|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
111-413 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 530.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 111 FFARLKRSLSRTKANIGAGFFGLF-KDKQIDDDLFEELEEQLLIADVGMDTTTKIIGNLTEKASRRDLKDGEALYGLLKE 189
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFsGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 190 EMAEILSHVEKPLEVDTTKtPYVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVI 269
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKK-PFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 270 AQHTGADSASVIYDAIEAAKARGVDVVIADTAGRLQNKANLMEELRKIVRVMKKIDESAPHEIMLTLDAGTGQNAISQAK 349
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330653883 350 LFSDVAPITGITLTKLDGTAKGGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDALFSRD 413
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
104-414 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 524.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 104 QEKPTESFFARLKRSLSRTKANIGAGFFGLFKDKQIDDDLFEELEEQLLIADVGMDTTTKIIGNLTEKASRRDLKDGEAL 183
Cdd:PRK10416 9 KKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 184 YGLLKEEMAEILSHVEKPLEVDTTKtPYVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGER 263
Cdd:PRK10416 89 KELLKEELAEILEPVEKPLNIEEKK-PFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 264 NNVPVIAQHTGADSASVIYDAIEAAKARGVDVVIADTAGRLQNKANLMEELRKIVRVMKKIDESAPHEIMLTLDAGTGQN 343
Cdd:PRK10416 168 VGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQN 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330653883 344 AISQAKLFSDVAPITGITLTKLDGTAKGGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDALFSRDE 414
Cdd:PRK10416 248 ALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
138-410 |
6.80e-135 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 387.77 E-value: 6.80e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 138 QIDDDLFEELEEQLLIADVGMDTTTKIIGNLTEKASRRDLKDGEALYGLLKEEMAEILSHVE----KPLEVDTTKTPYVI 213
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 214 LMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKARGV 293
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 294 DVVIADTAGRLQNKANLMEELRKIVRVMKKIDESAPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKGGV 373
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1330653883 374 IFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDALF 410
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
211-409 |
8.17e-119 |
|
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: 343.78 E-value: 8.17e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 211 YVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKA 290
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRLQNKANLMEELRKIVRVMKKIDESAPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAK 370
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1330653883 371 GGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDAL 409
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
210-410 |
6.73e-106 |
|
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: 310.88 E-value: 6.73e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 210 PYVILMVGVNGVGKTTTIGKLAKQFQGQG-KKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAA 288
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 289 KARGVDVVIADTAGRLQNKANLMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGT 368
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1330653883 369 AKGGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDALF 410
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
212-409 |
4.99e-101 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 298.30 E-value: 4.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKAR 291
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 292 GVDVVIADTAGRLQNKANLMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKG 371
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKG 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1330653883 372 GVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDAL 409
Cdd:pfam00448 156 GAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
211-409 |
4.75e-94 |
|
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: 280.41 E-value: 4.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 211 YVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKA 290
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRLQNKANLMEELRKIVRVMkkidesAPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAK 370
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVE------SPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1330653883 371 GGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDAL 409
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
154-411 |
6.47e-87 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 267.61 E-value: 6.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 154 ADVGMDTTTKIIGNLTEKAS----RRDLKDGEALYGLLKEEMAEILS---HVEKPLEVDTTKTPYVILMVGVNGVGKTTT 226
Cdd:PRK14974 77 SDVALEVAEEILESLKEKLVgkkvKRGEDVEEIVKNALKEALLEVLSvgdLFDLIEEIKSKGKPVVIVFVGVNGTGKTTT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 227 IGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKARGVDVVIADTAGRLQN 306
Cdd:PRK14974 157 IAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 307 KANLMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKGGVIFAIADQFQIPIR 386
Cdd:PRK14974 237 DANLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPIL 310
|
250 260
....*....|....*....|....*
gi 1330653883 387 FIGVGEGIDDLRPFETQDFIDALFS 411
Cdd:PRK14974 311 FLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
154-400 |
1.74e-76 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 243.39 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 154 ADVGMDTTTKIIGNLTEKASRRD----LKDGEALYGLLKEEMAEILSHVEKPLEVDTTKtPYVILMVGVNGVGKTTTIGK 229
Cdd:COG0541 41 ADVNLKVVKDFIERVKERALGEEvlksLTPGQQVIKIVHDELVELLGGENEELNLAKKP-PTVIMMVGLQGSGKTTTAAK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 230 LAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKARGVDVVIADTAGRLQNKAN 309
Cdd:COG0541 120 LAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 310 LMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKGGVIFAIADQFQIPIRFIG 389
Cdd:COG0541 200 LMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIG 273
|
250
....*....|.
