|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
42-345 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 502.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 42 LFQRLKSGLARTRANFTDGLASLVLGRRKIDDELLEDLETLLLTADVGVDATRRIIDELTERVKRKTLADPEALVAALKE 121
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 122 LLEEILEKVDAPVQqPAPGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVI 201
Cdd:COG0552 81 ELLEILDPVDKPLA-IEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 202 AQHSGADSASVIYDALEAATARGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIDPDAPHEVMLVVDATTGQNAVNQAE 281
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796678138 282 QFSRAIPLTGITLTKLDGTARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDALFERE 345
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
22-346 |
1.45e-175 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 489.61 E-value: 1.45e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 22 MFGFGKKNQsapteEQKKPGLFQRLKSGLARTRANFTDGLASLvLGRRKIDDELLEDLETLLLTADVGVDATRRIIDELT 101
Cdd:PRK10416 1 FFSWLKKKK-----KEKKEGWFERLKKGLSKTRENFGEGINGL-FAKKKIDEDLLEELEELLIEADVGVETTEEIIEELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 102 ERVKRKTLADPEALVAALKELLEEILEKVDAPVQqPAPGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTF 181
Cdd:PRK10416 75 ERVKRKNLKDPEELKELLKEELAEILEPVEKPLN-IEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 182 RAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATARGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIDPDAP 261
Cdd:PRK10416 154 RAAAIEQLQVWGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 262 HEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDAL 341
Cdd:PRK10416 234 HEVLLVLDATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDAL 313
|
....*
gi 2796678138 342 FEREE 346
Cdd:PRK10416 314 LGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
86-342 |
6.06e-129 |
|
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: 370.05 E-value: 6.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 86 ADVGVDATRRIIDELTERVKRKTLADPEALVAALKELLEEILEKVDAPVQQ----PAPGHPQVILMVGINGAGKTTTIGK 161
Cdd:TIGR00064 17 SDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDleliVEENKPNVILFVGVNGVGKTTTIAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 162 LAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATARGVDVLIADTAGRLHTKSN 241
Cdd:TIGR00064 97 LANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNIDVVLIDTAGRLQNKVN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 242 LMEELAKIARVMKKIDPDAPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARGGIIFAIAEKMGIPIRFIG 321
Cdd:TIGR00064 177 LMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGIILSIAYELKLPIKFIG 256
|
250 260
....*....|....*....|.
gi 2796678138 322 VGEGIEDLRIFDPRAFVDALF 342
Cdd:TIGR00064 257 VGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
144-341 |
3.54e-120 |
|
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: 344.55 E-value: 3.54e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATAR 223
Cdd:cd17874 2 VILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 224 GVDVLIADTAGRLHTKSNLMEELAKIARVMKKIDPDAPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARG 303
Cdd:cd17874 82 GIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAKG 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796678138 304 GIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDAL 341
Cdd:cd17874 162 GIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
142-343 |
1.04e-105 |
|
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: 307.80 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 142 PQVILMVGINGAGKTTTIGKLAKQLQDEGQ-TVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAA 220
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGGkKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 221 TARGVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGT 300
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2796678138 301 ARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDALFE 343
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
144-341 |
5.12e-102 |
|
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: 5.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATAR 223
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 224 GVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARG 303
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKG 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796678138 304 GIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDAL 341
Cdd:pfam00448 156 GAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
144-341 |
1.44e-90 |
|
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: 269.24 E-value: 1.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATAR 223
Cdd:cd03115 2 VILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 224 GVDVLIADTAGRLHTKSNLMEELAKIARVmkkidpDAPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARG 303
Cdd:cd03115 82 GYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAKG 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796678138 304 GIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDAL 341
Cdd:cd03115 156 GAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
27-343 |
2.43e-87 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 266.07 E-value: 2.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 27 KKNQSAPTEEQKKPGLFQRLKSgLARTRANFTDGLASLVLGrrkiddelledletlLLTADVGVDATRRIIDELTERV-- 104
Cdd:PRK14974 34 EEEEEDEEEKKEKPGFFDKAKI-TEIKEKDIEDLLEELELE---------------LLESDVALEVAEEILESLKEKLvg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 105 -KRKTLADPEALVAALKELLEEILEKVDAPVQQP----APGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGD 179
Cdd:PRK14974 98 kKVKRGEDVEEIVKNALKEALLEVLSVGDLFDLIeeikSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 180 TFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATARGVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpd 259
Cdd:PRK14974 178 TFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTK----- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 260 aPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVD 339
Cdd:PRK14974 253 -PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVD 331
|
....
