|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
24-326 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 515.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 24 FFARLKRGLKRTSENIGSGFVGLFKG-KKIDDDLFEELEEQLLIADVGVETTTRLIKNLTEQASRKQLKDGEALYELLRE 102
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 103 EMQKTLEPVSIPLVPENaDGPFVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVI 182
Cdd:COG0552 81 ELLEILDPVDKPLAIEE-KKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 183 AQHTGADSASVLFDALQAARARNVDVLIADTAGRLQNKSHLMDELKKVVRVMKKLDENAPHEVMLTLDACTGQNAISQAE 262
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906291060 263 LFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDALFTQE 326
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
18-326 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 514.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 18 KPVKEGFFARLKRGLKRTSENIGSGFVGLFKGKKIDDDLFEELEEQLLIADVGVETTTRLIKNLTEQASRKQLKDGEALY 97
Cdd:PRK10416 10 KEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEELK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 98 ELLREEMQKTLEPVSIPLVPENaDGPFVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRN 177
Cdd:PRK10416 90 ELLKEELAEILEPVEKPLNIEE-KKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 178 DIPVIAQHTGADSASVLFDALQAARARNVDVLIADTAGRLQNKSHLMDELKKVVRVMKKLDENAPHEVMLTLDACTGQNA 257
Cdd:PRK10416 169 GVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQNA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906291060 258 ISQAELFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDALFTQE 326
Cdd:PRK10416 249 LSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGE 317
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
51-323 |
1.93e-131 |
|
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: 375.44 E-value: 1.93e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 51 KIDDDLFEELEEQLLIADVGVETTTRLIKNLTEQASRKQLKDGEALYELLREEMQKTLEPVSIPLVPEN----ADGPFVI 126
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDLEliveENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 127 LMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARARNV 206
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 207 DVLIADTAGRLQNKSHLMDELKKVVRVMKKLDENAPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGGV 286
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1906291060 287 IFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDALF 323
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
124-322 |
3.05e-114 |
|
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: 329.15 E-value: 3.05e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 124 FVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARA 203
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 204 RNVDVLIADTAGRLQNKSHLMDELKKVVRVMKKLDENAPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAK 283
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906291060 284 GGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDAL 322
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
123-323 |
4.64e-100 |
|
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: 292.78 E-value: 4.64e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 123 PFVILMVGVNGVGKTTTIGKLAKQYQAQG-KSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAA 201
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 202 RARNVDVLIADTAGRLQNKSHLMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGT 281
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906291060 282 AKGGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDALF 323
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
124-322 |
1.66e-97 |
|
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: 286.36 E-value: 1.66e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 124 FVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARA 203
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 204 RNVDVLIADTAGRLQNKSHLMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAK 283
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906291060 284 GGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDAL 322
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
124-322 |
6.09e-91 |
|
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: 269.63 E-value: 6.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 124 FVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARA 203
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 204 RNVDVLIADTAGRLQNKSHLMDELKKVVRVmkkldeNAPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAK 283
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906291060 284 GGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDAL 322
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
67-323 |
1.02e-78 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 243.73 E-value: 1.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 67 ADVGVETTTRLIKNLTEQASRKQLKDGEALYELLREEMQKTLEPV-------SIPLVPENADGPFVILMVGVNGVGKTTT 139
Cdd:PRK14974 77 SDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVlsvgdlfDLIEEIKSKGKPVVIVFVGVNGTGKTTT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 140 IGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARARNVDVLIADTAGRLQN 219
Cdd:PRK14974 157 IAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 220 KSHLMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIPIR 299
Cdd:PRK14974 237 DANLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPIL 310
|
250 260
....*....|....*....|....
gi 1906291060 300 HIGVGEQIDDLRTFDAKDFIDALF 323
Cdd:PRK14974 311 FLGVGQGYDDLIPFDPDWFVDKLL 334
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
67-320 |
9.44e-69 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 220.66 E-value: 9.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 67 ADVGVETTTRLIKNLTEQAS----RKQLKDGEALYELLREEMQKTLEPVSIPLVpENADGPFVILMVGVNGVGKTTTIGK 142
Cdd:COG0541 41 ADVNLKVVKDFIERVKERALgeevLKSLTPGQQVIKIVHDELVELLGGENEELN-LAKKPPTVIMMVGLQGSGKTTTAAK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 143 LAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARARNVDVLIADTAGRLQNKSH 222
Cdd:COG0541 120 LAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 223 LMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIG 302
Cdd:COG0541 200 LMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIG 273
|
250
....*....|....*...
