|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
149-451 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 522.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 149 FFARLRQGLSKTSASIGEGMASLFLGRKEIDDDLLDDIETRLLTADVGVEATTLIVQNLTKRVARKELADSGALYKALQE 228
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 229 ELASLLRPVEQPLQVDVARePYVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVI 308
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKK-PFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 309 AQHTGADSASVIFDAVQAAKARGIDVLIADTAGRLHTKDNLMEELKKVRRVIGKLDETAPHEVLLVLDAGTGQNAINQAK 388
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595570 389 QFNLAVELTGLALTKLDGTAKGGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQALFAE 451
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGE 302
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
146-453 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 514.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 146 RPGFFARLRQGLSKTSASIGEGMASLFLGRKEIDDDLLDDIETrLLTADVGVEATTLIVQNLTKRVARKELADSGALYKA 225
Cdd:PRK10416 13 KEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEEL-LIEADVGVETTEEIIEELRERVKRKNLKDPEELKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 226 LQEELASLLRPVEQPLQVDVARePYVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRI 305
Cdd:PRK10416 92 LKEELAEILEPVEKPLNIEEKK-PFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERVGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 306 PVIAQHTGADSASVIFDAVQAAKARGIDVLIADTAGRLHTKDNLMEELKKVRRVIGKLDETAPHEVLLVLDAGTGQNAIN 385
Cdd:PRK10416 171 PVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQNALS 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595570 386 QAKQFNLAVELTGLALTKLDGTAKGGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQALFAERE 453
Cdd:PRK10416 251 QAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
190-449 |
5.52e-133 |
|
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: 384.30 E-value: 5.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 190 LLTADVGVEATTLIVQNLTKRVARKELADSGALYKALQEELASLLRPVE----QPLQVDVAREPYVILVVGVNGVGKTTT 265
Cdd:TIGR00064 14 LLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVILFVGVNGVGKTTT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 266 IGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKARGIDVLIADTAGRLHT 345
Cdd:TIGR00064 94 IAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNIDVVLIDTAGRLQN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 346 KDNLMEELKKVRRVIGKLDETAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKGGVIFALAKQFGLPIR 425
Cdd:TIGR00064 174 KVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGIILSIAYELKLPIK 253
|
250 260
....*....|....*....|....
gi 15595570 426 YIGVGEGIDDLRTFEADAFVQALF 449
Cdd:TIGR00064 254 FIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
250-448 |
1.31e-118 |
|
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: 344.94 E-value: 1.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 250 YVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKA 329
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 330 RGIDVLIADTAGRLHTKDNLMEELKKVRRVIGKLDETAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAK 409
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 15595570 410 GGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQAL 448
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
249-449 |
6.78e-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: 312.42 E-value: 6.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 249 PYVILVVGVNGVGKTTTIGKLAKKLQLEG-KKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAA 327
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 328 KARGIDVLIADTAGRLHTKDNLMEELKKVRRVIgkldetAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGT 407
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVI------KPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15595570 408 AKGGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQALF 449
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
251-448 |
1.70e-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: 301.00 E-value: 1.70e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKAR 330
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 331 GIDVLIADTAGRLHTKDNLMEELKKVRRVIgkldetAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKG 410
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVV------APDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKG 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 15595570 411 GVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQAL 448
Cdd:pfam00448 156 GAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
250-448 |
8.55e-91 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 273.87 E-value: 8.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 250 YVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKA 329
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 330 RGIDVLIADTAGRLHTKDNLMEELKKVRRVIGkldetaPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAK 409
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVES------PDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 15595570 410 GGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQAL 448
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
190-451 |
1.53e-89 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 275.70 E-value: 1.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 190 LLTADVGVEATTLIVQNLTKRVA---RKELADSGAL-YKALQEELASLL---RPVEQPLQVDVAREPYVILVVGVNGVGK 262
Cdd:PRK14974 74 LLESDVALEVAEEILESLKEKLVgkkVKRGEDVEEIvKNALKEALLEVLsvgDLFDLIEEIKSKGKPVVIVFVGVNGTGK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 263 TTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKARGIDVLIADTAGR 342
Cdd:PRK14974 154 TTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 343 LHTKDNLMEELKKVRRVigkldeTAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKGGVIFALAKQFGL 422
Cdd:PRK14974 234 MHTDANLMDELKKIVRV------TKPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGK 307
|
250 260
....*....|....*....|....*....
