|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
116-421 |
4.94e-179 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 501.55 E-value: 4.94e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 116 EEHKLGWAARLKQGLTKSRDKMAKSLAGVFGGGQIDEDLYEELETVLITSDMGMEATEYLMKDVRDRVSLKGLKDGNELR 195
Cdd:PRK10416 10 KEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEELK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 196 GALKEALYDLIKPLEKPLVLPETKePFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERN 275
Cdd:PRK10416 90 ELLKEELAEILEPVEKPLNIEEKK-PFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 276 NVTVISQTTG-DSAAVCFDAVQAAKARGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQKAMPDAPHEIIVVLDANIGQNA 354
Cdd:PRK10416 169 GVPVIAQKEGaDPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQNA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485354372 355 VNQVKAFDDALGLTGLIVTKLDGTAKGGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDALLD 421
Cdd:PRK10416 249 LSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLG 315
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
122-421 |
4.99e-172 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 482.99 E-value: 4.99e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 122 WAARLKQGLTKSRDKMAKSLAGVFGG-GQIDEDLYEELETVLITSDMGMEATEYLMKDVRDRVSLKGLKDGNELRGALKE 200
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 201 ALYDLIKPLEKPLVLPETKePFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVI 280
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKK-PFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 281 SQTTG-DSAAVCFDAVQAAKARGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQKAMPDAPHEIIVVLDANIGQNAVNQVK 359
Cdd:COG0552 160 AQKEGaDPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485354372 360 AFDDALGLTGLIVTKLDGTAKGGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDALLD 421
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFG 301
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
149-420 |
3.72e-135 |
|
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: 388.54 E-value: 3.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 149 QIDEDLYEELETVLITSDMGMEATEYLMKDVRDRVSLKGLKDGNELRGALKEALYDLIKPLE----KPLVLPETKEPFVI 224
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 225 MLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTG-DSAAVCFDAVQAAKARGI 303
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGaDPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 304 DIVLADTAGRLPTQLHLMEEIKKVKRVLQKAMPDAPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAKGGI 383
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 485354372 384 LAALASDRPVPVRYIGVGESIDDLRPFDARAFVDALL 420
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
222-419 |
2.87e-109 |
|
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: 319.90 E-value: 2.87e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 222 FVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTG-DSAAVCFDAVQAAKA 300
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGaDPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQKAMPDAPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAK 380
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 485354372 381 GGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDAL 419
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
221-421 |
4.15e-95 |
|
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: 283.53 E-value: 4.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 221 PFVIMLAGINGAGKTTSIGKLAKYFQAQG-KSVLLAAGDTFRAAAREQLQAWGER-NNVTVISQTTGDSAAVCFDAVQAA 298
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEIlGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 299 KARGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGT 378
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 485354372 379 AKGGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDALLD 421
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
222-419 |
3.97e-94 |
|
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: 280.97 E-value: 3.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 222 FVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTG-DSAAVCFDAVQAAKA 300
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGaDPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEIKKVKRVLqkampdAPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAK 380
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVV------APDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 485354372 381 GGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDAL 419
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
99-420 |
1.63e-83 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 259.13 E-value: 1.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 99 ETVGEAVGQVQEAVATTEEHKLGWAARLKQGLTKSRDKMAKSLAGVFGGGQIDE----DLYEELETVLITSDMGMEATEY 174
Cdd:PRK14974 7 EKLSKFVEKVEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAKITEIKEkdieDLLEELELELLESDVALEVAEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 175 LMKDVRDRVSLKGLKDGNELRG----ALKEALYDLI---KPLEKPLVLPETKEPFVIMLAGINGAGKTTSIGKLAKYFQA 247
Cdd:PRK14974 87 ILESLKEKLVGKKVKRGEDVEEivknALKEALLEVLsvgDLFDLIEEIKSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 248 QGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTG-DSAAVCFDAVQAAKARGIDIVLADTAGRLPTQLHLMEEIKK 326
Cdd:PRK14974 167 NGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGaDPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 327 VKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAKGGILAALASDRPVPVRYIGVGESIDD 406
Cdd:PRK14974 247 IVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDD 320
|
330
....*....|....
