|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
1-320 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 512.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 1 MFSFFKKSETPaetvatpaeaPKASWLSRLKAGLARTSSSLG----SVFSLRKIDEELLEDLEATLLMADCGVEATQTLL 76
Cdd:PRK10416 1 FFSWLKKKKKE----------KKEGWFERLKKGLSKTRENFGeginGLFAKKKIDEDLLEELEELLIEADVGVETTEEII 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 77 AELRRRWKHDKLETGDQLRAALAEHLVKLLTPLQQPLVIDGHQPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAG 156
Cdd:PRK10416 71 EELRERVKRKNLKDPEELKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 157 DTFRAAAREQLVEWGNRNNVSVIAQ-DGGDPAAVAFDAISAAKARGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEP 235
Cdd:PRK10416 151 DTFRAAAIEQLQVWGERVGVPVIAQkEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 236 SGPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKGGVIAAIARTHPKPLRFIGVGEGIEDLQPFMATEYV 315
Cdd:PRK10416 231 DAPHEVLLVLDATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFV 310
|
....*
gi 1326112735 316 DALLA 320
Cdd:PRK10416 311 DALLG 315
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
26-320 |
1.94e-171 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 477.98 E-value: 1.94e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 26 WLSRLKAGLARTSSSLG----SVFS-LRKIDEELLEDLEATLLMADCGVEATQTLLAELRRRWKHDKLETGDQLRAALAE 100
Cdd:COG0552 1 FFERLKEGLSKTRSGLGeklkSLFSgKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 101 HLVKLLTPLQQPLVIDGHQPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIA 180
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 181 Q-DGGDPAAVAFDAISAAKARGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEPSGPHEVLLVLDGNVGQNALAQLKA 259
Cdd:COG0552 161 QkEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAKV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1326112735 260 FDKAVGITGLIITKLDGTAKGGVIAAIARTHPKPLRFIGVGEGIEDLQPFMATEYVDALLA 320
Cdd:COG0552 241 FNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFG 301
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
49-319 |
5.83e-124 |
|
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: 356.57 E-value: 5.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 49 KIDEELLEDLEATLLMADCGVEATQTLLAELRRRWKHDKLETGDQLRAALAEHLVKLLTP-----LQQPLVIDGHQPYII 123
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEdllknTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 124 MLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQD-GGDPAAVAFDAISAAKARGI 202
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKeGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 203 DVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEPSGPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKGGV 282
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1326112735 283 IAAIARTHPKPLRFIGVGEGIEDLQPFMATEYVDALL 319
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
121-318 |
3.86e-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: 316.05 E-value: 3.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 121 YIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDGG-DPAAVAFDAISAAKA 199
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGaDPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 200 RGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEPSGPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAK 279
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1326112735 280 GGVIAAIARTHPKPLRFIGVGEGIEDLQPFMATEYVDAL 318
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
120-319 |
2.57e-96 |
|
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: 283.15 E-value: 2.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 120 PYIIMLSGVNGAGKTTSIGKLARHFQSQG-KSVLLAAGDTFRAAAREQLVEWGNR-NNVSVIAQDGGDPAAVAFDAISAA 197
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEIlGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 198 KARGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGT 277
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1326112735 278 AKGGVIAAIARTHPKPLRFIGVGEGIEDLQPFMATEYVDALL 319
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
122-318 |
2.89e-92 |
|
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: 272.88 E-value: 2.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDGG-DPAAVAFDAISAAKAR 200
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGaDPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 201 GIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKG 280
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKG 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1326112735 281 GVIAAIARTHPKPLRFIGVGEGIEDLQPFMATEYVDAL 318
Cdd:pfam00448 156 GAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
3-320 |
3.20e-89 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 270.31 E-value: 3.20e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 3 SFFKKSETPAETVATPAEAPKASWLSRLKAGLARTSSSLGSVFSLRKIDE----ELLEDLEATLLMADCGVEATQTLLAE 78
Cdd:PRK14974 11 KFVEKVEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAKITEIKEkdieDLLEELELELLESDVALEVAEEILES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 79 LRRRWKHDKL----ETGDQLRAALAEHLVKLLTPLQQPLVIDGHQ----PYIIMLSGVNGAGKTTSIGKLARHFQSQGKS 150
Cdd:PRK14974 91 LKEKLVGKKVkrgeDVEEIVKNALKEALLEVLSVGDLFDLIEEIKskgkPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 151 VLLAAGDTFRAAAREQLVEWGNRNNVSVIAQD-GGDPAAVAFDAISAAKARGIDVVMVDTAGRLPTQLHLMEEIAKVRRV 229
Cdd:PRK14974 171 VVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKyGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 230 IQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKGGVIAAIARTHPKPLRFIGVGEGIEDLQPF 309
Cdd:PRK14974 251 TK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPF 324
|
330
....*....|.
