|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
141-427 |
6.64e-121 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 355.05 E-value: 6.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 141 GFFAKIArtltTKKLNEKKFEELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRSK-INETITNSLHKSIEELFD 219
Cdd:PRK14974 48 GFFDKAK----ITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEdVEEIVKNALKEALLEVLS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 220 V-KEIDLVQEIKKK-KPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDY 297
Cdd:PRK14974 124 VgDLFDLIEEIKSKgKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 298 GSDPAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDA 377
Cdd:PRK14974 204 GADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGIDG 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1231969908 378 IILSKADIDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:PRK14974 284 VILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKL 333
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
141-421 |
3.36e-100 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 300.79 E-value: 3.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 141 GFFAKIARTLT-TKKLNEkkfeELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRSkinETITNSLHKSIEELFD 219
Cdd:COG0552 15 GLGEKLKSLFSgKKKIDE----DLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDP---EELKEALKEELLEILD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 220 VKEIDLvqEIKKKKPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLaaadtfraaAIDQLQLHADKLGVKLIKHDYGS 299
Cdd:COG0552 88 PVDKPL--AIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLaagdtfraaAIEQLEVWGERVGVPVIAQKEGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 300 DPAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESI 373
Cdd:COG0552 166 DPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKkldpdaPHEVLLVLDATTGQNALSQAKVFNEAV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1231969908 374 QIDAIILSKADIDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFDKE 421
Cdd:COG0552 246 GVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAE 293
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
161-422 |
1.08e-92 |
|
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: 280.68 E-value: 1.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 161 EELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRS-KINETITNSLHKSIEELfDVKEIDLVQEIKKKKPYVICF 239
Cdd:TIGR00064 4 EDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAeKLKEILKEYLKEILKED-LLKNTDLELIVEENKPNVILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 240 VGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAESTGKDV 319
Cdd:TIGR00064 83 VGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNIDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 320 VLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAI 393
Cdd:TIGR00064 163 VLIDTAGRLQNKVNLMDELKKIKRVIKkvdkdaPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGIIL 242
|
250 260
....*....|....*....|....*....
gi 1231969908 394 SISYVTKKPILFLGVGQEYKDLEPFDKER 422
Cdd:TIGR00064 243 SIAYELKLPIKFIGVGEKIDDLAPFDADW 271
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
235-427 |
3.32e-81 |
|
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: 248.64 E-value: 3.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 235 YVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAES 314
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 315 TGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEK 388
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKkkdpeaPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1231969908 389 GGAAISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
234-427 |
4.18e-80 |
|
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: 245.40 E-value: 4.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 234 PYVICFVGINGSGKTTTIAKIANWLKKQG-FSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHA 312
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 313 ESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAA 392
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTAKGGAA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1231969908 393 ISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:smart00962 161 LSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRL 195
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
236-423 |
1.75e-78 |
|
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: 241.29 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAEST 315
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 316 GKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAISI 395
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKGGAALSI 161
|
170 180
....*....|....*....|....*...