gi 485354372 407 LRPFDARAFVDALL 420
Cdd:PRK14974 321 LIPFDPDWFVDKLL 334
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
222-419 |
3.66e-78 |
|
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: 240.35 E-value: 3.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 222 FVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTG-DSAAVCFDAVQAAKA 300
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGtDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAK 380
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVES------PDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 485354372 381 GGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDAL 419
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
218-421 |
1.82e-70 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 227.98 E-value: 1.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 218 TKEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVI-SQTTGDSAAVCFDAVQ 296
Cdd:COG0541 97 KKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFpEEDGKDPVDIAKRALE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 297 AAKARGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLD 376
Cdd:COG0541 177 YAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLD 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 485354372 377 GTAKGGilAALaSDRPV---PVRYIGVGESIDDLRPFDARAFVDALLD 421
Cdd:COG0541 251 GDARGG--AAL-SIRAVtgkPIKFIGTGEKLDDLEPFHPDRMASRILG 295
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
223-411 |
1.44e-62 |
|
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: 200.13 E-value: 1.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTGDSAA-VCFDAVQAAKAR 301
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVdIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 302 GIDIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAKG 381
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|
gi 485354372 382 GILAALASDRPVPVRYIGVGESIDDLRPFD 411
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFH 185
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
135-420 |
1.35e-59 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 200.05 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 135 DKMAKSLAGVFGGGQIDEDLYEE----LETVLITSDMGMEATEYLMKDVRDRV----SLKGLKDGNELRGALKEALYDLI 206
Cdd:PRK00771 3 ESLRDALKKLAGKSRIDEKTVKEvvkdIQRALLQADVNVKLVKELSKSIKERAleeePPKGLTPREHVIKIVYEELVKLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 207 KPLEKPLVLPetKEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTGD 286
Cdd:PRK00771 83 GEETEPLVLP--LKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 287 saavcfDAVQAAKaRGI------DIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKA 360
Cdd:PRK00771 161 ------DAVEIAK-EGLekfkkaDVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485354372 361 FDDALGLTGLIVTKLDGTAKGG-ILAALASDRpVPVRYIGVGESIDDLRPFDARAFVDALL 420
Cdd:PRK00771 228 FHEAVGIGGIIITKLDGTAKGGgALSAVAETG-APIKFIGTGEKIDDLERFDPDRFISRLL 287
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
222-416 |
8.26e-56 |
|
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: 182.78 E-value: 8.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 222 FVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVI-SQTTGDSAAVCFDAVQAAKA 300
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYgSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAK 380
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 485354372 381 -GGILAALASDRpVPVRYIGVGESIDDLRPFDARAFV 416
Cdd:cd17875 155 gGGALSAVAATG-APIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
136-420 |
7.17e-48 |
|
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: 168.86 E-value: 7.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 136 KMAKSLAGVFGGGQIDED----LYEELETVLITSDMGMEATEYLMKDVRDRVSLKGLKDGNELRGALKEALYD-LIKPLE 210
Cdd:TIGR01425 8 SLVTALRSMSSATVIDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEeLCNLVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 211 --KPLVLPETKEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVI-SQTTGDS 287
Cdd:TIGR01425 88 pgVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYgSYEESDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 288 AAVCFDAVQAAKARGIDIVLADTAGRLPTQLHLMEEIKKVKRVLQkampdaPHEIIVVLDANIGQNAVNQVKAFDDALGL 367
Cdd:TIGR01425 168 VKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 485354372 368 TGLIVTKLDGTAK-GGILAALASDRPvPVRYIGVGESIDDLRPFDARAFVDALL 420
Cdd:TIGR01425 242 GSVIITKLDGHAKgGGALSAVAATKS-PIIFIGTGEHVDEFEIFDAEPFVSKLL 294