gi 1326112735 310 MATEYVDALLA 320
Cdd:PRK14974 325 DPDWFVDKLLG 335
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
121-318 |
3.73e-80 |
|
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: 242.28 E-value: 3.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 121 YIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQD-GGDPAAVAFDAISAAKA 199
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYtGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 200 RGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAK 279
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVES------PDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1326112735 280 GGVIAAIARTHPKPLRFIGVGEGIEDLQPFMATEYVDAL 318
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
38-309 |
3.92e-76 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 239.54 E-value: 3.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 38 SSSLGSVFS-LR---KIDE----ELLEDLEATLLMADCGVEATQTLLAELRRR------WKHdkLETGDQLRAALAEHLV 103
Cdd:COG0541 6 SERLQGAFKkLRgkgRLTEenikEALREVRRALLEADVNLKVVKDFIERVKERalgeevLKS--LTPGQQVIKIVHDELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 104 KLLTPLQQPLVIDGHQPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIA-QD 182
Cdd:COG0541 84 ELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPeED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 183 GGDPAAVAFDAISAAKARGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDK 262
Cdd:COG0541 164 GKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1326112735 263 AVGITGLIITKLDGTAKGGviAAI---ARTHpKPLRFIGVGEGIEDLQPF 309
Cdd:COG0541 238 ALGLTGVILTKLDGDARGG--AALsirAVTG-KPIKFIGTGEKLDDLEPF 284
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
38-322 |
4.69e-69 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 221.62 E-value: 4.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 38 SSSLGSVFS-LR---KIDEELLE----DLEATLLMADCGVEATQTLLAELRRRWKHDKLETG----DQLRAALAEHLVKL 105
Cdd:PRK00771 2 GESLRDALKkLAgksRIDEKTVKevvkDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGltprEHVIKIVYEELVKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 106 LTPLQQPLVIDgHQPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIA-QDGG 184
Cdd:PRK00771 82 LGEETEPLVLP-LKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGdPDNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 185 DPAAVAFDAISAAKARgiDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAV 264
Cdd:PRK00771 161 DAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1326112735 265 GITGLIITKLDGTAKGGVI-AAIARTHpKPLRFIGVGEGIEDLQPFMATEYVDALLATG 322
Cdd:PRK00771 233 GIGGIIITKLDGTAKGGGAlSAVAETG-APIKFIGTGEKIDDLERFDPDRFISRLLGMG 290
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
122-309 |
1.75e-63 |
|
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: 199.75 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIA-QDGGDPAAVAFDAISAAKAR 200
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFEsGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 201 GIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKG 280
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180
....*....|....*....|....*....