gi 1231969908 396 SYVTKKPILFLGVGQEYKDLEPFDKERL 423
Cdd:pfam00448 162 VAETGKPIKFIGVGEKIDDLEPFDPERF 189
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
141-427 |
6.64e-121 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 355.05 E-value: 6.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 141 GFFAKIArtltTKKLNEKKFEELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRSK-INETITNSLHKSIEELFD 219
Cdd:PRK14974 48 GFFDKAK----ITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEdVEEIVKNALKEALLEVLS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 220 V-KEIDLVQEIKKK-KPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDY 297
Cdd:PRK14974 124 VgDLFDLIEEIKSKgKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 298 GSDPAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDA 377
Cdd:PRK14974 204 GADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGIDG 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1231969908 378 IILSKADIDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:PRK14974 284 VILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKL 333
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
141-421 |
3.36e-100 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 300.79 E-value: 3.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 141 GFFAKIARTLT-TKKLNEkkfeELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRSkinETITNSLHKSIEELFD 219
Cdd:COG0552 15 GLGEKLKSLFSgKKKIDE----DLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDP---EELKEALKEELLEILD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 220 VKEIDLvqEIKKKKPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLaaadtfraaAIDQLQLHADKLGVKLIKHDYGS 299
Cdd:COG0552 88 PVDKPL--AIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLaagdtfraaAIEQLEVWGERVGVPVIAQKEGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 300 DPAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESI 373
Cdd:COG0552 166 DPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKkldpdaPHEVLLVLDATTGQNALSQAKVFNEAV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1231969908 374 QIDAIILSKADIDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFDKE 421
Cdd:COG0552 246 GVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAE 293
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
161-422 |
1.08e-92 |
|
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: 280.68 E-value: 1.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 161 EELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRS-KINETITNSLHKSIEELfDVKEIDLVQEIKKKKPYVICF 239
Cdd:TIGR00064 4 EDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAeKLKEILKEYLKEILKED-LLKNTDLELIVEENKPNVILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 240 VGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAESTGKDV 319
Cdd:TIGR00064 83 VGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNIDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 320 VLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAI 393
Cdd:TIGR00064 163 VLIDTAGRLQNKVNLMDELKKIKRVIKkvdkdaPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGIIL 242
|
250 260
....*....|....*....|....*....
gi 1231969908 394 SISYVTKKPILFLGVGQEYKDLEPFDKER 422
Cdd:TIGR00064 243 SIAYELKLPIKFIGVGEKIDDLAPFDADW 271
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
235-427 |
3.32e-81 |
|
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: 248.64 E-value: 3.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 235 YVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAES 314
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 315 TGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEK 388
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKkkdpeaPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1231969908 389 GGAAISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
234-427 |
4.18e-80 |
|
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: 245.40 E-value: 4.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 234 PYVICFVGINGSGKTTTIAKIANWLKKQG-FSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHA 312
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 313 ESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAA 392
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTAKGGAA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1231969908 393 ISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:smart00962 161 LSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRL 195
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
236-423 |
1.75e-78 |
|
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: 241.29 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAEST 315
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 316 GKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAISI 395
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKGGAALSI 161
|
170 180
....*....|....*....|....*...
gi 1231969908 396 SYVTKKPILFLGVGQEYKDLEPFDKERL 423
Cdd:pfam00448 162 VAETGKPIKFIGVGEKIDDLEPFDPERF 189
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
141-421 |
6.44e-73 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 231.53 E-value: 6.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 141 GFFAKIARTLTTKKLNEKKFEELfwdlEIALLENNVAVEVIEKIKQDLKKSLVDKpipRSKINETITNSLHKSIEELFDV 220
Cdd:PRK10416 30 NFGEGINGLFAKKKIDEDLLEEL----EELLIEADVGVETTEEIIEELRERVKRK---NLKDPEELKELLKEELAEILEP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 221 KEIDLvqEIKKKKPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSD 300
Cdd:PRK10416 103 VEKPL--NIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERVGVPVIAQKEGAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 301 PAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAK------PDLKIFVGESITGNDCVEQAKKFNESIQ 374
Cdd:PRK10416 181 PASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKkadpdaPHEVLLVLDATTGQNALSQAKAFHEAVG 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1231969908 375 IDAIILSKADIDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFDKE 421
Cdd:PRK10416 261 LTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAE 307
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
235-419 |
4.32e-71 |
|
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: 222.87 E-value: 4.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 235 YVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAES 314
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 315 TGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQ----------IDAIILSKAD 384
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALAdyspsdnprlIDGIVLTKFD 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1231969908 385 -IDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFD 419
Cdd:cd17876 161 tIDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLN 196
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
235-427 |
1.72e-64 |
|
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: 205.30 E-value: 1.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 235 YVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAES 314
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 315 TGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAIS 394
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAKGGAALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1231969908 395 ISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:cd03115 161 IVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
143-423 |
5.58e-63 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 208.72 E-value: 5.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 143 FAKIARTLTTK-KLNEKKFEELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRS--------KI-NETITNSLHK 212
Cdd:COG0541 9 LQGAFKKLRGKgRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERALGEEVLKSltpgqqviKIvHDELVELLGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 213 SIEELfdvkeidlvqEIKKKKPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKL 292
Cdd:COG0541 89 ENEEL----------NLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 293 IKHDYGSDPAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNES 372
Cdd:COG0541 159 FPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQDAVNVAKAFNEA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1231969908 373 IQIDAIILSKADIDEKGGAAISISYVTKKPILFLGVGQEYKDLEPFDKERL 423
Cdd:COG0541 239 LGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRM 289
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
236-423 |
1.97e-55 |
|
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: 182.03 E-value: 1.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHAEST 315
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 316 GKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAISI 395
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARGGAALSI 161
|
170 180
....*....|....*....|....*...