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
222-419 |
8.28e-39 |
|
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: 138.52 E-value: 8.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 222 FVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTG-DSAAVCFDAVQAAKA 300
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGkDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEIKKVKRVlqkAMPDApheIIVVLDANIGQNAVNQVKAFDDAL----------GLTGL 370
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKE---NNPDL---VLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 485354372 371 IVTKLDGTA-KGGILAALASDRPVPVRYIGVGESIDDLRPFDARAFVDAL 419
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
95-420 |
6.38e-33 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 126.90 E-value: 6.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 95 EAVAETVGEAVGQVQEAVATTEEHKLgwaARLKQGLTKSRDKMAKSLAGVFGGGQIDEDLYEELETVLItsDMGMEAT-- 172
Cdd:COG1419 51 EDEAEKAPAAAAAPAAASAAAEEEEL---EELRRELAELKELLEEQLSGLAGESARLPPELAELLERLL--EAGVSPEla 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 173 EYLMKDVRDRVslkglkDGNELRGALKEALYDLIKPLEKPLVlpetKEPFVIMLAGINGAGKTTSIGKLA-KYFQAQGKS 251
Cdd:COG1419 126 RELLEKLPEDL------SAEEAWRALLEALARRLPVAEDPLL----DEGGVIALVGPTGVGKTTTIAKLAaRFVLRGKKK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 252 VLLAAGDTFRAAAREQLQAWGERNNVTVIsqttgdsaaVCFDAVQAAKA----RGIDIVLADTAGRLPTQLHLMEEIKKV 327
Cdd:COG1419 196 VALITTDTYRIGAVEQLKTYARILGVPVE---------VAYDPEELKEAlerlRDKDLVLIDTAGRSPRDPELIEELKAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 328 KRVLQkampdaPHEIIVVLDANI-GQNAVNQVKAFDDaLGLTGLIVTKLDGTAKGGILAALASDRPVPVRYIGVGESI-D 405
Cdd:COG1419 267 LDAGP------PIEVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpE 339
|
330
....*....|....*
gi 485354372 406 DLRPFDARAFVDALL 420
Cdd:COG1419 340 DIEVADPERLARLLL 354
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
223-416 |
1.69e-26 |
|
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: 104.94 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLA-KYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVisqttgdsaAVCFDAVQAAKA- 300
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAaRYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPV---------EVAEDPEDLADAl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 ---RGIDIVLADTAGRLPTQLHLMEEIKKvkrvLQKAMPDAphEIIVVLDANI-GQNAVNQVKAFdDALGLTGLIVTKLD 376
Cdd:cd17873 73 erlSDRDLILIDTAGRSPRDKEQLEELKE----LLGAGEDI--EVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 485354372 377 GTAKGGILAALASDRPVPVRYIGVGESI-DDLRPFDARAFV 416
Cdd:cd17873 146 ETTSLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLA 186
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
152-421 |
4.55e-19 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 88.41 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 152 EDLYEELETVLITSDMGMEATEYLMKDVRDrvslkglkDGNELRGALKEALYDLIKPLEKPLVLPETKEPFVIMLAGING 231
Cdd:PRK05703 160 PPEFAELYKRLKRSGLSPEIAEKLLKLLLE--------HMPPRERTAWRYLLELLANMIPVRVEDILKQGGVVALVGPTG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 232 AGKTTSIGKLAKYFQA--QGKSVLLAAGDTFRAAAREQLQAWGERNNVTVIsqttgdsaaVCFDAVQAAKA----RGIDI 305
Cdd:PRK05703 232 VGKTTTLAKLAARYALlyGKKKVALITLDTYRIGAVEQLKTYAKIMGIPVE---------VVYDPKELAKAleqlRDCDV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 306 VLADTAGRLPTQLHLMEEIKKVkrvlqKAMPDAPHEIIVVLDANiGQNAVNQ--VKAFDDaLGLTGLIVTKLDGTAK-GG 382
Cdd:PRK05703 303 ILIDTAGRSQRDKRLIEELKAL-----IEFSGEPIDVYLVLSAT-TKYEDLKdiYKHFSR-LPLDGLIFTKLDETSSlGS 375
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 485354372 383 ILAALASDRpVPVRYIGVGESI-DDLRPFDARAFVDALLD 421
Cdd:PRK05703 376 ILSLLIESG-LPISYLTNGQRVpDDIKVANPEELVRLLLG 414
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
223-421 |
1.97e-15 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 78.11 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAKYFQAQ--GKSVLLAAGDTFRAAAREQLQAWGERNNVTVisqTTGDSAAVCFDAVQaaKA 300
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HEADSAESLLDLLE--RL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAG------RLPTQLHLMEEIKKVKRVLqkampdapheiivVLDANIGQNAVNQVKAFDDALGLTGLIVTK 374
Cdd:PRK12727 427 RDYKLVLIDTAGmgqrdrALAAQLNWLRAARQVTSLL-------------VLPANAHFSDLDEVVRRFAHAKPQGVVLTK 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 485354372 375 LDGTAKGGILAALASDRPVPVRYIGVGESI-DDLRPFDARAFVDALLD 421
Cdd:PRK12727 494 LDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRLED 541