gi 1326112735 281 GVIAAIARTHPKPLRFIGVGEGIEDLQPF 309
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPF 184
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
121-315 |
2.65e-57 |
|
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: 183.55 E-value: 2.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 121 YIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIA-QDGGDPAAVAFDAISAAKA 199
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGsYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 200 RGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAK 279
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1326112735 280 -GGVIAAIARTHpKPLRFIGVGEGIEDLQPFMATEYV 315
Cdd:cd17875 155 gGGALSAVAATG-APIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
36-323 |
5.59e-49 |
|
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: 169.24 E-value: 5.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 36 RTSSSLGSVFSLRKIDEE----LLEDLEATLLMADCGVEATQTLLAELRRRWKHDKLETG----DQLRAALAEHLVKLLT 107
Cdd:TIGR01425 8 SLVTALRSMSSATVIDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGinkrKLIQDAVFEELCNLVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 108 PLQQPLVIDGHQPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVI-AQDGGDP 186
Cdd:TIGR01425 88 PGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYgSYEESDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 187 AAVAFDAISAAKARGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGI 266
Cdd:TIGR01425 168 VKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1326112735 267 TGLIITKLDGTAK-GGVIAAIARTHpKPLRFIGVGEGIEDLQPFMATEYVDALLATGN 323
Cdd:TIGR01425 242 GSVIITKLDGHAKgGGALSAVAATK-SPIIFIGTGEHVDEFEIFDAEPFVSKLLGMGD 298
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
121-318 |
9.51e-44 |
|
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: 149.30 E-value: 9.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 121 YIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQD-GGDPAAVAFDAISAAKA 199
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGyGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 200 RGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAV----------GITGL 269
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN------PDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1326112735 270 IITKLDgTAKGGVIAAIARTHP--KPLRFIGVGEGIEDLQPFMATEYVDAL 318
Cdd:cd17876 155 VLTKFD-TIDDKVGAALSMVYAtgQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
8-326 |
3.39e-35 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 131.14 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 8 SETPAETVATPAEAPKASW---LSRLKAGLARTSSSLGSVFSLRkidEELLEDLEATLLmaDCGVEAT--QTLLAELRRR 82
Cdd:COG1419 61 AAAPAAASAAAEEEELEELrreLAELKELLEEQLSGLAGESARL---PPELAELLERLL--EAGVSPElaRELLEKLPED 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 83 WkhdkleTGDQLRAALAEHLVKLLTPLQQPLVIDGHqpyIIMLSGVNGAGKTTSIGKLARHF-QSQGKSVLLAAGDTFRA 161
Cdd:COG1419 136 L------SAEEAWRALLEALARRLPVAEDPLLDEGG---VIALVGPTGVGKTTTIAKLAARFvLRGKKKVALITTDTYRI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 162 AAREQLVEWGNRNNVSVIaqdggdpaaVAFDAISAAKA----RGIDVVMVDTAGRLPTQLHLMEEIAKVrrviqkAEPSG 237
Cdd:COG1419 207 GAVEQLKTYARILGVPVE---------VAYDPEELKEAlerlRDKDLVLIDTAGRSPRDPELIEELKAL------LDAGP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 238 PHEVLLVLDGNV-GQNALAQLKAFdKAVGITGLIITKLDGTAKGGVIAAIARTHPKPLRFIGVGEGI-EDLQPFMATEYV 315
Cdd:COG1419 272 PIEVYLVLSATTkYEDLKEIVEAF-SSLGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLA 350
|
330
....*....|.