gi 1330653883 390 VGEGIDDLRPF 400
Cdd:COG0541 274 TGEKLDDLEPF 284
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
212-400 |
1.26e-67 |
|
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: 212.84 E-value: 1.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKAR 291
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 292 GVDVVIADTAGRLQNKANLMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKG 371
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180
....*....|....*....|....*....
gi 1330653883 372 GVIFAIADQFQIPIRFIGVGEGIDDLRPF 400
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPF 184
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
154-406 |
4.57e-62 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 206.60 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 154 ADVGMdtttKIIGNLTEKASRRDLKDgEALYGL---------LKEEMAEILSHVEKPLEVDttKTPYVILMVGVNGVGKT 224
Cdd:PRK00771 37 ADVNV----KLVKELSKSIKERALEE-EPPKGLtprehvikiVYEELVKLLGEETEPLVLP--LKPQTIMLVGLQGSGKT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 225 TTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKARgvDVVIADTAGRL 304
Cdd:PRK00771 110 TTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKFKKA--DVIIVDTAGRH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 305 QNKANLMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKGGVIFAIADQFQIP 384
Cdd:PRK00771 188 ALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAP 261
|
250 260
....*....|....*....|..
gi 1330653883 385 IRFIGVGEGIDDLRPFETQDFI 406
Cdd:PRK00771 262 IKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
211-406 |
3.97e-56 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 183.16 E-value: 3.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 211 YVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKA 290
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRLQNKANLMEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAK 370
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1330653883 371 GGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFI 406
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
211-409 |
3.33e-48 |
|
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: 163.17 E-value: 3.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 211 YVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKA 290
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRLQNKANLMEELRKIvrvmkkIDESAPHEIMLTLDAGTGQNAISQAKLF----------SDVAPITGI 360
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKL------IKENNPDLVLFVGEALVGNDAVDQLKKFnqaladyspsDNPRLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1330653883 361 TLTKLDGTA-KGGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFIDAL 409
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
154-409 |
3.49e-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: 148.06 E-value: 3.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 154 ADVGMDTTTKIIGNLTEKASRRDLKDGEALYGLLKEEM-AEILSHVEKPLEVDTTK--TPYVILMVGVNGVGKTTTIGKL 230
Cdd:TIGR01425 41 SDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVfEELCNLVDPGVEAFTPKkgKTCVIMFVGLQGAGKTTTCTKL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 231 AKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKARGVDVVIADTAGRLQNKANL 310
Cdd:TIGR01425 121 AYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 311 MEELRKIVRVMKkidesaPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAKGGVIFAIADQFQIPIRFIGV 390
Cdd:TIGR01425 201 FEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIGT 274
|
250
....*....|....*....
gi 1330653883 391 GEGIDDLRPFETQDFIDAL 409
Cdd:TIGR01425 275 GEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
163-414 |
1.02e-38 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 142.70 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 163 KIIGNLTEKASRRDlkDGEALYGLLKEEMAEILSHVEKPLeVDTTKtpyVILMVGVNGVGKTTTIGKLAKQF-QGQGKKV 241
Cdd:COG1419 123 ELARELLEKLPEDL--SAEEAWRALLEALARRLPVAEDPL-LDEGG---VIALVGPTGVGKTTTIAKLAARFvLRGKKKV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 242 MLAAGDTFRAAAVEQLQVWGERNNVPViaqhtgadsaSVIYDAIEAAKA----RGVDVVIADTAGRLQNKANLMEELRKI 317
Cdd:COG1419 197 ALITTDTYRIGAVEQLKTYARILGVPV----------EVAYDPEELKEAlerlRDKDLVLIDTAGRSPRDPELIEELKAL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 318 VRVMKKIdesaphEIMLTLDAGT-GQNAISQAKLFSDVaPITGITLTKLDGTAKGGVIFAIADQFQIPIRFIGVGEGI-D 395
Cdd:COG1419 267 LDAGPPI------EVYLVLSATTkYEDLKEIVEAFSSL-GLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpE 339
|
250
....*....|....*....
