 2055718666 253 HNSAKAHGYDILIADTAGRLHTQSNLMEELKK 284
Cdd:pfam06414 83 LQHAIENGYNIILEGTLRSPDVAKKIARALKA 114
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2-50 |
3.31e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 39.06 E-value: 3.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2055718666 2 KKKQEARLKAEEEARLKAEEEARLKAEEEARLKAEEEARRAEESAKKVK 50
Cdd:TIGR02794 135 KAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKA 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2-50 |
7.47e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 38.25 E-value: 7.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2055718666 2 KKKQEARLKAEEEARLKAEEEARLKAEEEARLKAEEEARRAEESAKKVK 50
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
180-215 |
7.71e-03 |
|
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: 35.87 E-value: 7.71e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2055718666 180 VILVVG-VNGAGKTTTIGKLAKYYQTQGKSVMLAAGD 215
Cdd:cd01983 2 VIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| |