gi 1326112735 316 DALLATGNTGA 326
Cdd:COG1419 351 RLLLGGLEEEE 361
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
122-308 |
5.31e-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: 102.24 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLA-RHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDGGDPAAVAFDAisaakAR 200
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAaRYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADALER-----LS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 201 GIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEpsgpheVLLVLDGNVGQNALAQ-LKAFdKAVGITGLIITKLDGTAK 279
Cdd:cd17873 77 DRDLILIDTAGRSPRDKEQLEELKELLGAGEDIE------VHLVLSATTKAKDLKEiIERF-SPLGYRGLILTKLDETTS 149
|
170 180 190
....*....|....*....|....*....|
gi 1326112735 280 GGVIAAIARTHPKPLRFIGVGEGI-EDLQP 308
Cdd:cd17873 150 LGSVLSVLAESQLPVSYVTTGQRVpEDIEV 179
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
73-307 |
2.10e-19 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 88.03 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 73 QTLLAELRRRWKhdklETGDQLRAALAEHLVKLLTPLQQPLVIDGHqpyIIMLSGVNGAGKTTSIGKLARHFQS--QGKS 150
Cdd:PRK05703 181 EKLLKLLLEHMP----PRERTAWRYLLELLANMIPVRVEDILKQGG---VVALVGPTGVGKTTTLAKLAARYALlyGKKK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 151 VLLAAGDTFRAAAREQLVEWGNRNNVSVIaqdggdpaaVAFDAISAAKA----RGIDVVMVDTAGRLPTQLHLMEEIakv 226
Cdd:PRK05703 254 VALITLDTYRIGAVEQLKTYAKIMGIPVE---------VVYDPKELAKAleqlRDCDVILIDTAGRSQRDKRLIEEL--- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 227 RRVIQKAEPsgPHEVLLVLdgnvgqNALAQ-------LKAFdKAVGITGLIITKLDGTAK-GGVIAAIARTHpKPLRFIG 298
Cdd:PRK05703 322 KALIEFSGE--PIDVYLVL------SATTKyedlkdiYKHF-SRLPLDGLIFTKLDETSSlGSILSLLIESG-LPISYLT 391
|
250
....*....|
gi 1326112735 299 VGEGI-EDLQ 307
Cdd:PRK05703 392 NGQRVpDDIK 401
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
38-106 |
2.06e-13 |
|
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: 64.49 E-value: 2.06e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1326112735 38 SSSLGSVFSLRKIDEELLEDLEATLLMADCGVEATQTLLAELRRRWK---HDKLETGDQLRAALAEHLVKLL 106
Cdd:smart00963 6 GKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKgevLKGLTPKQEVKKILKEELVKIL 77
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
13-330 |
2.58e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 70.38 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 13 ETVATPAEAPKAswLSRLKAGLARTSSSLGSVFSLRKIDEELLEDLEATLLMADCGVEATQTLLAELRRRwkhdkLETGD 92
Cdd:PRK12724 117 EEVITEPERPVG--LSFEKELFEKNSFLESETTIVRKEKDSPLQRLGERLVREGMSQSYVEEMASKLEER-----LSPVD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 93 QLR-AALAEHLVKLLTPLQQ--PLVIDG---HQPYIIMLSGVNGAGKTTSIGKL-ARHFQSQGKSVLLAAGDTFRAAARE 165
Cdd:PRK12724 190 QGRnHNVTERAVTYLEERVSvdSDLFSGtgkNQRKVVFFVGPTGSGKTTSIAKLaAKYFLHMGKSVSLYTTDNYRIAAIE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 166 QLVEWgnrnnvsviaqdgGDPAAVAFDAISAAK------AR-GIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEPSgp 238
Cdd:PRK12724 270 QLKRY-------------ADTMGMPFYPVKDIKkfketlARdGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSV-- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 239 hEVLLVLDGNVG-QNALAQLKAFDkAVGITGLIITKLDGTAKGGVIAAIARTHPKPLRFIGVGEGIedlqPFmateyvDA 317
Cdd:PRK12724 335 -ENLLVLSSTSSyHHTLTVLKAYE-SLNYRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQEV----PF------DI 402
|
330
....*....|...