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
111-312 |
5.03e-13 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 68.90 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 111 AVATTEEHKLGWAARLKQGLTKSRDKMAKSLAGVFGGGQIDE--DLYEELEtvlitsDMGMEAT--EYLMKDVRDRvslk 186
Cdd:TIGR03499 94 APAAQAAEPLLPEEELRKELEALRELLERLLAGLAWLQRPPEraKLYERLL------EAGVSEElaRELLEKLPED---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 187 glKDGNELRGALKEALYDLIKplEKPLVLPETKEPFVIMLAGINGAGKTTSIGKLAKYF--QAQGKSVLLAAGDTFRAAA 264
Cdd:TIGR03499 164 --ADAEDAWRWLREALEGMLP--VKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 485354372 265 REQLQAWGERNNVTVIsqttgdsaaVCFDAVQAAKA----RGIDIVLADTAG 312
Cdd:TIGR03499 240 VEQLKTYAEILGIPVK---------VARDPKELREAldrlRDKDLILIDTAG 282
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
134-205 |
3.94e-12 |
|
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: 61.41 E-value: 3.94e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485354372 134 RDKMAKSLAGVFGGGQIDEDLYEELETVLITSDMGMEATEYLMKDVRDRV---SLKGLKDGNELRGALKEALYDL 205
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAkgeVLKGLTPKQEVKKILKEELVKI 76
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
223-411 |
3.07e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 64.60 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLA-KYFQAQGKSVLLAAGDTFRAAAREQLQAWgernnvtvisqttGDSAAVCFDAVQAAK-- 299
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRY-------------ADTMGMPFYPVKDIKkf 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 300 ----AR-GIDIVLADTAGRLPTQLhlmEEIKKVKRVLQKAMPDAPHEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTK 374
Cdd:PRK12724 292 ketlARdGSELILIDTAGYSHRNL---EQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTK 368
|
170 180 190
....*....|....*....|....*....|....*..
gi 485354372 375 LDGTAKGGILAALASDRPVPVRYIGVGESIddlrPFD 411
Cdd:PRK12724 369 LDEADFLGSFLELADTYSKSFTYLSVGQEV----PFD 401
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
223-365 |
4.61e-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: 60.46 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLqawgeRNNVTVISQTTGDSAAVCFDAVQAAKARG 302
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQL-----LLIIVGGKKASGSGELRLRLALALARKLK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485354372 303 IDIVLADTAGRLPTQLHLMEEIKKVKRVLQKAMPDAPHEIIVVldanigqnAVNQVKAFDDAL 365
Cdd:smart00382 79 PDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL--------TTNDEKDLGPAL 133
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
135-202 |
1.45e-10 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 57.09 E-value: 1.45e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485354372 135 DKMAKSLAGVFGGGQIDEDLYEE----LETVLITSDMGMEATEYLMKDVRDR-VSLKGLKDGNELRGALKEAL 202
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLREKaVGEKKLKPPQEVKKILKEEL 75
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
223-409 |
1.05e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 59.75 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTtgdSAAVCFDAVQ-AAKAR 301
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVAT---SPAELEEAVQyMTYVN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 302 GIDIVLADTAGRLPTQLHLMEEIkkvkrvlqKAMPDAPHEIIVVLDANIGQNAVNQVKAFDD--ALGLTGLIVTKLDGTA 379
Cdd:PRK12726 285 CVDHILIDTVGRNYLAEESVSEI--------SAYTDVVHPDLTCFTFSSGMKSADVMTILPKlaEIPIDGFIITKMDETT 356
|
170 180 190
....*....|....*....|....*....|..
gi 485354372 380 KGGILAALASDRPVPVRYIGVGESIDD--LRP 409
Cdd:PRK12726 357 RIGDLYTVMQETNLPVLYMTDGQNITEniFRP 388
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
156-404 |
3.45e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 58.37 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 156 EELETVLITSDMgmeaTEYLMKDVRDRV----SLKGLKDGNELRGALKEALYDLIKpLEKPLVlpETKEPFVIMLAGING 231
Cdd:PRK12723 112 LKIEDILRENDF----SESYIKDINEFIkkefSLSDLDDYDKVRDSVIIYIAKTIK-CSGSII--DNLKKRVFILVGPTG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 232 AGKTTSIGKLAKYF----QAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVisqttgdSAAVCFDAV--QAAKARGIDI 305
Cdd:PRK12723 185 VGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPV-------KAIESFKDLkeEITQSKDFDL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 306 VLADTAGRLPTQLHlmeEIKKVKRVLQKAMPDAphEIIVVLDANIGQNAVNQVKAFDDALGLTGLIVTKLDGTAKGGILA 385
Cdd:PRK12723 258 VLVDTIGKSPKDFM---KLAEMKELLNACGRDA--EFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTKLDETTCVGNLI 332
|
250
....*....|....*....