gi 15595570 423 PIRYIGVGEGIDDLRTFEADAFVQALFAE 451
Cdd:PRK14974 308 PILFLGVGQGYDDLIPFDPDWFVDKLLGE 336
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
190-446 |
2.03e-79 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 252.63 E-value: 2.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 190 LLTADVGVEattlIVQNLTKRVARK----ELADS----GALYKALQEELASLLRPVEQPLQVDvAREPYVILVVGVNGVG 261
Cdd:COG0541 38 LLEADVNLK----VVKDFIERVKERalgeEVLKSltpgQQVIKIVHDELVELLGGENEELNLA-KKPPTVIMMVGLQGSG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 262 KTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKARGIDVLIADTAG 341
Cdd:COG0541 113 KTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 342 RLHTKDNLMEELKKVRRVIgkldetAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKGGVIFALAKQFG 421
Cdd:COG0541 193 RLHIDEELMDELKAIKAAV------NPDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTG 266
|
250 260
....*....|....*....|....*
gi 15595570 422 LPIRYIGVGEGIDDLRTFEADAFVQ 446
Cdd:COG0541 267 KPIKFIGTGEKLDDLEPFHPDRMAS 291
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
251-442 |
9.63e-70 |
|
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: 219.78 E-value: 9.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKAR 330
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 331 GIDVLIADTAGRLHTKDNLMEELKKVRRVIGkldetaPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKG 410
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|..
gi 15595570 411 GVIFALAKQFGLPIRYIGVGEGIDDLRTFEAD 442
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
190-445 |
6.84e-64 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 212.37 E-value: 6.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 190 LLTADVGVEattlIVQNLTKRV---ARKELADSGA-----LYKALQEELASLLRPVEQPLQVDvaREPYVILVVGVNGVG 261
Cdd:PRK00771 34 LLQADVNVK----LVKELSKSIkerALEEEPPKGLtprehVIKIVYEELVKLLGEETEPLVLP--LKPQTIMLVGLQGSG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 262 KTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKARgiDVLIADTAG 341
Cdd:PRK00771 108 KTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKFKKA--DVIIVDTAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 342 RLHTKDNLMEELKKVRRVIgkldetAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKGGVIFALAKQFG 421
Cdd:PRK00771 186 RHALEEDLIEEMKEIKEAV------KPDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETG 259
|
250 260
....*....|....*....|....