gi 1326112735 318 LLATGNTgAAEAV 330
Cdd:PRK12724 403 LNATKNL-MAECV 414
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
5-211 |
1.51e-12 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 66.97 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 5 FKKSETPAETVATPAE--APKASW---LSRLKAGLARTSSSLGsvfslRKIDEELLEDLEATLLMADCGVEATQTLLAEL 79
Cdd:TIGR03499 86 PAPQEEPAAPAAQAAEplLPEEELrkeLEALRELLERLLAGLA-----WLQRPPERAKLYERLLEAGVSEELARELLEKL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 80 RRRwkHDKLETGDQLRAALAEHLVKLltPLQQPLVidgHQPYIIMLSGVNGAGKTTSIGKLA-RHFQSQG-KSVLLAAGD 157
Cdd:TIGR03499 161 PED--ADAEDAWRWLREALEGMLPVK--PEEDPIL---EQGGVIALVGPTGVGKTTTLAKLAaRFALEHGkKKVALITTD 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1326112735 158 TFRAAAREQLVEWGNRNNVSVIAQDggDPAAVAfDAISAAKARgiDVVMVDTAG 211
Cdd:TIGR03499 234 TYRIGAVEQLKTYAEILGIPVKVAR--DPKELR-EALDRLRDK--DLILIDTAG 282
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
122-305 |
4.54e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 66.55 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLARHFQSQ--GKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDGGDPAAVAFDAISAAKa 199
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLLERLRDYK- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 200 rgidVVMVDTAG------RLPTQLHLMEEIAKVRRviqkaepsgphevLLVLDGNVGQNALAQLKAFDKAVGITGLIITK 273
Cdd:PRK12727 431 ----LVLIDTAGmgqrdrALAAQLNWLRAARQVTS-------------LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTK 493
|
170 180 190
....*....|....*....|....*....|..
gi 1326112735 274 LDGTAKGGVIAAIARTHPKPLRFIGVGEGIED 305
Cdd:PRK12727 494 LDETGRFGSALSVVVDHQMPITWVTDGQRVPD 525
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
122-232 |
6.50e-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: 59.69 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLvewgnRNNVSVIAQDGGDPAAVAFDAISAAKARG 201
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQL-----LLIIVGGKKASGSGELRLRLALALARKLK 78
|
90 100 110
....*....|....*....|....*....|.
gi 1326112735 202 IDVVMVDTAGRLPTQLHLMEEIAKVRRVIQK 232
Cdd:smart00382 79 PDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
123-304 |
1.27e-10 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 62.01 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 123 IMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDggDPAAVAfDAISAAKARG- 201
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR--DEAAMT-RALTYFKEEAr 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 202 IDVVMVDTAGRlptQLHLMEEIAKVRRVIQKAEPSgphEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKGG 281
Cdd:PRK11889 321 VDYILIDTAGK---NYRASETVEEMIETMGQVEPD---YICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSG 394
|
170 180
....*....|....*....|...
gi 1326112735 282 VIAAIARTHPKPLRFIGVGEGIE 304
Cdd:PRK11889 395 ELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
38-102 |
1.72e-09 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 53.62 E-value: 1.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1326112735 38 SSSLGSVFSL----RKIDEELLED----LEATLLMADCGVEATQTLLAELR-RRWKHDKLETGDQLRAALAEHL 102
Cdd:pfam02881 2 GEKLSSLFKGlrgkGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLReKAVGEKKLKPPQEVKKILKEEL 75
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
123-304 |
2.03e-09 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 57.45 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 123 IMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDggDPAAVAFDAISAAKARGI 202
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR--DEAAMTRALTYFKEEARV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 203 DVVMVDTAGRLPTQLHLMEEIAKVRRVIQkaepsgPHEVLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDGTAKGGV 282
Cdd:PRK06731 156 DYILIDTAGKNYRASETVEEMIETMGQVE------PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGE 229
|
170 180
....*....|....*....|..
gi 1326112735 283 IAAIARTHPKPLRFIGVGEGIE 304
Cdd:PRK06731 230 LLKIPAVSSAPIVLMTDGQDVK 251
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
115-305 |
3.10e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 57.82 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 115 IDGHQpyIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAREQLVEWGNRNNVSVIAqdGGDPAAVAFDAI 194
Cdd:PRK12726 203 LSNHR--IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV--ATSPAELEEAVQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 195 SAAKARGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIqkaepsgpHEVLLVLDGNVGQNALAQLKAFDK--AVGITGLIIT 272
Cdd:PRK12726 279 YMTYVNCVDHILIDTVGRNYLAEESVSEISAYTDVV--------HPDLTCFTFSSGMKSADVMTILPKlaEIPIDGFIIT 350
|
170 180 190
....*....|....*....|....*....|...