gi 485354372 386 ALASDRPVPVRYIGVGESI 404
Cdd:PRK12723 333 SLIYEMRKEVSYVTDGQIV 351
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
219-404 |
7.87e-09 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 57.38 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 219 KEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISqtTGDSAAVCFDAVQAA 298
Cdd:PRK11889 239 KEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIA--VRDEAAMTRALTYFK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 299 KARGIDIVLADTAGR-LPTQLHLMEEIKKVKRVlqkampdAPHEIIVVLDANI-GQNAVNQVKAFDDaLGLTGLIVTKLD 376
Cdd:PRK11889 317 EEARVDYILIDTAGKnYRASETVEEMIETMGQV-------EPDYICLTLSASMkSKDMIEIITNFKD-IHIDGIVFTKFD 388
|
170 180
....*....|....*....|....*...
gi 485354372 377 GTAKGGILAALASDRPVPVRYIGVGESI 404
Cdd:PRK11889 389 ETASSGELLKIPAVSSAPIVLMTDGQDV 416
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
223-406 |
9.24e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 53.57 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAK--YFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTGDSAAVCFdavqaAKA 300
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAArcVMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLAL-----AEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEIKkvkrVLQKAmpDAPHEIIVVLDANIGQNAVNQV-KAFDDALG--------LTGLI 371
Cdd:PRK14722 214 RNKHMVLIDTIGMSQRDRTVSDQIA----MLHGA--DTPVQRLLLLNATSHGDTLNEVvQAYRSAAGqpkaalpdLAGCI 287
|
170 180 190
....*....|....*....|....*....|....*.
gi 485354372 372 VTKLDGTAK-GGILAALASDRpVPVRYIGVGESIDD 406
Cdd:PRK14722 288 LTKLDEASNlGGVLDTVIRYK-LPVHYVSTGQKVPE 322
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
219-404 |
1.26e-07 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 52.83 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 219 KEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISqtTGDSAAVCFDAVQAA 298
Cdd:PRK06731 73 KEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIA--VRDEAAMTRALTYFK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 299 KARGIDIVLADTAGRlptQLHLMEEIKKVKRVLQKAMPDApheIIVVLDANI-GQNAVNQVKAFDDaLGLTGLIVTKLDG 377
Cdd:PRK06731 151 EEARVDYILIDTAGK---NYRASETVEEMIETMGQVEPDY---ICLTLSASMkSKDMIEIITNFKD-IHIDGIVFTKFDE 223
|
170 180
....*....|....*....|....*..
gi 485354372 378 TAKGGILAALASDRPVPVRYIGVGESI 404
Cdd:PRK06731 224 TASSGELLKIPAVSSAPIVLMTDGQDV 250
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
223-417 |
5.18e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 52.11 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAKYFQAQ--GKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTtgdSAAVCFDAVQAAKA 300
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCVARegADQLALLTTDSFRIGALEQLRIYGRILGVPVHAVK---DAADLRFALAALGD 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RgiDIVLADTAGRLPTQLHLMEEI-------KKVKRVLqkampdapheiivVLDANIGQNAVNQV-KAF--DDALGLTGL 370
Cdd:PRK14723 264 K--HLVLIDTVGMSQRDRNVSEQIamlcgvgRPVRRLL-------------LLNAASHGDTLNEVvHAYrhGAGEDVDGC 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 485354372 371 IVTKLDGTAKGGILAALASDRPVPVRYIGVGESI-DDLRPFDARAFVD 417
Cdd:PRK14723 329 IITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVD 376
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
223-417 |
2.60e-05 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 46.10 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 223 VIMLAGINGAGKTTSIGKLAK--YFQAQGKSVLLAAGDTFRAAAREQLQAWGERNNVTVISQTTGDSAAVCFDAVqaaka 300
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAAraVIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLHEL----- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 301 RGIDIVLADTAGRLPTQLHLMEEI-------KKVKRVLqkampdapheiivVLDANIGQNAVNQVKAFDDALGLTGLIVT 373
Cdd:PRK14721 268 RGKHMVLIDTVGMSQRDQMLAEQIamlsqcgTQVKHLL-------------LLNATSSGDTLDEVISAYQGHGIHGCIIT 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 485354372 374 KLDGTAKGGILAALASDRPVPVRYIGVGESI-DDLRPFDARAFVD 417