gi 2796678138 340 ALFE 343
Cdd:PRK14974 332 KLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
138-334 |
3.77e-82 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 255.72 E-value: 3.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 138 APGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDAL 217
Cdd:COG0541 96 AKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRAL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 218 EAATARGVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKL 297
Cdd:COG0541 176 EYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKL 249
|
170 180 190
....*....|....*....|....*....|....*..
gi 2796678138 298 DGTARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDP 334
Cdd:COG0541 250 DGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHP 286
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
144-334 |
1.44e-74 |
|
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: 228.64 E-value: 1.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATAR 223
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 224 GVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTARG 303
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|.
gi 2796678138 304 GIIFAIAEKMGIPIRFIGVGEGIEDLRIFDP 334
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHP 186
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
139-346 |
3.99e-69 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 222.39 E-value: 3.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 139 PGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALE 218
Cdd:PRK00771 92 PLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 219 AAtaRGVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLD 298
Cdd:PRK00771 172 KF--KKADVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLD 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796678138 299 GTARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFV---------DALFEREE 346
Cdd:PRK00771 244 GTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFIsrllgmgdlESLLEKVE 300
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
143-338 |
5.40e-58 |
|
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: 185.86 E-value: 5.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 143 QVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATA 222
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 223 RGVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTAR 302
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2796678138 303 GGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFV 338
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
144-341 |
3.71e-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: 161.24 E-value: 3.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDALEAATAR 223
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARDQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 224 GVDVLIADTAGRLHTKSNLMEELAKIARVMKkidPDApheVMLVVDATTGQNAVNQAEQFSRAI----------PLTGIT 293
Cdd:cd17876 82 GFDVVLIDTAGRMQNNEPLMRALAKLIKENN---PDL---VLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGIV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2796678138 294 LTKLD------GTArggiiFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDAL 341
Cdd:cd17876 156 LTKFDtiddkvGAA-----LSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
133-346 |
5.07e-39 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 141.54 E-value: 5.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 133 PVQQPAPGHPQVILMVGINGAGKTTTIGKLA-KQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPViaqhsgadsaS 211
Cdd:COG1419 155 VAEDPLLDEGGVIALVGPTGVGKTTTIAKLAaRFVLRGKKKVALITTDTYRIGAVEQLKTYARILGVPV----------E 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 212 VIYDALEAATA----RGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIdpdaphEVMLVVDATT-GQNAVNQAEQFSRa 286
Cdd:COG1419 225 VAYDPEELKEAlerlRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPI------EVYLVLSATTkYEDLKEIVEAFSS- 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796678138 287 IPLTGITLTKLDGTARGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFVDALFEREE 346
Cdd:COG1419 298 LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLLGGLE 358
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
137-341 |
7.53e-38 |
|
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: 139.97 E-value: 7.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 137 PAPGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDA 216
Cdd:TIGR01425 95 PKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 217 LEAATARGVDVLIADTAGRLHTKSNLMEELAKIARVMKkidpdaPHEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTK 296
Cdd:TIGR01425 175 VEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITK 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2796678138 297 LDGTARGGIIFAIAEKMGIPIRFIGVGEGIEDLRIFDPRAFVDAL 341
Cdd:TIGR01425 249 LDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
143-338 |
5.95e-36 |
|
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: 128.82 E-value: 5.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 143 QVILMVGINGAGKTTTIGKLAKQLQ-DEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAqhsgADSASVIYDALEAat 221
Cdd:cd17873 1 RVIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDPEDLADALER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 ARGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIdpdaphEVMLVVDATT-GQNAVNQAEQFSRaIPLTGITLTKLDGT 300
Cdd:cd17873 75 LSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDI------EVHLVLSATTkAKDLKEIIERFSP-LGYRGLILTKLDET 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 2796678138 301 ARGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFV 338
Cdd:cd17873 148 TSLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLA 186
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
144-346 |
9.43e-27 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 109.60 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQ--LQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSAsviyDALEAAT 221
Cdd:PRK05703 223 VVALVGPTGVGKTTTLAKLAARyaLLYGKKKVALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELA----KALEQLR 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 ARGVdVLIaDTAGRLHTKSNLMEELAKIARvmkkiDPDAPHEVMLVVDATTgQNAVNQA--EQFSRaIPLTGITLTKLDG 299
Cdd:PRK05703 299 DCDV-ILI-DTAGRSQRDKRLIEELKALIE-----FSGEPIDVYLVLSATT-KYEDLKDiyKHFSR-LPLDGLIFTKLDE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2796678138 300 TARGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFVDALFEREE 346
Cdd:PRK05703 370 TSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLLLGGFN 417
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
140-336 |
4.85e-17 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 81.32 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 140 GHpQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADsasvIYDALEA 219
Cdd:PRK12726 205 NH-RIISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVATSPAE----LEEAVQY 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 220 AT-ARGVDVLIADTAGRLHTKSnlmEELAKIARVMKKIDPDaphevMLVVDATTGQNAVNQAEQFSR--AIPLTGITLTK 296
Cdd:PRK12726 280 MTyVNCVDHILIDTVGRNYLAE---ESVSEISAYTDVVHPD-----LTCFTFSSGMKSADVMTILPKlaEIPIDGFIITK 351
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2796678138 297 LDGTARGGIIFAIAEKMGIPIRFIGVGEGIEDlRIFDPRA 336
Cdd:PRK12726 352 MDETTRIGDLYTVMQETNLPVLYMTDGQNITE-NIFRPKS 390
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
133-234 |
2.04e-15 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 75.45 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 133 PVQQPAPGHPQVILMVGINGAGKTTTIGKLAKQ--LQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAqhsgADSA 210
Cdd:TIGR03499 185 PEEDPILEQGGVIALVGPTGVGKTTTLAKLAARfaLEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKV----ARDP 260
|
90 100
....*....|....*....|....