gi 1326112735 273 KLDGTAKGGVIAAIARTHPKPLRFIGVGEGIED 305
Cdd:PRK12726 351 KMDETTRIGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
122-305 |
7.05e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 53.57 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKL-ARHFQSQGKS-VLLAAGDTFRAAAREQLVEWGNRNNVSVIA-QDGGDPaavafdAISAAK 198
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLaARCVMRFGASkVALLTTDSYRIGGHEQLRIFGKILGVPVHAvKDGGDL------QLALAE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 199 ARGIDVVMVDTAGRLPTQLHLMEEIAkvrrVIQKAEPsgPHEVLLVLDGNVGQNALAQ-LKAFDKAVG--------ITGL 269
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQIA----MLHGADT--PVQRLLLLNATSHGDTLNEvVQAYRSAAGqpkaalpdLAGC 286
|
170 180 190
....*....|....*....|....*....|....*..
gi 1326112735 270 IITKLDGTAK-GGVIAAIARtHPKPLRFIGVGEGIED 305
Cdd:PRK14722 287 ILTKLDEASNlGGVLDTVIR-YKLPVHYVSTGQKVPE 322
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
79-303 |
8.03e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 53.37 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 79 LRRRWKHDKLETGDQLRAALAEHLVKLLTpLQQPLvIDGHQPYIIMLSGVNGAGKTTSIGKLARHF----QSQGKSVLLA 154
Cdd:PRK12723 135 IKKEFSLSDLDDYDKVRDSVIIYIAKTIK-CSGSI-IDNLKKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKII 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 155 AGDTFRAAAREQLVEWGNRNNVSVIA----QDGGDPAAVAFDaisaakargIDVVMVDTAGRLPTQLHlmeEIAKVRRVI 230
Cdd:PRK12723 213 TIDNYRIGAKKQIQTYGDIMGIPVKAiesfKDLKEEITQSKD---------FDLVLVDTIGKSPKDFM---KLAEMKELL 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1326112735 231 QKAEPSGphEVLLVLDGNVG----QNALAQLKAFdkavGITGLIITKLDGTAKGGVIAAIARTHPKPLRFIGVGEGI 303
Cdd:PRK12723 281 NACGRDA--EFHLAVSSTTKtsdvKEIFHQFSPF----SYKTVIFTKLDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
125-326 |
5.18e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 51.34 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 125 LSGVNGAGKTTSIGKLA-----RHFQSQgksVLLAAGDTFRAAAREQLVEWGNRNNVSVIA-QDggdpAAVAFDAISAAK 198
Cdd:PRK14723 190 LVGPTGVGKTTTTAKLAarcvaREGADQ---LALLTTDSFRIGALEQLRIYGRILGVPVHAvKD----AADLRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 199 ARGIdvVMVDTAGRLPTQLHLMEEIAKVrrviqkAEPSGPHEVLLVLDGNVGQNALAQL-KAFDKAVG--ITGLIITKLD 275
Cdd:PRK14723 263 DKHL--VLIDTVGMSQRDRNVSEQIAML------CGVGRPVRRLLLLNAASHGDTLNEVvHAYRHGAGedVDGCIITKLD 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1326112735 276 GTAKGGVIAAIARTHPKPLRFIGVGEGI-EDLQPFMATEYVDALLATGNTGA 326
Cdd:PRK14723 335 EATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAFATPRRGA 386
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
120-273 |
8.79e-05 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 41.26 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 120 PYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDtfraaareqlvewgnrnnvsviaqdggdpaavafdaisaaka 199
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------ 38
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1326112735 200 rgiDVVMVDTAGrlptQLHLMEEIAKVRRVIQkaePSGPHEVLLV-----LDGNVGQNALAQLKAFDKAVGITGLIITK 273
Cdd:cd01983 39 ---DYVLIDGGG----GLETGLLLGTIVALLA---LKKADEVIVVvdpelGSLLEAVKLLLALLLLGIGIRPDGIVLNK 107
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
122-282 |
2.54e-04 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 42.63 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLA-----RHFQSQgksVLLAAGDTFRAAAREQLVEWGNRNNVSVIAQDGGDPAAVAFDAIsa 196
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAaraviRHGADK---VALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLHEL-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 197 akaRGIDVVMVDTAGRLPTQLHLMEEIAKVRRVIQKAEPsgphevLLVLDGNVGQNALAQLKAFDKAVGITGLIITKLDG 276
Cdd:PRK14721 268 ---RGKHMVLIDTVGMSQRDQMLAEQIAMLSQCGTQVKH------LLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDE 338
|
....*.