gi 15595570 422 LPIRYIGVGEGIDDLRTFEADAFV 445
Cdd:PRK00771 260 APIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
250-448 |
1.44e-55 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 182.78 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 250 YVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKA 329
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 330 RGIDVLIADTAGRLHTKDNLMEELKKVRRVIgkldetAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAK 409
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAV------KPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 15595570 410 GGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQAL 448
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
250-448 |
3.07e-49 |
|
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: 167.02 E-value: 3.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 250 YVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKA 329
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 330 RGIDVLIADTAGRLHTKDNLMEELKKVrrvigkLDETAPHEVLLVLDAGTGQNAINQAKQFNLAV----------ELTGL 399
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKL------IKENNPDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15595570 400 ALTKLDGTA-KGGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFVQAL 448
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
188-448 |
1.53e-42 |
|
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: 155.76 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 188 TRLLTADVGVEATTLIVQNLTKRVARKELADSGALYKALQ----EELASLLRPVEQPLQVDVARePYVILVVGVNGVGKT 263
Cdd:TIGR01425 36 TALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQdavfEELCNLVDPGVEAFTPKKGK-TCVIMFVGLQGAGKT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 264 TTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDAVQAAKARGIDVLIADTAGRL 343
Cdd:TIGR01425 115 TTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 344 HTKDNLMEELKKVRrvigklDETAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAKGGVIFALAKQFGLP 423
Cdd:TIGR01425 195 KQEKELFEEMQQVR------EAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSP 268
|
250 260
....*....|....*....|....*
gi 15595570 424 IRYIGVGEGIDDLRTFEADAFVQAL 448
Cdd:TIGR01425 269 IIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
166-455 |
6.30e-40 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 146.93 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 166 EGMASLFLGRKEIDDDLLDDIETRLLTADVGVEATTLIVQNLtkrvarKELADSGALYKALQEELASLLRPVEQPLQvdv 245
Cdd:COG1419 91 EEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKL------PEDLSAEEAWRALLEALARRLPVAEDPLL--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 246 aREPYVILVVGVNGVGKTTTIGKLAKKLQLEG-KKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIfdav 324
Cdd:COG1419 162 -DEGGVIALVGPTGVGKTTTIAKLAARFVLRGkKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 325 qaAKARGIDVLIADTAGRLHTKDNLMEELKKVRRVIGkldetaPHEVLLVLDAGT-GQNAINQAKQFNlAVELTGLALTK 403
Cdd:COG1419 237 --ERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGP------PIEVYLVLSATTkYEDLKEIVEAFS-SLGLDGLILTK 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15595570 404 LDGTAKGGVIFALAKQFGLPIRYIGVGEGI-DDLRTFEADAFVQALFAERENA 455
Cdd:COG1419 308 LDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLLGGLEEE 360
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
251-448 |
7.54e-32 |
|
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: 119.96 E-value: 7.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLE-GKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIfdavqaAKA 329
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVLKkGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADAL------ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 330 RGIDVLIADTAGRLHTKDNLMEELKKVrrvigkLDETAPHEVLLVLDAGT-GQNAINQAKQFNlAVELTGLALTKLDGTA 408
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKEL------LGAGEDIEVHLVLSATTkAKDLKEIIERFS-PLGYRGLILTKLDETT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15595570 409 KGGVIFALAKQFGLPIRYIGVGEGI-DDLRTFEADAFVQAL 448
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
203-451 |
7.74e-28 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 114.61 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 203 IVQNLTKRVARKELADSGALYKALQEELASLLRPVEQplqvDVAREPYVILVVGVNGVGKTTTIGKLAKKLQL--EGKKV 280
Cdd:PRK05703 179 IAEKLLKLLLEHMPPRERTAWRYLLELLANMIPVRVE----DILKQGGVVALVGPTGVGKTTTLAKLAARYALlyGKKKV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 281 MLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSAsvifDAVQAAKARGIdVLIaDTAGRLHTKDNLMEELKKVrrvI 360
Cdd:PRK05703 255 ALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELA----KALEQLRDCDV-ILI-DTAGRSQRDKRLIEELKAL---I 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 361 GKLDEtaPHEVLLVLDAgTGQN----AInqAKQFNLaVELTGLALTKLDGTAKGGVIFALAKQFGLPIRYIGVGEGI-DD 435
Cdd:PRK05703 326 EFSGE--PIDVYLVLSA-TTKYedlkDI--YKHFSR-LPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDD 399
|
250
....*....|....*.
gi 15595570 436 LRTFEADAFVQALFAE 451
Cdd:PRK05703 400 IKVANPEELVRLLLGG 415
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
87-341 |
6.01e-19 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 86.62 E-value: 6.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 87 AGDEPASAEEHSPRPEAPVAQPEPILAAEPEPEPEPEPEPEPEPVAPLAAAPAVSEPAtrpgffARLRQGLSKTSASIGE 166
Cdd:TIGR03499 49 AIDEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPE------EELRKELEALRELLER 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 167 GMASLFLGRKEIDDDLLDDietRLLTAdvGVEATtlIVQNLTKRVarKELADSGALYKALQEELASLLRpvEQPLQVDVA 246
Cdd:TIGR03499 123 LLAGLAWLQRPPERAKLYE---RLLEA--GVSEE--LARELLEKL--PEDADAEDAWRWLREALEGMLP--VKPEEDPIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 247 REPYVILVVGVNGVGKTTTIGKLA--KKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSAsvifDAV 324
Cdd:TIGR03499 192 EQGGVIALVGPTGVGKTTTLAKLAarFALEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKELR----EAL 267
|
250
....*....|....*..