gi 1330653883 396 DLRPFETQDFIDALFSRDE 414
Cdd:COG1419 340 DIEVADPERLARLLLGGLE 358
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
212-402 |
9.06e-35 |
|
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: 127.28 E-value: 9.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQG-QGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAqhtgADSASVIYDAIEAakA 290
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVLkKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDPEDLADALER--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRLQNKANLMEELRKIVRVMKKIdesaphEIMLTLDAGT-GQNAISQAKLFSDVaPITGITLTKLDGTA 369
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKELLGAGEDI------EVHLVLSATTkAKDLKEIIERFSPL-GYRGLILTKLDETT 148
|
170 180 190
....*....|....*....|....*....|....
gi 1330653883 370 KGGVIFAIADQFQIPIRFIGVGEGI-DDLRPFET 402
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASP 182
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
162-398 |
1.37e-25 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 107.67 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 162 TKIIGNLTEKASRRDLKDGEALYGLLKEEMaeilshveKPLEVDTTKTPYVILMVGVNGVGKTTTIGKLAKQFQG--QGK 239
Cdd:PRK05703 181 EKLLKLLLEHMPPRERTAWRYLLELLANMI--------PVRVEDILKQGGVVALVGPTGVGKTTTLAKLAARYALlyGKK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 240 KVMLAAGDTFRAAAVEQLQVWGERNNVPVIaqhtgadsasVIYDAIEAAKA----RGVDVVIADTAGRLQNKANLMEELR 315
Cdd:PRK05703 253 KVALITLDTYRIGAVEQLKTYAKIMGIPVE----------VVYDPKELAKAleqlRDCDVILIDTAGRSQRDKRLIEELK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 316 KIvrvmkkIDES-APHEIMLTLDAgTGQN-----AISQaklFSDVaPITGITLTKLDGTAKGGVIFAIADQFQIPIRFIG 389
Cdd:PRK05703 323 AL------IEFSgEPIDVYLVLSA-TTKYedlkdIYKH---FSRL-PLDGLIFTKLDETSSLGSILSLLIESGLPISYLT 391
|
250
....*....|
gi 1330653883 390 VGEGI-DDLR 398
Cdd:PRK05703 392 NGQRVpDDIK 401
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
175-302 |
6.37e-18 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 83.15 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 175 RDLKDGEALYGLLKEEMAEILSHveKPLEVDTTKTPYVILMVGVNGVGKTTTIGKLAKQF--QGQGKKVMLAAGDTFRAA 252
Cdd:TIGR03499 161 PEDADAEDAWRWLREALEGMLPV--KPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIG 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1330653883 253 AVEQLQVWGERNNVPVIAqhtgADSASVIYDAIEaaKARGVDVVIADTAG 302
Cdd:TIGR03499 239 AVEQLKTYAEILGIPVKV----ARDPKELREALD--RLRDKDLILIDTAG 282
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
213-394 |
1.70e-14 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 74.72 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 213 ILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKarg 292
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEEAR--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 293 VDVVIADTAGRLQNKANLMEELrkiVRVMKKIDesaPHEIMLTLDAG-TGQNAISQAKLFSDVApITGITLTKLDGTAKG 371
Cdd:PRK11889 321 VDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASmKSKDMIEIITNFKDIH-IDGIVFTKFDETASS 393
|
170 180
....*....|....*....|...