gi 1231969908 396 SYVTKKPILFLGVGQEYKDLEPFDKERL 423
Cdd:cd18539 162 RHVTGKPIKFIGVGEKIEDLEPFHPDRM 189
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
154-427 |
6.99e-48 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 169.23 E-value: 6.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 154 KLNEKKFEELFWDLEIALLENNVAVE-VIEKIKQDLKKSLVDKPIPRSKINETITNSLHksiEELFDVKEIDLVQEIKKK 232
Cdd:PRK00771 17 RIDEKTVKEVVKDIQRALLQADVNVKlVKELSKSIKERALEEEPPKGLTPREHVIKIVY---EELVKLLGEETEPLVLPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 233 KPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHA 312
Cdd:PRK00771 94 KPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 313 EStgKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAA 392
Cdd:PRK00771 174 KK--ADVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGGGA 251
|
250 260 270
....*....|....*....|....*....|....*
gi 1231969908 393 ISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:PRK00771 252 LSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRL 286
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
235-427 |
1.96e-47 |
|
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: 161.21 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 235 YVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLikhdYGS----DPAAVAFDAIK 310
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPF----YGSytekDPVKIAKEGVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 311 HAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGG 390
Cdd:cd17875 77 KFKKEKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAKGG 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1231969908 391 AAISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:cd17875 157 GALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
155-427 |
7.18e-41 |
|
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: 150.37 E-value: 7.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 155 LNEKKFEELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPrSKINE--TITNSLHKSIEELFDVKEIDLvqEIKKK 232
Cdd:TIGR01425 22 IDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIA-SGINKrkLIQDAVFEELCNLVDPGVEAF--TPKKG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 233 KPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVAFDAIKHA 312
Cdd:TIGR01425 99 KTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 313 ESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAA 392
Cdd:TIGR01425 179 RKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGA 258
|
250 260 270
....*....|....*....|....*....|....*
gi 1231969908 393 ISISYVTKKPILFLGVGQEYKDLEPFDKERLLANL 427
Cdd:TIGR01425 259 LSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
171-424 |
1.18e-26 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 109.95 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 171 LLENNVAVEVIEKIKQDLKKSLVDkpiprskinETITNSLHKSIEELFDVKEIDLVQEIKkkkpyVICFVGINGSGKTTT 250
Cdd:COG1419 115 LLEAGVSPELARELLEKLPEDLSA---------EEAWRALLEALARRLPVAEDPLLDEGG-----VIALVGPTGVGKTTT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 251 IAKIANWLK-KQGFSVVLaaadtfraaaI----------DQLQLHADKLGVKLIKHDygsDPAAVAfDAIkhAESTGKDV 319
Cdd:COG1419 181 IAKLAARFVlRGKKKVAL----------IttdtyrigavEQLKTYARILGVPVEVAY---DPEELK-EAL--ERLRDKDL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 320 VLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFV-GESITGNDCVEQAKKFnESIQIDAIILSKADIDEKGGAAISISYV 398
Cdd:COG1419 245 VLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVlSATTKYEDLKEIVEAF-SSLGLDGLILTKLDETASLGSILNLLIR 323
|
250 260
....*....|....*....|....*..