gi 15595570 325 QAAKARGIdVLIaDTAG 341
Cdd:TIGR03499 268 DRLRDKDL-ILI-DTAG 282
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
251-433 |
1.16e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 72.69 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLE-GKKVMLAAGDTFRAAAVEQLQVWgernripviaqhtgADSASVIFDAVQAAK- 328
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAAKYFLHmGKSVSLYTTDNYRIAAIEQLKRY--------------ADTMGMPFYPVKDIKk 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 329 -----AR-GIDVLIADTAGRLHTKDNLMEELKKVRRVIGKLDETaphEVLLVLDAGTGQNAINQAKQFNLAVELTGLALT 402
Cdd:PRK12724 291 fketlARdGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSV---ENLLVLSSTSSYHHTLTVLKAYESLNYRRILLT 367
|
170 180 190
....*....|....*....|....*....|.
gi 15595570 403 KLDGTAKGGVIFALAKQFGLPIRYIGVGEGI 433
Cdd:PRK12724 368 KLDEADFLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
251-363 |
4.25e-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: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVwgernrIPVIAQHTGADSASVIFDAVQAAKAR 330
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALARKL 77
|
90 100 110
....*....|....*....|....*....|...
gi 15595570 331 GIDVLIADTAGRLHTKDNLMEELKKVRRVIGKL 363
Cdd:smart00382 78 KPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
251-435 |
1.28e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 65.91 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAqhtgADSASVIFDAVQ-AAKA 329
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQyMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 330 RGIDVLIADTAGRlhtkDNLMEElkKVRRVIGKLDETAPHEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTAK 409
Cdd:PRK12726 284 NCVDHILIDTVGR----NYLAEE--SVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTR 357
|
170 180
....*....|....*....|....*.
gi 15595570 410 GGVIFALAKQFGLPIRYIGVGEGIDD 435
Cdd:PRK12726 358 IGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
251-455 |
3.91e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 64.36 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKK--LQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIfdavqaAK 328
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLAL------AE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 329 ARGIDVLIADTAGRLHTKDNLMEELKKVRrvigklDETAPHEVLLVLDAGTGQNAINQAKQFNLAV---------ELTGL 399
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQIAMLH------GADTPVQRLLLLNATSHGDTLNEVVQAYRSAagqpkaalpDLAGC 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15595570 400 ALTKLDGTAKGGVIFALAKQFGLPIRYIGVGEGIDDLRTFEADAFV--QALFAERENA 455
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFLlkSAFCAPREDS 344
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
243-448 |
1.39e-10 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 63.47 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 243 VDVAREPYVILVVGVNGVGKTTTIGKLAKKL--QLEGKKVMLAAGDTFRAAAVEQLQVWGernRIPVIAQHTgADSASVI 320
Cdd:PRK12727 344 VDPLERGGVIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYG---RQLGIAVHE-ADSAESL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 321 FDAVQaaKARGIDVLIADTAGRLHTKDNLMEELKKVRrvigkldetAPHEV--LLVLDAGTGQNAINQAKQFNLAVELTG 398
Cdd:PRK12727 420 LDLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNWLR---------AARQVtsLLVLPANAHFSDLDEVVRRFAHAKPQG 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15595570 399 LALTKLDGTAKGGVIFALAKQFGLPIRYIGVGEGI-DDLRTFEADAFVQAL 448
Cdd:PRK12727 489 VVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 539
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
251-450 |
9.20e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 60.97 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQL-EGK-KVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADsasvIFDAVQAAK 328
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCVArEGAdQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 329 ARGIdVLIaDTAGRLHTKDNLMEELKKVRRVigkldeTAPHEVLLVLDA---GTGQNAINQAKQFNLAVELTGLALTKLD 405
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLLNAashGDTLNEVVHAYRHGAGEDVDGCIITKLD 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15595570 406 GTAKGGVIFALAKQFGLPIRYIGVGEGI-DDLRTFEADAFVQALFA 450
Cdd:PRK14723 335 EATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAFA 380
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
247-433 |
7.53e-09 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 57.38 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 247 REPYVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHtgaDSASVIFDAVQA 326
Cdd:PRK11889 239 KEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTYF 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 327 AKARGIDVLIADTAGRLHTKDNLMEELkkvrrvIGKLDETAPHEVLLVLDAGT-GQNAINQAKQFNlAVELTGLALTKLD 405
Cdd:PRK11889 316 KEEARVDYILIDTAGKNYRASETVEEM------IETMGQVEPDYICLTLSASMkSKDMIEIITNFK-DIHIDGIVFTKFD 388
|
170 180
....*....|....*....|....*...
gi 15595570 406 GTAKGGVIFALAKQFGLPIRYIGVGEGI 433
Cdd:PRK11889 389 ETASSGELLKIPAVSSAPIVLMTDGQDV 416
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
247-433 |
7.83e-09 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 56.68 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 247 REPYVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHtgaDSASVIFDAVQA 326
Cdd:PRK06731 73 KEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTYF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 327 AKARGIDVLIADTAGRLHTKDNLMEELkkvrrvIGKLDETAPHEVLLVLDAG-TGQNAINQAKQFNlAVELTGLALTKLD 405
Cdd:PRK06731 150 KEEARVDYILIDTAGKNYRASETVEEM------IETMGQVEPDYICLTLSASmKSKDMIEIITNFK-DIHIDGIVFTKFD 222
|
170 180
....*....|....*....|....*...
gi 15595570 406 GTAKGGVIFALAKQFGLPIRYIGVGEGI 433
Cdd:PRK06731 223 ETASSGELLKIPAVSSAPIVLMTDGQDV 250
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
249-433 |
2.49e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 55.68 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 249 PYVILVVGVNGVGKTTTIGKLAKKLQLEGKK----VMLAAGDTFRAAAVEQLQVWGERNRIPVIAQHTGADSASVIFDav 324
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAIYGINSDDkslnIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 325 qaakARGIDVLIADTAGRlHTKDNLmeELKKVRRVIGKLDETAphEVLLVLDAGTGQNAINQA-KQFNlAVELTGLALTK 403
Cdd:PRK12723 252 ----SKDFDLVLVDTIGK-SPKDFM--KLAEMKELLNACGRDA--EFHLAVSSTTKTSDVKEIfHQFS-PFSYKTVIFTK 321
|
170 180 190
....*....|....*....|....*....|
gi 15595570 404 LDGTAKGGVIFALAKQFGLPIRYIGVGEGI 433
Cdd:PRK12723 322 LDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
190-234 |
1.45e-06 |
|
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: 45.62 E-value: 1.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15595570 190 LLTADVGVEATTLIVQNLTKRVAR---KELADSGALYKALQEELASLL 234
Cdd:smart00963 30 LLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
190-230 |
5.28e-06 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 43.99 E-value: 5.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15595570 190 LLTADVGVEATTLIVQNLTKR-VARKELADSGALYKALQEEL 230
Cdd:pfam02881 34 LLEADVGVEVVKKIIERLREKaVGEKKLKPPQEVKKILKEEL 75
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
251-455 |
2.95e-05 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 46.10 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLE--GKKVMLAAGDTFRAAAVEQLQVWGernRIPVIAQHTGADSASVifdAVQAAK 328
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARAVIRhgADKVALLTTDSYRIGGHEQLRIYG---KLLGVSVRSIKDIADL---QLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 329 ARGIDVLIADTAGrLHTKDNLMEElkKVRRVIGKLDETaphEVLLVLDAGTGQNAINQAKQFNLAVELTGLALTKLDGTA 408