gi 1330653883 372 GVIFAIADQFQIPIRFIGVGEGI 394
Cdd:PRK11889 394 GELLKIPAVSSAPIVLMTDGQDV 416
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
204-397 |
2.72e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 71.56 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 204 VDTTKTPYVILMVGVNGVGKTTTIGKLAKQFQGQ--GKKVMLAAGDTFRAAAVEQLQVWGERNNvpvIAQHTgADSASVI 281
Cdd:PRK12727 344 VDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLG---IAVHE-ADSAESL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 282 YDAIEaaKARGVDVVIADTAGRLQNKANLMEELRKIvRVMKKIDEsapheiMLTLDAGTGqnaisqaklFSDV------- 354
Cdd:PRK12727 420 LDLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNWL-RAARQVTS------LLVLPANAH---------FSDLdevvrrf 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1330653883 355 --APITGITLTKLDGTAKGGVIFAIADQFQIPIRFIGVGEGI-DDL 397
Cdd:PRK12727 482 ahAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDL 527
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
212-327 |
4.14e-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: 66.63 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQvwgernNVPVIAQHTGADSASVIYDAIEAAKAR 291
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALALARKL 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 1330653883 292 GVDVVIADTAGRLQNKANLMEELRKIVRVMKKIDES 327
Cdd:smart00382 78 KPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS 113
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
212-410 |
7.05e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 70.60 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQF---QGQGKKVMLAAgDTFRAAAVEQLQVWGERNNVPVIAQHTGADsasvIYDAIEAA 288
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCvarEGADQLALLTT-DSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAAL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 289 KARgvDVVIADTAGRLQNKANLMEELRKIVRVmkkideSAPHEIMLTLdagtgqNAISQAKLFSDVA---------PITG 359
Cdd:PRK14723 262 GDK--HLVLIDTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLL------NAASHGDTLNEVVhayrhgageDVDG 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1330653883 360 ITLTKLDGTAKGGVIFAIADQFQIPIRFIGVGEGI-DDLRPFETQDFIDALF 410
Cdd:PRK14723 328 CIITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
213-394 |
2.59e-12 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 66.69 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 213 ILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDAIEAAKarg 292
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEEAR--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 293 VDVVIADTAGRLQNKANLMEELrkiVRVMKKIDesaPHEIMLTLDAG-TGQNAISQAKLFSDVApITGITLTKLDGTAKG 371
Cdd:PRK06731 155 VDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASmKSKDMIEIITNFKDIH-IDGIVFTKFDETASS 227
|
170 180
....*....|....*....|...
gi 1330653883 372 GVIFAIADQFQIPIRFIGVGEGI 394
Cdd:PRK06731 228 GELLKIPAVSSAPIVLMTDGQDV 250
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
212-399 |
6.75e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 66.68 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAqhtgADSASVIYDAIE-AAKA 290
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQyMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRlqnkaNLMEElRKIVRVMKKIDESAPHEIMLTLDAGTGQNAISQAKLFSDVAPITGITLTKLDGTAK 370
Cdd:PRK12726 284 NCVDHILIDTVGR-----NYLAE-ESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTR 357
|
170 180 190
....*....|....*....|....*....|.
gi 1330653883 371 GGVIFAIADQFQIPIRFIGVGEGIDD--LRP 399
Cdd:PRK12726 358 IGDLYTVMQETNLPVLYMTDGQNITEniFRP 388
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
212-401 |
5.28e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 63.83 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLA-KQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAqhtgadsASVIYDAIEAAKA 290
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYP-------VKDIKKFKETLAR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 291 RGVDVVIADTAGRLQNKANLMEELRKIVRVMKKIDESaphEIMLTLDAGTG-QNAISQAKLFSDVApITGITLTKLDGTA 369
Cdd:PRK12724 298 DGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSV---ENLLVLSSTSSyHHTLTVLKAYESLN-YRRILLTKLDEAD 373
|
170 180 190
....*....|....*....|....*....|..