gi 1906291060 303 VGEQIDDLRTFDAKDFID 320
Cdd:COG0541 274 TGEKLDDLEPFHPDRMAS 291
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
125-314 |
2.08e-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: 199.36 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARAR 204
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 205 NVDVLIADTAGRLQNKSHLMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKG 284
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|
gi 1906291060 285 GVIFAIADKFGIPIRHIGVGEQIDDLRTFD 314
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFH 185
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
67-319 |
1.21e-59 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 197.35 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 67 ADVGVetttRLIKNLTEQASRKQLKDG--------EALYELLREEMQKTL-EPVSIPLVPENadgPFVILMVGVNGVGKT 137
Cdd:PRK00771 37 ADVNV----KLVKELSKSIKERALEEEppkgltprEHVIKIVYEELVKLLgEETEPLVLPLK---PQTIMLVGLQGSGKT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 138 TTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARarNVDVLIADTAGRL 217
Cdd:PRK00771 110 TTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKFK--KADVIIVDTAGRH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 218 QNKSHLMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIP 297
Cdd:PRK00771 188 ALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAP 261
|
250 260
....*....|....*....|..
gi 1906291060 298 IRHIGVGEQIDDLRTFDAKDFI 319
Cdd:PRK00771 262 IKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
124-319 |
2.80e-53 |
|
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: 173.53 E-value: 2.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 124 FVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARA 203
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 204 RNVDVLIADTAGRLQNKSHLMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAK 283
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1906291060 284 GGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFI 319
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
124-322 |
2.83e-45 |
|
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: 153.15 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 124 FVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARA 203
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 204 RNVDVLIADTAGRLQNKSHLMDELKKVVrvmkklDENAPHEVMLTLDACTGQNAISQAELFKQAV----------GVTGI 273
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLI------KENNPDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906291060 274 TISKLDGTA-KGGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFIDAL 322
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
67-322 |
2.99e-40 |
|
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: 146.13 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 67 ADVGVETTTRLIKNLTEQASRKQLKDGEALYELLR----EEMQKTLEPVSIPLVPENADgPFVILMVGVNGVGKTTTIGK 142
Cdd:TIGR01425 41 SDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQdavfEELCNLVDPGVEAFTPKKGK-TCVIMFVGLQGAGKTTTCTK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 143 LAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARARNVDVLIADTAGRLQNKSH 222
Cdd:TIGR01425 120 LAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 223 LMDELKKVVRVMKkldenaPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIG 302
Cdd:TIGR01425 200 LFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIG 273
|
250 260
....*....|....*....|
gi 1906291060 303 VGEQIDDLRTFDAKDFIDAL 322
Cdd:TIGR01425 274 TGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
1-323 |
4.55e-36 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 133.45 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 1 EATELADDEDRQPEPQAKPVKEGFFARLKR---GLKRTSENIGSGFvglfkGKKIDDDLFEELEEQLLIADVGVETTtrL 77
Cdd:COG1419 52 DEAEKAPAAAAAPAAASAAAEEEELEELRRelaELKELLEEQLSGL-----AGESARLPPELAELLERLLEAGVSPE--L 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 78 IKNLTEQASRKqlKDGEALYELLREEMQKTLEPVSIPLVPENAdgpfVILMVGVNGVGKTTTIGKLAKQY-QAQGKSVML 156
Cdd:COG1419 125 ARELLEKLPED--LSAEEAWRALLEALARRLPVAEDPLLDEGG----VIALVGPTGVGKTTTIAKLAARFvLRGKKKVAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 157 AAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLfdalqaARARNVDVLIADTAGRLQNKSHLMDELKKVVRVMKk 236
Cdd:COG1419 199 ITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGP- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 237 ldenaPHEVMLTLDACT-GQNAISQAELFKQaVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQI-DDLRTFD 314
Cdd:COG1419 272 -----PIEVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVAD 345
|
....*....