Cdd:PRK14721 267 LRGKHMVLIDTVG-MSQRDQMLAE--QIAMLSQCGTQV---KHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15595570 409 KGGVIFALAKQFGLPIRYIGVGEGI-DDLRTFEADAFVQALFA-ERENA 455
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIFKpSRENS 389
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
249-337 |
8.15e-04 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 40.04 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 249 PYVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGDTFRaaaveqlqvwgernripVIAQHTGADSASVIFDAVQAAK 328
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELR-----------------EILGHYGYDKQSRIEMALKRAK 69
|
90
....*....|....*
gi 15595570 329 ------ARGIDVLIA 337
Cdd:PRK05541 70 lakflaDQGMIVIVT 84
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
252-309 |
1.42e-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: 39.94 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 252 ILVVGVNGVGKTTTIGKLAKKLQLEGKKVML--AAGDTFRAAAVEQLQVWGERNRIPVIA 309
Cdd:cd01672 3 IVFEGIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
249-343 |
1.64e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 39.62 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 249 PYVILVVGVNGVGKTTtigkLAKKLqleGKKVMLaagDTFRAAAVeqLQVWgernRIPVIAQHTGADSASVIFDAVQAAK 328
Cdd:pfam13479 2 KLKILIYGPSGIGKTT----FAKTL---PKPLFL---DTEKGSKA--LDGD----RFPDIVIRDSWQDFLDAIDELTAAE 65
|
90
....*....|....*
gi 15595570 329 ARGIDVLIADTAGRL 343
Cdd:pfam13479 66 LADYKTIVIDTVDWL 80
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
255-294 |
2.00e-03 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 38.37 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15595570 255 VGVNGVGKTTTIGKLAKKLQLEgkkvMLAAGDTFRAAAVE 294
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGFP----HISAGDLLREEAKE 36
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
251-360 |
2.52e-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: 40.35 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595570 251 VILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAA--GdtfRAAAVeqLQvwgERNRIPV--IAQHTGADSASVIFDAVQA 326
Cdd:COG0507 142 VSVLTGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKR--LS---ESTGIEArtIHRLLGLRPDSGRFRHNRD 213
|
90 100 110
....*....|....*....|....*....|....*..
gi 15595570 327 AKARGIDVLIADTAG--RLHTKDNLMEELKKVR-RVI 360
Cdd:COG0507 214 NPLTPADLLVVDEASmvDTRLMAALLEALPRAGaRLI 250
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
251-286 |
2.74e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 37.41 E-value: 2.74e-03
10 20 30
....*....|....*....|....*....|....*..
gi 15595570 251 VILVVG-VNGVGKTTTIGKLAKKLQLEGKKVMLAAGD 286
Cdd:cd01983 2 VIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
245-293 |
2.93e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 38.30 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15595570 245 VAREPyVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAgDTFRAAAV 293
Cdd:cd17933 9 VLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
396-435 |
6.33e-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: 38.63 E-value: 6.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15595570 396 LTGLALTKLDGTAKGGVIFaLAKQFGLPIRYIGVGEGIDD 435
Cdd:cd03108 275 LTELALTKLDVNAQKYIER-IEELLGVPITYISVGPDREQ 313
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
221-286 |
8.78e-03 |
|
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).
Pssm-ID: 275109 [Multi-domain] Cd Length: 566 Bit Score: 38.53 E-value: 8.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595570 221 ALYKALQEELASLLRPVEQPLQVDV-----------AREPYVILVVGVNGVGKTTTIGKLAKKLQLEGKKVMLAAGD 286
Cdd:TIGR04291 282 ALRQLLNDDQPQLSLDITTPQVPDLpslsrlideiaKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
|
|
| |