gi 2796678138 211 SVIYDALEAatARGVDVLIADTAG 234
Cdd:TIGR03499 261 KELREALDR--LRDKDLILIDTAG 282
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
143-327 |
1.23e-14 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 74.33 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 143 QVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIA-QHSGADSASVIYDALEAAt 221
Cdd:PRK11889 242 QTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAvRDEAAMTRALTYFKEEAR- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 argVDVLIADTAGRLHTKSNLMEELAKiarVMKKIDPDApheVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTA 301
Cdd:PRK11889 321 ---VDYILIDTAGKNYRASETVEEMIE---TMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETA 391
|
170 180
....*....|....*....|....*.
gi 2796678138 302 RGGIIFAIAEKMGIPIRFIGVGEGIE 327
Cdd:PRK11889 392 SSGELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
142-341 |
1.33e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 71.09 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 142 PQVILMVGINGAGKTTTIGKLAK----QLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSASVIYDal 217
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAiygiNSDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 218 eaatARGVDVLIADTAGRlhTKSNLMeELAKIARVMKKIDPDAphEVMLVVDATTGQNAVNQA-EQFSrAIPLTGITLTK 296
Cdd:PRK12723 252 ----SKDFDLVLVDTIGK--SPKDFM-KLAEMKELLNACGRDA--EFHLAVSSTTKTSDVKEIfHQFS-PFSYKTVIFTK 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2796678138 297 LDGTARGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFVDAL 341
Cdd:PRK12723 322 LDETTCVGNLISLIYEMRKEVSYVTDGQIVpHNISIAEPLTFIKKI 367
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
143-327 |
5.44e-13 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 68.23 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 143 QVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIA-QHSGADSASVIYDALEAAt 221
Cdd:PRK06731 76 QTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAvRDEAAMTRALTYFKEEAR- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 argVDVLIADTAGRLHTKSNLMEELAKiarVMKKIDPDApheVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTA 301
Cdd:PRK06731 155 ---VDYILIDTAGKNYRASETVEEMIE---TMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETA 225
|
170 180
....*....|....*....|....*.
gi 2796678138 302 RGGIIFAIAEKMGIPIRFIGVGEGIE 327
Cdd:PRK06731 226 SSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
130-326 |
1.37e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 68.07 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 130 VDAPVQQPAP-GHPQVILMVGINGAGKTTTIGKL-AKQLQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAqhsga 207
Cdd:PRK12724 210 VDSDLFSGTGkNQRKVVFFVGPTGSGKTTSIAKLaAKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYP----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 208 dsASVIYDALEAATARGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIDPDaphEVMLVVDATTGQNAVNQAEQFSRAI 287
Cdd:PRK12724 285 --VKDIKKFKETLARDGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSV---ENLLVLSSTSSYHHTLTVLKAYESL 359
|
170 180 190
....*....|....*....|....*....|....*....