gi 1231969908 399 TKKPILFLGVGQEY-KDLEPFDKERLL 424
Cdd:COG1419 324 TGLPLSYITNGQRVpEDIEVADPERLA 350
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
236-427 |
2.32e-21 |
|
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: 91.07 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLK-KQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDygsDPAAVAfDAIkhAES 314
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAE---DPEDLA-DAL--ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 315 TGKDVVLIDTAGRIHSNVNLLDEMKKIIRiAKPDLKIFVGESIT--GNDCVEQAKKFnESIQIDAIILSKADIDEKGGAA 392
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKELLG-AGEDIEVHLVLSATtkAKDLKEIIERF-SPLGYRGLILTKLDETTSLGSV 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1231969908 393 ISISYVTKKPILFLGVGQEY-KDLEPFDKERLLANL 427
Cdd:cd17873 154 LSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
184-411 |
3.55e-14 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 73.77 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 184 IKQDLKKSLVDKPIprSKINETITNS-------LHKSIEELFDVKEIDLvqeIKKKKpyVICFVGINGSGKTTTIAKIA- 255
Cdd:PRK05703 171 KRSGLSPEIAEKLL--KLLLEHMPPRertawryLLELLANMIPVRVEDI---LKQGG--VVALVGPTGVGKTTTLAKLAa 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 256 -----NWLKKQGFsvvlaaadtfraaaI----------DQLQLHADKLGVKlIKHDYGSDPAAVAFDAIKHaestgKDVV 320
Cdd:PRK05703 244 ryallYGKKKVAL--------------ItldtyrigavEQLKTYAKIMGIP-VEVVYDPKELAKALEQLRD-----CDVI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 321 LIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITG--NDCVEQAKKFNeSIQIDAIILSKadIDEKG--GAAISIS 396
Cdd:PRK05703 304 LIDTAGRSQRDKRLIEELKALIEFSGEPIDVYLVLSATTkyEDLKDIYKHFS-RLPLDGLIFTK--LDETSslGSILSLL 380
|
250
....*....|....*
gi 1231969908 397 YVTKKPILFLGVGQE 411
Cdd:PRK05703 381 IESGLPISYLTNGQR 395
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
179-419 |
4.31e-14 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 73.84 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 179 EVIEKIKQDLKkslvdkPIPRSKiNETITNSLHKSIEELFDVkEIDLVQEIKKKKPYVICFVGINGSGKTTTIAKI-ANW 257
Cdd:PRK12724 176 EMASKLEERLS------PVDQGR-NHNVTERAVTYLEERVSV-DSDLFSGTGKNQRKVVFFVGPTGSGKTTSIAKLaAKY 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 258 LKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVklikhdygsdPAAVAFDAIKHAESTGKD---VVLIDTAGRIHSNVNL 334
Cdd:PRK12724 248 FLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGM----------PFYPVKDIKKFKETLARDgseLILIDTAGYSHRNLEQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 335 LDEMKKIIRI--AKPDLK-IFVGESITGNDCVEQAKKFNESIQIDAIILSKADIDEKGGAAISISYVTKKPILFLGVGQE 411
Cdd:PRK12724 318 LERMQSFYSCfgEKDSVEnLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQE 397
|
....*...
gi 1231969908 412 YkdlePFD 419
Cdd:PRK12724 398 V----PFD 401
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
217-413 |
2.73e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 68.17 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 217 LFDVKEIDLVQEIKKKKPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHd 296
Cdd:PRK11889 224 LEDMRSHFNTENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAV- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 297 ygSDPAAVAFDAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPD-LKIFVGESITGNDCVEQAKKFNEsIQI 375
Cdd:PRK11889 303 --RDEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDyICLTLSASMKSKDMIEIITNFKD-IHI 379
|
170 180 190
....*....|....*....|....*....|....*...