gi 1906291060 315 AKDFIDALF 323
Cdd:COG1419 346 PERLARLLL 354
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
125-316 |
1.40e-31 |
|
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: 116.88 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQYQA-QGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAqhtgADSASVLFDALqaARA 203
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVLkKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDPEDLADAL--ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 204 RNVDVLIADTAGRLQNKSHLMDELKKVvrvmkkLDENAPHEVMLTLDACT-GQNAISQAELFKqAVGVTGITISKLDGTA 282
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKEL------LGAGEDIEVHLVLSATTkAKDLKEIIERFS-PLGYRGLILTKLDETT 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1906291060 283 KGGVIFAIADKFGIPIRHIGVGEQI-DDLRTFDAK 316
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPL 183
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
72-331 |
2.87e-23 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 99.20 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 72 ETTTRLIKNLTEQASRKQLKDGEALYELLREEMQKTLEPVSIplvpenadGPFVILMVGVNGVGKTTTIGKLAKQYQA-- 149
Cdd:PRK05703 178 EIAEKLLKLLLEHMPPRERTAWRYLLELLANMIPVRVEDILK--------QGGVVALVGPTGVGKTTTLAKLAARYALly 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 150 QGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADsasvLFDALQAARARNVdVLIaDTAGRLQNKSHLMDELKK 229
Cdd:PRK05703 250 GKKKVALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKE----LAKALEQLRDCDV-ILI-DTAGRSQRDKRLIEELKA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 230 VVRvmkklDENAPHEVMLTLdACTGQN-----AISQaelFKQaVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIGVG 304
Cdd:PRK05703 324 LIE-----FSGEPIDVYLVL-SATTKYedlkdIYKH---FSR-LPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNG 393
|
250 260
....*....|....*....|....*....
gi 1906291060 305 EQI-DDLRTFDAKDFIDALFT-QENDEKK 331
Cdd:PRK05703 394 QRVpDDIKVANPEELVRLLLGgFNKSEPS 422
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
76-215 |
1.11e-15 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 75.83 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 76 RLIKNLTEQAsrKQLKDGEALYELLREEMQKTLEpvSIPLVPENADGPFVILMVGVNGVGKTTTIGKLAKQY--QAQGKS 153
Cdd:TIGR03499 151 ELARELLEKL--PEDADAEDAWRWLREALEGMLP--VKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFalEHGKKK 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906291060 154 VMLAAGDTFRAAAVEQLQVWGQRNDIPVIAqhtgADSASVLFDALQaaRARNVDVLIADTAG 215
Cdd:TIGR03499 227 VALITTDTYRIGAVEQLKTYAEILGIPVKV----ARDPKELREALD--RLRDKDLILIDTAG 282
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
126-307 |
5.45e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 69.32 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 126 ILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARarn 205
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEEAR--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 206 VDVLIADTAGRLQNKSHLMDELkkvVRVMKKLDenaPHEVMLTLDAC-TGQNAISQAELFKQaVGVTGITISKLDGTAKG 284
Cdd:PRK11889 321 VDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASmKSKDMIEIITNFKD-IHIDGIVFTKFDETASS 393
|
170 180
....*....|....*....|...
gi 1906291060 285 GVIFAIADKFGIPIRHIGVGEQI 307
Cdd:PRK11889 394 GELLKIPAVSSAPIVLMTDGQDV 416
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
110-319 |
6.82e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 69.25 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 110 PVSiPLVPENADGpfVILMVGVNGVGKTTTIGKLAKQYQAQ--GKSVMLAAGDTFRAAAVEQLQVWGQRNDIPViaqHTg 187
Cdd:PRK12727 340 PVA-PVDPLERGG--VIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 188 ADSASVLFDALQaaRARNVDVLIADTAGRLQNKSHLMDELK-----KVVRVMKKLDENAP----HEVMLTLDACTGQnai 258
Cdd:PRK12727 413 ADSAESLLDLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNwlraaRQVTSLLVLPANAHfsdlDEVVRRFAHAKPQ--- 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906291060 259 sqaelfkqavgvtGITISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQI-DDLRTFDAKDFI 319
Cdd:PRK12727 488 -------------GVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLV 536
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
125-237 |
9.81e-13 |
|
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: 64.70 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVwgqrndIPVIAQHTGADSASVLFDALQAARAR 204
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALARKL 77
|
90 100 110
....*....|....*....|....*....|...