gi 2796678138 288 PLTGITLTKLDGTARGGIIFAIAEKMGIPIRFIGVGEGI 326
Cdd:PRK12724 360 NYRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
141-286 |
1.41e-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: 61.62 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 141 HPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFRAAAVEQLQtwgernDIPVIAQHSGADSASVIYDALEAA 220
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796678138 221 TARGVDVLIADTAGRLHTKSNLMEELAKIarVMKKIDPDAPHEVMLVVDATTGQNAVNQAEQFSRA 286
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLE--ELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
144-328 |
2.59e-11 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 64.63 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQL--QDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPViaqHSgADSASVIYDALEaaT 221
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAESLLDLLE--R 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 ARGVDVLIADTAGRLHTKSNLMEELA--KIARVMKKidpdaphevMLVVDATTGQNAVNQ-AEQFSRAIPlTGITLTKLD 298
Cdd:PRK12727 426 LRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTS---------LLVLPANAHFSDLDEvVRRFAHAKP-QGVVLTKLD 495
|
170 180 190
....*....|....*....|....*....|
gi 2796678138 299 GTARGGIIFAIAEKMGIPIRFIGVGEGIED 328
Cdd:PRK12727 496 ETGRFGSALSVVVDHQMPITWVTDGQRVPD 525
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
144-342 |
3.39e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 63.59 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQ--LQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPVIAQHSGADSasviydALEAAT 221
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDL------QLALAE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 ARGVDVLIADTAGRLHTKSNLMEELAKIArvmkkiDPDAPHEVMLVVDATTGQNAVNQAEQFSR--------AIP-LTGI 292
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQIAMLH------GADTPVQRLLLLNATSHGDTLNEVVQAYRsaagqpkaALPdLAGC 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2796678138 293 TLTKLDGTARGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFVDALF 342
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVpENLYVATKKFLLKSAF 337
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
144-342 |
3.68e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 58.27 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQ--LQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPViaqHSGADSASvIYDALEAAT 221
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARcvAREGADQLALLTTDSFRIGALEQLRIYGRILGVPV---HAVKDAAD-LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 ARGVdVLIaDTAGRLHTKSNLMEELAKIARVmkkidpDAPHEVMLVVDATTGQNAVNQAEQFSR---AIPLTGITLTKLD 298
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLLNAASHGDTLNEVVHAYRhgaGEDVDGCIITKLD 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2796678138 299 GTARGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFVDALF 342
Cdd:PRK14723 335 EATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
144-343 |
1.81e-06 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 49.18 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQ--LQDEGQTVMLAAGDTFRAAAVEQLQTWGERNDIPViaqHSGADSASViydALEAAT 221
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADL---QLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 222 ARGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIdpdaphEVMLVVDATTGQNAVNQAEQFSRAIPLTGITLTKLDGTA 301
Cdd:PRK14721 267 LRGKHMVLIDTVGMSQRDQMLAEQIAMLSQCGTQV------KHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2796678138 302 RGGIIFAIAEKMGIPIRFIGVGEGI-EDLRIFDPRAFVDALFE 343
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIFK 383
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
143-251 |
1.33e-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: 42.17 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 143 QVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAgDTFRAAAveqlqtwgerndipVIAQHSGADS---ASVIYDALEA 219
Cdd:pfam13604 19 RVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLA-PTGRAAK--------------VLGEELGIPAdtiAKLLHRLGGR 83
|
90 100 110
....*....|....*....|....*....|..
gi 2796678138 220 ATARGVDVLIADTAGRLHTKsnLMEELAKIAR 251
Cdd:pfam13604 84 AGLDPGTLLIVDEAGMVGTR--QMARLLKLAE 113
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
141-251 |
2.39e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 40.97 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 141 HPQVILMVGINGAGKTTtigkLAKQLQDEGQTVMLaagDTFRAaaveqlQTWGERNDipviaQHSGADSASVIYDALEAA 220
Cdd:COG4639 1 MLSLVVLIGLPGSGKST----FARRLFAPTEVVSS---DDIRA------LLGGDEND-----QSAWGDVFQLAHEIARAR 62
|
90 100 110
....*....|....*....|....*....|.
gi 2796678138 221 TARGVDVLIADTagrlHTKSNLMEELAKIAR 251
Cdd:COG4639 63 LRAGRLTVVDAT----NLQREARRRLLALAR 89
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
135-248 |
3.68e-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: 40.81 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 135 QQPAPGHPQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLaAGDTFRAAAVEQLQTwgERNDIPVIAQHSGADSASVIY 214
Cdd:pfam06414 4 KTTSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELHPHYREL--QAADPKTASEYTQPDASRWVE 80
|
90 100 110
....*....|....*....|....*....|....
gi 2796678138 215 DALEAATARGVDVLIADTAGRLHTKSNLMEELAK 248
Cdd:pfam06414 81 KLLQHAIENGYNIILEGTLRSPDVAKKIARALKA 114
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
289-331 |
1.04e-03 |
|
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.