gi 1231969908 376 DAIILSKADIDEKGGAAISISYVTKKPILFLGVGQEYK 413
Cdd:PRK11889 380 DGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
227-413 |
1.85e-10 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 61.30 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 227 QEIKKKKPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHdygSDPAAVAF 306
Cdd:PRK06731 68 ENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAV---RDEAAMTR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 307 DAIKHAESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPD-LKIFVGESITGNDCVEQAKKFNEsIQIDAIILSKADI 385
Cdd:PRK06731 145 ALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDyICLTLSASMKSKDMIEIITNFKD-IHIDGIVFTKFDE 223
|
170 180
....*....|....*....|....*...
gi 1231969908 386 DEKGGAAISISYVTKKPILFLGVGQEYK 413
Cdd:PRK06731 224 TASSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
236-425 |
3.60e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 61.29 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIkhdYGSDPAAVAfDAIKHAEST 315
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELI---VATSPAELE-EAVQYMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 316 G-KDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGES-ITGNDCVEQAKKFNEsIQIDAIILSKADIDEKGGAAI 393
Cdd:PRK12726 284 NcVDHILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSSgMKSADVMTILPKLAE-IPIDGFIITKMDETTRIGDLY 362
|
170 180 190
....*....|....*....|....*....|..
gi 1231969908 394 SISYVTKKPILFLGVGQEYKDLEPFDKERLLA 425
Cdd:PRK12726 363 TVMQETNLPVLYMTDGQNITENIFRPKSRWLA 394
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
233-357 |
3.65e-10 |
|
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: 58.15 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 233 KPYVICFVGINGSGKTTTIAKIANWLKKQGFSVVLAAADTFRAAAIDQLQLHADKLGvklikhDYGSDPAAVAFDAIKHA 312
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------KASGSGELRLRLALALA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1231969908 313 ESTGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESI 357
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
153-326 |
1.26e-08 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 55.80 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 153 KKLNEKKFEELFW--------DLEIALLENNVAVEVIEKIKQDLKKSLVDkpiprskinETITNSLHKSIEELFDVKeiD 224
Cdd:TIGR03499 117 RELLERLLAGLAWlqrpperaKLYERLLEAGVSEELARELLEKLPEDADA---------EDAWRWLREALEGMLPVK--P 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 225 LVQEIKKKKPYVIcFVGINGSGKTTTIAKIANW--LKKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDygsDPA 302
Cdd:TIGR03499 186 EEDPILEQGGVIA-LVGPTGVGKTTTLAKLAARfaLEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVAR---DPK 261
|
170 180
....*....|....*....|....
gi 1231969908 303 AVAfDAIkhAESTGKDVVLIDTAG 326
Cdd:TIGR03499 262 ELR-EAL--DRLRDKDLILIDTAG 282
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
142-217 |
4.77e-06 |
|
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: 44.08 E-value: 4.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231969908 142 FFAKIARTLTTKKLNEKKFEELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDKPIPRSKINETITNSLHKSIEEL 217
Cdd:smart00963 1 LSKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGEVLKGLTPKQEVKKILKEELVKI 76
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
237-267 |
1.13e-05 |
|
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: 46.11 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|.
gi 1231969908 237 ICFVGINGSGKTTTIAKIANWLKKQGFSVVL 267
Cdd:cd01672 3 IVFEGIDGAGKTTLIELLAERLEARGYEVVL 33
|
|
| Tmk |
COG0125 |
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ... |
237-267 |
2.31e-05 |
|
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 439895 [Multi-domain] Cd Length: 206 Bit Score: 45.15 E-value: 2.31e-05
10 20 30
....*....|....*....|....*....|.