Cdd:PRK14721 335 KVDEAASLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLH 379
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
216-334 |
2.27e-04 |
|
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: 41.96 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 216 PETKEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLaAGDTFRAAAREQLQAWGErNNVTVISQTTGDSAAVCFDAV 295
Cdd:pfam06414 6 TSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELHPHYRELQAA-DPKTASEYTQPDASRWVEKLL 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 485354372 296 QAAKARGIDIVLaDTAGRLPtqlhlmEEIKKVKRVLQKA 334
Cdd:pfam06414 84 QHAIENGYNIIL-EGTLRSP------DVAKKIARALKAA 115
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
221-261 |
6.85e-04 |
|
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: 39.99 E-value: 6.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 485354372 221 PFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGDTFR 261
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. ... |
218-265 |
2.18e-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: 2.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 485354372 218 TKEPFVImLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAgDTFRAAAR 265
Cdd:cd17933 10 LRNRVSV-LTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| Tmk |
COG0125 |
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ... |
228-274 |
2.57e-03 |
|
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: 38.98 E-value: 2.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 485354372 228 GINGAGKTTSIGKLAKYFQAQGKSVLLAA--GDTFRA-AAREQLQAWGER 274
Cdd:COG0125 10 GIDGSGKSTQIKLLAEYLEARGYDVVLTRepGGTPLGeAIRELLLGDNED 59
|
|
| VirC1 |
pfam07015 |
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ... |
231-312 |
4.01e-03 |
|
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.
Pssm-ID: 148565 [Multi-domain] Cd Length: 231 Bit Score: 38.71 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 231 GAGKTTSIGKLAKYFQAQGKSVLLAAGDTFR--AAAREQLQ---AWGERNNVTVisqttGDSAAVCFDAVQAAKARGIDI 305
Cdd:pfam07015 12 GAGKTTALMGLCSALASDGKRVALFEADENRplTKWRENALrkgTWDPACEIFN-----ADELPLLEQAYEHAEGSGFDY 86
|
....*..
gi 485354372 306 VLADTAG 312
Cdd:pfam07015 87 ALADTHG 93
|
|
| MMAA-like |
cd03114 |
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ... |
212-312 |
4.31e-03 |
|
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.
Pssm-ID: 349768 Cd Length: 252 Bit Score: 38.71 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 212 PLVLPETKEPFVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLLAAGD---TFRAAA----REQLQAWGERNNVTVISQTT 284
Cdd:cd03114 37 DALLPQAGRAFRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVDpssPRSGGSilgdKTRMQRLARDPNAFIRPSPS 116
|
90 100 110
....*....|....*....|....*....|..
gi 485354372 285 GDS----AAVCFDAVQAAKARGIDIVLADTAG 312
Cdd:cd03114 117 RGTlggvARATREAILLCEAAGYDVVLVETVG 148
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
222-254 |
4.66e-03 |
|
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: 38.02 E-value: 4.66e-03
10 20 30
....*....|....*....|....*....|...
gi 485354372 222 FVIMLAGINGAGKTTSIGKLAKYFQAQGKSVLL 254
Cdd:cd01672 1 MFIVFEGIDGAGKTTLIELLAERLEARGYEVVL 33
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
231-265 |
5.45e-03 |
|
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: 38.80 E-value: 5.45e-03
10 20 30
....*....|....*....|....*....|....*..
gi 485354372 231 GAGKTTSIGKLAKYFQAQGKSVLLAA--GdtfRAAAR 265
Cdd:COG0507 150 GTGKTTTLRALLAALEALGLRVALAAptG---KAAKR 183
|
|
| PRK13849 |
PRK13849 |
conjugal transfer ATPase VirC1; |
231-312 |
6.35e-03 |
|
conjugal transfer ATPase VirC1;
Pssm-ID: 139909 Cd Length: 231 Bit Score: 37.90 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485354372 231 GAGKTTSIGKLAKYFQAQGKSVLLAAGDTFR--AAAREQLQ---AWGERNNVTVisqttGDSAAVCFDAVQAAKARGIDI 305
Cdd:PRK13849 12 GAGKTTALMGLCAALASDGKRVALFEADENRplTRWKENALrsnTWDPACEVYA-----ADELPLLEAAYEDAELQGFDY 86
|
....*..
gi 485354372 306 VLADTAG 312
Cdd:PRK13849 87 ALADTHG 93
|
|
| |