gi 1326112735 277 TAKGGV 282
Cdd:PRK14721 339 AASLGI 344
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
70-164 |
2.61e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 42.66 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 70 EATQTLLAELRRRWKHD-KLETGDQLRAALAEHLVKLLTPLQQP---LVIDGHQpyIIMLSGVNGAGKTTSIGKLARHFQ 145
Cdd:COG0507 88 EAEQRLARRLRRLARPAlDEADVEAALAALEPRAGITLSDEQREavaLALTTRR--VSVLTGGAGTGKTTTLRALLAALE 165
|
90 100
....*....|....*....|.
gi 1326112735 146 SQGKSVLLAA--GdtfRAAAR 164
Cdd:COG0507 166 ALGLRVALAAptG---KAAKR 183
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
122-164 |
5.96e-04 |
|
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: 39.85 E-value: 5.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAgDTFRAAAR 164
Cdd:cd17933 14 VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
130-212 |
7.49e-04 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 40.22 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 130 GAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAreqlvEWGNrnnvsviAQDGGDP--AAVAFDAISAAK----ARGID 203
Cdd:PHA02518 11 GAGKTTVATNLASWLHADGHKVLLVDLDPQGSST-----DWAE-------AREEGEPliPVVRMGKSIRADlpkvASGYD 78
|
....*....
gi 1326112735 204 VVMVDTAGR 212
Cdd:PHA02518 79 YVVVDGAPQ 87
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
119-160 |
1.37e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 38.84 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1326112735 119 QPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFR 160
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
119-160 |
1.61e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 38.88 E-value: 1.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1326112735 119 QPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFR 160
Cdd:PRK05541 6 NGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELR 47
|
|
| MMAA-like |
cd03114 |
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ... |
95-211 |
2.36e-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: 39.09 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 95 RAALAE----------HLVKLLTPLQQPLVIDGHQPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLAAGDTFRAAAR 164
Cdd:cd03114 11 RRALARaitlvesgrpDHRELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVDPSSPRSG 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 165 EQLVewGNRNNVSVIAQD-------------GGDPAAVAFDAISAAKARGIDVVMVDTAG 211
Cdd:cd03114 91 GSIL--GDKTRMQRLARDpnafirpspsrgtLGGVARATREAILLCEAAGYDVVLVETVG 148
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
122-180 |
4.09e-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: 4.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1326112735 122 IIMLSGVNGAGKTTSIGKLARHFQSQGKSVLL--AAGDTFRAAAREQLVEWGNRNNVSVIA 180
Cdd:cd01672 2 FIVFEGIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
119-233 |
8.76e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 36.96 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326112735 119 QPYIIMLSGVNGAGKTTSIGKLARHFQSQGKSVLLaAGDTFRAAARE--QLVEWGNRNNVSVIAQDGGDPAAVAFDaisA 196
Cdd:pfam06414 10 RPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELHPHyrELQAADPKTASEYTQPDASRWVEKLLQ---H 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 1326112735 197 AKARGIDVVMvDTAGRLPtqlhlmEEIAKVRRVIQKA 233
Cdd:pfam06414 86 AIENGYNIIL-EGTLRSP------DVAKKIARALKAA 115
|
|
| |