gi 1906291060 205 NVDVLIADTAGRLQNKSHLMDELKKVVRVMKKL 237
Cdd:smart00382 78 KPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
101-323 |
1.62e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 68.29 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 101 REEMQKTLePVsipLVPENA--DGPFVILMVGVNGVGKTTTIGKLAKQYQAQ--GKSVMLAAGDTFRAAAVEQLQVWGQR 176
Cdd:PRK14723 165 RNELATHL-PV---LRDEDAllAQGGVLALVGPTGVGKTTTTAKLAARCVARegADQLALLTTDSFRIGALEQLRIYGRI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 177 NDIPVIAQHTGADsasvLFDALQAARARNVdVLIaDTAGRLQNKSHLMDELKKVVRVmkkldeNAPHEVMLTLDACTGQN 256
Cdd:PRK14723 241 LGVPVHAVKDAAD----LRFALAALGDKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLLNAASHGD 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906291060 257 AISQ-AELFKQAVG--VTGITISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQI-DDLRTFDAKDFIDALF 323
Cdd:PRK14723 309 TLNEvVHAYRHGAGedVDGCIITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
84-309 |
2.64e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 67.07 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 84 QASRKQLKDGEALYelLREEMQKTLEPVSIPLVPENA---DGPFVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGD 160
Cdd:PRK12726 166 QAGRKQFKQVETAH--LDDITDWFVPYLSGKLAVEDSfdlSNHRIISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 161 TFRAAAVEQLQVWGQRNDIPVIAqhtgADSASVLFDALQAARARN-VDVLIADTAGRlqnkSHLMDElkKVVRVMKKLDE 239
Cdd:PRK12726 244 TFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQYMTYVNcVDHILIDTVGR----NYLAEE--SVSEISAYTDV 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 240 NAPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQIDD 309
Cdd:PRK12726 314 VHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
126-307 |
5.21e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 62.07 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 126 ILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASVLFDALQAARarn 205
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEEAR--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 206 VDVLIADTAGRLQNKSHLMDELkkvvrvMKKLDENAPHEVMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTAKGG 285
Cdd:PRK06731 155 VDYILIDTAGKNYRASETVEEM------IETMGQVEPDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSG 228
|
170 180
....*....|....*....|..
gi 1906291060 286 VIFAIADKFGIPIRHIGVGEQI 307
Cdd:PRK06731 229 ELLKIPAVSSAPIVLMTDGQDV 250
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
125-319 |
8.33e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 62.43 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQ--YQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSasvlfdALQAAR 202
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDL------QLALAE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 203 ARNVDVLIADTAGRLQNKSHLMDELKKVvrvmkkLDENAPHEVMLTLDACTGQNAISQ-AELFKQAVG--------VTGI 273
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQIAML------HGADTPVQRLLLLNATSHGDTLNEvVQAYRSAAGqpkaalpdLAGC 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906291060 274 TISKLDGTAKGGVIFAIADKFGIPIRHIGVGEQIDDLRTFDAKDFI 319
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFL 332
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
125-307 |
5.86e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 59.98 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQYQAQ-GKSVMLAAGDTFRAAAVEQLQVWgqrndipviaqhtgADSASVLFDALQAAR- 202
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAAKYFLHmGKSVSLYTTDNYRIAAIEQLKRY--------------ADTMGMPFYPVKDIKk 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 203 -----ARNVDVLI-ADTAGRLQNKSHLMDELKKVVRVMKKLDENaphEVMLTLDACTGQNAISQAELFKQAVGVTGITIS 276
Cdd:PRK12724 291 fketlARDGSELIlIDTAGYSHRNLEQLERMQSFYSCFGEKDSV---ENLLVLSSTSSYHHTLTVLKAYESLNYRRILLT 367
|
170 180 190
....*....|....*....|....*....|.