gi 1231969908 237 ICFVGINGSGKTTTIAKIANWLKKQGFSVVL 267
Cdd:COG0125 6 IVFEGIDGSGKSTQIKLLAEYLEARGYDVVL 36
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
153-195 |
3.66e-05 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 41.68 E-value: 3.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1231969908 153 KKLNEKKFEELFWDLEIALLENNVAVEVIEKIKQDLKKSLVDK 195
Cdd:pfam02881 16 GKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGE 58
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
236-414 |
2.19e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 43.44 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLKKQGF--SVVLAAADTFRAAAIDQLQLHADKLGVKLIKHDYGSDPAAVaFDAIKHAE 313
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFAAQHAprDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDL-LERLRDYK 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 314 stgkdVVLIDTAGRIHSNVNLLDEMkKIIRIAKPDLKIFVGESITG-NDCVEQAKKFNeSIQIDAIILSKadIDEKG--G 390
Cdd:PRK12727 431 -----LVLIDTAGMGQRDRALAAQL-NWLRAARQVTSLLVLPANAHfSDLDEVVRRFA-HAKPQGVVLTK--LDETGrfG 501
|
170 180
....*....|....*....|....
gi 1231969908 391 AAISISYVTKKPILFLGVGQEYKD 414
Cdd:PRK12727 502 SALSVVVDHQMPITWVTDGQRVPD 525
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
236-265 |
3.99e-04 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 40.93 E-value: 3.99e-04
10 20 30
....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIANWLKKQGFSV 265
Cdd:COG1763 3 VLGIVGYSGSGKTTLLEKLIPELKARGLRV 32
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
236-424 |
7.43e-04 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 42.10 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 236 VICFVGINGSGKTTTIAKIA-NWLKKQGFS-VVLAAADTFRAAAIDQLQLHADKLGVKLikhdYGSDPAAVAFDAIkhAE 313
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAaRCVAREGADqLALLTTDSFRIGALEQLRIYGRILGVPV----HAVKDAADLRFAL--AA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 314 STGKDVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITGNDC---VEQAKKFNESIQIDAIILSKADIDEKGG 390
Cdd:PRK14723 261 LGDKHLVLIDTVGMSQRDRNVSEQIAMLCGVGRPVRRLLLLNAASHGDTlneVVHAYRHGAGEDVDGCIITKLDEATHLG 340
|
170 180 190
....*....|....*....|....*....|....*
gi 1231969908 391 AAISISYVTKKPILFLGVGQEY-KDLEPFDKERLL 424
Cdd:PRK14723 341 PALDTVIRHRLPVHYVSTGQKVpEHLELAQADELV 375
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
229-410 |
1.69e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 40.27 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 229 IKKKKPYVICFVGINGSGKTTTIAKIANWL----KKQGFSVVLAAADTFRAAAIDQLQLHADKLGVKLikhdygsdPAAV 304
Cdd:PRK12723 169 IDNLKKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPV--------KAIE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969908 305 AFDAIKHAESTGK--DVVLIDTAGRIHSNVNLLDEMKKIIRIAKPDLKIFVGESITG-----NDCVEQAKKFNESiqidA 377
Cdd:PRK12723 241 SFKDLKEEITQSKdfDLVLVDTIGKSPKDFMKLAEMKELLNACGRDAEFHLAVSSTTktsdvKEIFHQFSPFSYK----T 316
|
170 180 190
....*....|....*....|....*....|...
gi 1231969908 378 IILSKADIDEKGGAAISISYVTKKPILFLGVGQ 410
Cdd:PRK12723 317 VIFTKLDETTCVGNLISLIYEMRKEVSYVTDGQ 349
|
|
| PRK13768 |
PRK13768 |
GTPase; Provisional |
234-265 |
2.47e-03 |
|
GTPase; Provisional
Pssm-ID: 237498 [Multi-domain] Cd Length: 253 Bit Score: 39.47 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|..
gi 1231969908 234 PYVICFVGINGSGKTTTIAKIANWLKKQGFSV 265
Cdd:PRK13768 2 MYIVFFLGTAGSGKTTLTKALSDWLEEQGYDV 33
|
|
| DTMP_kinase |
TIGR00041 |
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ... |
237-267 |
4.98e-03 |
|
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 161676 Cd Length: 195 Bit Score: 38.11 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|.
gi 1231969908 237 ICFVGINGSGKTTTIAKIANWLKKQGFSVVL 267
Cdd:TIGR00041 6 IVIEGIDGAGKTTQANLLKKLLQENGYDVLF 36
|
|
| |