gi 1330653883 370 KGGVIFAIADQFQIPIRFIGVGEGIddlrPFE 401
Cdd:PRK12724 374 FLGSFLELADTYSKSFTYLSVGQEV----PFD 401
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
212-406 |
1.16e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 62.82 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQ--FQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSasviydAIEAAK 289
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDL------QLALAE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 290 ARGVDVVIADTAGRLQNKANLMEElrkiVRVMKKIDesAPHEIMLTLDA---GTGQNAISQAKLFSDVAP------ITGI 360
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQ----IAMLHGAD--TPVQRLLLLNAtshGDTLNEVVQAYRSAAGQPkaalpdLAGC 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1330653883 361 TLTKLDGTAKGGVIFAIADQFQIPIRFIGVGEGIDDLRPFETQDFI 406
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFL 332
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
123-195 |
8.63e-08 |
|
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: 49.09 E-value: 8.63e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330653883 123 KANIGAGFFGLFKDKQIDDDLFEELEEQLLIADVGMDTTTKIIGNLTEKASR---RDLKDGEALYGLLKEEMAEIL 195
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
210-394 |
9.50e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 50.67 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 210 PYVILMVGVNGVGKTTTIGKLAKQF----QGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGADSASVIYDai 285
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 286 eaakARGVDVVIADTAGRLQNKANLMEELRKIVRVMKKidesaPHEIMLTLDAGTGQNAISQakLFSDVAPI--TGITLT 363
Cdd:PRK12723 252 ----SKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGR-----DAEFHLAVSSTTKTSDVKE--IFHQFSPFsyKTVIFT 320
|
170 180 190
....*....|....*....|....*....|.
gi 1330653883 364 KLDGTAKGGVIFAIADQFQIPIRFIGVGEGI 394
Cdd:PRK12723 321 KLDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
212-410 |
1.40e-05 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 46.87 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQ--FQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPViaqHTGADSASViydAIEAAK 289
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADL---QLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 290 ARGVDVVIADTAGRLQNKANLMEELRKIVRVMKKIDesapHEIMLtldagtgqNAISQAKLFSDVAP------ITGITLT 363
Cdd:PRK14721 267 LRGKHMVLIDTVGMSQRDQMLAEQIAMLSQCGTQVK----HLLLL--------NATSSGDTLDEVISayqghgIHGCIIT 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1330653883 364 KLDGTAKGGVIFAIADQFQIPIRFIGVGEGI-DDLRPFETQDFIDALF 410
Cdd:PRK14721 335 KVDEAASLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
212-276 |
3.02e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 43.03 E-value: 3.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQF---QGQGkKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQHTGAD 276
Cdd:PRK06995 258 VFALMGPTGVGKTTTTAKLAARCvmrHGAS-KVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAAD 324
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
153-191 |
7.98e-04 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 37.83 E-value: 7.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1330653883 153 IADVGMDTTTKIIGNLTEKA-SRRDLKDGEALYGLLKEEM 191
Cdd:pfam02881 36 EADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
212-316 |
2.45e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 39.96 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAA--GdtfRAAAVeqLQvwgERNNVPV--IAQHTGADSASVIYDAIEA 287
Cdd:COG0507 142 VSVLTGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKR--LS---ESTGIEArtIHRLLGLRPDSGRFRHNRD 213
|
90 100 110
....*....|....*....|....*....|.
gi 1330653883 288 AKARGVDVVIADTAG--RLQNKANLMEELRK 316
Cdd:COG0507 214 NPLTPADLLVVDEASmvDTRLMAALLEALPR 244
|
|
| MMAA-like |
cd03114 |
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ... |
188-302 |
2.54e-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: 39.48 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 188 KEEMAEILSHVekpleVDTTKTPYVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAGD---TFRAAAveqlqVWGERN 264
Cdd:cd03114 29 RELAQELLDAL-----LPQAGRAFRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVDpssPRSGGS-----ILGDKT 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1330653883 265 NVPVIAQHTGA---DSAS---------VIYDAIEAAKARGVDVVIADTAG 302
Cdd:cd03114 99 RMQRLARDPNAfirPSPSrgtlggvarATREAILLCEAAGYDVVLVETVG 148
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
217-299 |
2.67e-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: 38.79 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 217 GVNGVGKTTTIGKLAKQFQGQGKKVML--AAGDTFRAAAVEQLQVWGERNNVPVI----------AQHTgadsASVIYDA 284
Cdd:cd01672 7 GIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRaelllfaadrAQHV----EEVIKPA 82
|
90
....*....|....*
gi 1330653883 285 IEAAKargvdVVIAD 299
Cdd:cd01672 83 LARGK-----IVLSD 92
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
212-319 |
2.81e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 38.70 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAgDTFRAAAveqlqvwgernnvpVIAQHTGADS---ASVIYDAIEAA 288
Cdd:pfam13604 20 VAVLVGPAGTGKTTALKALREAWEAAGYRVIGLA-PTGRAAK--------------VLGEELGIPAdtiAKLLHRLGGRA 84
|
90 100 110
....*....|....*....|....*....|.