gi 1906291060 277 KLDGTAKGGVIFAIADKFGIPIRHIGVGEQI 307
Cdd:PRK12724 368 KLDEADFLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
75-293 |
1.20e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 55.68 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 75 TRLIKNLTEQASRKQLKDgealYELLREE----MQKTLEpVSIPLVpeNADGPFVILMVGVNGVGKTTTIGKLAKQY--- 147
Cdd:PRK12723 129 KDINEFIKKEFSLSDLDD----YDKVRDSviiyIAKTIK-CSGSII--DNLKKRVFILVGPTGVGKTTTIAKLAAIYgin 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 148 -QAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADSASvlfdalQAARARNVDVLIADTAGRLQNKSHLMDE 226
Cdd:PRK12723 202 sDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKE------EITQSKDFDLVLVDTIGKSPKDFMKLAE 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 227 LKKVVRVMKKldenaPHEVMLTLDACTGQNAISqaELFKQ--AVGVTGITISKLDGTAK-GGVIFAIADK 293
Cdd:PRK12723 276 MKELLNACGR-----DAEFHLAVSSTTKTSDVK--EIFHQfsPFSYKTVIFTKLDETTCvGNLISLIYEM 338
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
36-108 |
1.16e-07 |
|
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: 48.32 E-value: 1.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906291060 36 SENIGSGFVGLFKGKKIDDDLFEELEEQLLIADVGVETTTRLIKNLTEQASR---KQLKDGEALYELLREEMQKTL 108
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
36-104 |
7.20e-07 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 46.31 E-value: 7.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906291060 36 SENIGSGFVGLFKGKKIDDDLFEELEEQLLI----ADVGVETTTRLIKNLTEQA-SRKQLKDGEALYELLREEM 104
Cdd:pfam02881 2 GEKLSSLFKGLRGKGKIDEEDLEEALKELEEalleADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
125-323 |
1.36e-04 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 43.40 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQ--YQAQGKSVMLAAGDTFRAAAVEQLQVWGQRNDIPViaqHTGADSASVLFdALQAAR 202
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADLQL-MLHELR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 203 ARNVdVLIaDTAGRLQNKSHLMDELKKVVRVMKKLDEnaphevMLTLDACTGQNAISQAELFKQAVGVTGITISKLDGTA 282
Cdd:PRK14721 269 GKHM-VLI-DTVGMSQRDQMLAEQIAMLSQCGTQVKH------LLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906291060 283 KGGVIFAIADKFGIPIRHIGVGEQI-DDLRTFDAKDFIDALF 323
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
74-212 |
1.83e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 43.04 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 74 TTRLIKNLTEQASR-KQLKDGEALYELLREEMQKTLEPVSIPLVPE--------NADGPFVILmVGVNGVGKTTTIGKLA 144
Cdd:COG0507 83 LTRLLEAEQRLARRlRRLARPALDEADVEAALAALEPRAGITLSDEqreavalaLTTRRVSVL-TGGAGTGKTTTLRALL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906291060 145 KQYQAQGKSVMLAA--GdtfRAAAV--EQLQVWGQrndipVIAQHTGADSASVLFDALQAARARNVDVLIAD 212
Cdd:COG0507 162 AALEALGLRVALAAptG---KAAKRlsESTGIEAR-----TIHRLLGLRPDSGRFRHNRDNPLTPADLLVVD 225
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
120-215 |
2.80e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 41.40 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 120 ADGPFVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAgDTFRAAAveqlqvwgqrndipVIAQHTGADS---ASVLFD 196
Cdd:pfam13604 15 TSGDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLA-PTGRAAK--------------VLGEELGIPAdtiAKLLHR 79
|
90
....*....|....*....
gi 1906291060 197 ALQAARARNVDVLIADTAG 215
Cdd:pfam13604 80 LGGRAGLDPGTLLIVDEAG 98
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
123-229 |
5.40e-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: 40.42 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 123 PFVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLaAGDTFRAA---AVEQLQVWGQRNdipviAQHTGADSASVLFDALQ 199
Cdd:pfam06414 11 PKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELhphYRELQAADPKTA-----SEYTQPDASRWVEKLLQ 84
|
90 100 110
....*....|....*....|....*....|
gi 1906291060 200 AARARNVDVLIADTAGRLQNKSHLMDELKK 229
Cdd:pfam06414 85 HAIENGYNIILEGTLRSPDVAKKIARALKA 114
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
120-167 |
8.58e-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: 39.46 E-value: 8.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1906291060 120 ADGPFVILmVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAgDTFRAAAV 167
Cdd:cd17933 10 LRNRVSVL-TGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
125-215 |
2.32e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 39.56 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906291060 125 VILMVGVNGVGKTTTIGKLAKQYQAQ-GKS-VMLAAGDTFRAAAVEQLQVWGQRNDIPVIAQHTGADsasvLFDALQAAR 202
Cdd:PRK06995 258 VFALMGPTGVGKTTTTAKLAARCVMRhGASkVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAAD----LRLALSELR 333
|
90
....*....|...
gi 1906291060 203 ARNVdVLIaDTAG 215
Cdd:PRK06995 334 NKHI-VLI-DTIG 344
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
123-163 |
2.52e-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: 38.07 E-value: 2.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1906291060 123 PFVILMVGVNGVGKTTTIGKLAKQYQAQGKSVMLAAGDTFR 163
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
130-183 |
3.14e-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: 3.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906291060 130 GVNGVGKTTTIGKLAKQYQAQGKSVML--AAGDTFRAAAVEQLQVWGQRNDIPVIA 183
Cdd:cd01672 7 GIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| |