Pssm-ID: 349762 Cd Length: 316 Bit Score: 40.56 E-value: 1.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796678138 289 LTGITLTKLDGTARGGIIFaIAEKMGIPIRFIGVGEGIEDLRI 331
Cdd:cd03108 275 LTELALTKLDVNAQKYIER-IEELLGVPITYISVGPDREQTII 316
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
142-182 |
1.64e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 38.88 E-value: 1.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2796678138 142 PQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFR 182
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELR 47
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
86-118 |
1.70e-03 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 36.68 E-value: 1.70e-03
10 20 30
....*....|....*....|....*....|....
gi 2796678138 86 ADVGVDATRRIIDELTER-VKRKTLADPEALVAA 118
Cdd:pfam02881 37 ADVGVEVVKKIIERLREKaVGEKKLKPPQEVKKI 70
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
149-202 |
2.47e-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: 38.40 E-value: 2.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2796678138 149 GINGAGKTTTIGKLAKQLQDEGQTVML--AAGDTFRAAAVEQLQTWGERNDIPVIA 202
Cdd:cd01672 7 GIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
144-182 |
2.91e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 38.08 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFR 182
Cdd:PRK00889 6 TVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVR 44
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
145-236 |
3.55e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 38.12 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 145 ILMVGIN---GAGKTTTIGKLAKQLQDEgqtvmlaagdtFRAAAVE-QLQTwgeRND--------IPVIAQHSGA----D 208
Cdd:COG0378 13 VLAVNLMgspGSGKTTLLEKTIRALKDR-----------LRIAVIEgDIYT---TEDaerlraagVPVVQINTGGcchlD 78
|
90 100
....*....|....*....|....*...
gi 2796678138 209 sASVIYDALEAATARGVDVLIADTAGRL 236
Cdd:COG0378 79 -ASMVLEALEELDLPDLDLLFIENVGNL 105
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
86-118 |
3.58e-03 |
|
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: 35.99 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2796678138 86 ADVGVDATRRIIDELTERVKR---KTLADPEALVAA 118
Cdd:smart00963 33 ADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKI 68
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
152-251 |
5.07e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 38.42 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 152 GAGKTTTIGKLAKQLQDEGQTVMLAA--GdtfRAAAVeqLQtwgERNDIPV--IAQHSGADSASVIYDALEAATARGVDV 227
Cdd:COG0507 150 GTGKTTTLRALLAALEALGLRVALAAptG---KAAKR--LS---ESTGIEArtIHRLLGLRPDSGRFRHNRDNPLTPADL 221
|
90 100
....*....|....*....|....
gi 2796678138 228 LIADTAGRLHTKsnLMEELAKIAR 251
Cdd:COG0507 222 LVVDEASMVDTR--LMAALLEALP 243
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
144-182 |
5.22e-03 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 37.07 E-value: 5.22e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2796678138 144 VILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFR 182
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVR 39
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
144-265 |
6.07e-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: 36.52 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 144 VILMVGINGAGKTTtigkLAKQLQDEGQTVMLAAgDTFRAAAveqlqtWGERNDIPVIAQHSGADSASVIYDALEAATAR 223
Cdd:pfam13671 1 LILLVGLPGSGKST----LARRLLEELGAVRLSS-DDERKRL------FGEGRPSISYYTDATDRTYERLHELARIALRA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2796678138 224 GVDVlIADTAgrlHTKSNLMEELAKIARVM----KKIDPDAPHEVM 265
Cdd:pfam13671 70 GRPV-ILDAT---NLRRDERARLLALAREYgvpvRIVVFEAPEEVL 111
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
142-182 |
7.21e-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: 36.53 E-value: 7.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2796678138 142 PQVILMVGINGAGKTTTIGKLAKQLQDEGQTVMLAAGDTFR 182
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
132-260 |
8.60e-03 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 37.81 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796678138 132 APVQQPAPGHPQVILMVGINGAGKTTTIGKLAKQLQDEGqtvmlaagdtFRAAAVEQLQtwgERNDIpviaQHSGADSAS 211
Cdd:PRK14489 195 AIPDGTTTGAPPLLGVVGYSGTGKTTLLEKLIPELIARG----------YRIGLIKHSH---HRVDI----DKPGKDSHR 257
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2796678138 212 viydaLEAAtarGVDVLIADTAGRLHTKSNLMEELAKIARVMKKIDPDA 260
Cdd:PRK14489 258 -----LRAA---GANPTMIVCPERWALMRETPEEAVPFKVLIATFDPEE 298
|
|
| |