gi 1330653883 289 KARGVDVVIADTAGRLQNKanLMEELRKIVR 319
Cdd:pfam13604 85 GLDPGTLLIVDEAGMVGTR--QMARLLKLAE 113
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
220-304 |
3.11e-03 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 38.69 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 220 GVGKTTTIGKLAKQFQGQGKKVMLA-------AGDTFRAAaveqlqvwGERNNVPVIaqhtGADSASVIYDAIEAakARG 292
Cdd:NF041546 10 GVGKTTLATHLAAALARRGYRVLLVdadpqgsALDWAAAR--------EDERPFPVV----GLARPTLHRELPSL--ARD 75
|
90
....*....|..
gi 1330653883 293 VDVVIADTAGRL 304
Cdd:NF041546 76 YDFVVIDGPPRA 87
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
210-316 |
3.27e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.89 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 210 PYVILMVGVNGVGKTTtigkLAKQFQGQGKKVMLaagDTFRAaaveqlQVWGERNNvpviaQHTGADSASVIYDAIEAAK 289
Cdd:COG4639 2 LSLVVLIGLPGSGKST----FARRLFAPTEVVSS---DDIRA------LLGGDEND-----QSAWGDVFQLAHEIARARL 63
|
90 100
....*....|....*....|....*..
gi 1330653883 290 ARGVDVVIADTagrlqnkaNLMEELRK 316
Cdd:COG4639 64 RAGRLTVVDAT--------NLQREARR 82
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
208-323 |
4.91e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.11 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 208 KTPYVILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLaAGDTFRAAAVEQLQVwgERNNVPVIAQHTGADSASVIYDAIEA 287
Cdd:pfam06414 9 ERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELHPHYREL--QAADPKTASEYTQPDASRWVEKLLQH 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 1330653883 288 AKARGVDVVIaDTAGRLQNKAnlmeelRKIVRVMKK 323
Cdd:pfam06414 86 AIENGYNIIL-EGTLRSPDVA------KKIARALKA 114
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
212-316 |
5.04e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 37.29 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQgkkvmLAAGDTFRAaaveqlQVWGERNNVPVIAQHTGADSASVIYDAIEAAKAR 291
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELGAV-----RLSSDDERK------RLFGEGRPSISYYTDATDRTYERLHELARIALRA 69
|
90 100
....*....|....*....|....*
gi 1330653883 292 GVDVVIADTagrlqnkaNLMEELRK 316
Cdd:pfam13671 70 GRPVILDAT--------NLRRDERA 86
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
212-254 |
5.19e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.53 E-value: 5.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1330653883 212 VILMVGVNGVGKTTTIGKLAKQFQGQGKKVMLAAgDTFRAAAV 254
Cdd:cd17933 14 VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
220-303 |
6.70e-03 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 37.91 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330653883 220 GVGKTTTIGKLAKQFQGQGKKVMLAAGDTFRAAAVEQLQVWGERNNVPVIAQhtgadSASVIYDAIEAakARGVDVVIAD 299
Cdd:PHA02518 11 GAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVRM-----GKSIRADLPKV--ASGYDYVVVD 83
|
....
gi 1330653883 300 TAGR 303
Cdd:PHA02518 84 GAPQ 87
|
|
| |
