|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
225-526 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 545.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 225 FFARLKRSLLKTKQNLGSGFMGLFSG-KKIDDDLFEELEEQLLIADVGVETTRKIITSLTEHASRKQLKDAEALYGKLKE 303
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 304 EMSEILSTVDKPLDVSGKNPFVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVA 383
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 384 QHTGADSASVIFDAIQAAKARGIDVLLADTAGRLQNKAHLMEELKKIVRVMKKLDGDAPHEVMLTLDASTGQNAVSQAKL 463
Cdd:COG0552 161 QKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAKV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914220865 464 FNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEALFARE 526
Cdd:COG0552 241 FNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
216-527 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 538.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 216 EQERPTKEGFFARLKRSLLKTKQNLGSGFMGLFSGKKIDDDLFEELEEQLLIADVGVETTRKIITSLTEHASRKQLKDAE 295
Cdd:PRK10416 7 KKKKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 296 ALYGKLKEEMSEILSTVDKPLDVSGKNPFVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGE 375
Cdd:PRK10416 87 ELKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 376 RNKIAVVAQHTGADSASVIFDAIQAAKARGIDVLLADTAGRLQNKAHLMEELKKIVRVMKKLDGDAPHEVMLTLDASTGQ 455
Cdd:PRK10416 167 RVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQ 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914220865 456 NAVSQAKLFNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEALFARED 527
Cdd:PRK10416 247 NALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
252-523 |
7.45e-139 |
|
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: 402.02 E-value: 7.45e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 252 KIDDDLFEELEEQLLIADVGVETTRKIITSLTEHASRKQLKDAEALYGKLKEEMSEILST-----VDKPLDVSGKNPFVI 326
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEdllknTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 327 LMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKARGI 406
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 407 DVLLADTAGRLQNKAHLMEELKKIVRVMKKLDGDAPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKGGV 486
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 914220865 487 IFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEALF 523
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
324-522 |
7.08e-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: 350.72 E-value: 7.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 324 FVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKA 403
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 404 RGIDVLLADTAGRLQNKAHLMEELKKIVRVMKKLDGDAPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAK 483
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 914220865 484 GGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEAL 522
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
323-523 |
1.46e-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: 316.66 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 323 PFVILMVGVNGVGKTTTIGKLARQFQAEG-KSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAA 401
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 402 KARGIDVLLADTAGRLQNKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGT 481
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 914220865 482 AKGGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEALF 523
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
324-522 |
2.27e-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: 305.62 E-value: 2.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 324 FVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKA 403
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 404 RGIDVLLADTAGRLQNKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAK 483
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 914220865 484 GGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEAL 522
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
324-522 |
5.03e-96 |
|
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: 289.66 E-value: 5.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 324 FVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKA 403
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 404 RGIDVLLADTAGRLQNKAHLMEELKKIVRVmkkldgDAPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAK 483
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 914220865 484 GGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEAL 522
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
268-524 |
1.13e-84 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 265.68 E-value: 1.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 268 ADVGVETTRKIITSLTEH---ASRKQLKDAEAL-YGKLKEEMSEILStVDKPLDV-----SGKNPFVILMVGVNGVGKTT 338
Cdd:PRK14974 77 SDVALEVAEEILESLKEKlvgKKVKRGEDVEEIvKNALKEALLEVLS-VGDLFDLieeikSKGKPVVIVFVGVNGTGKTT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 339 TIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKARGIDVLLADTAGRLQ 418
Cdd:PRK14974 156 TIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 419 NKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPI 498
Cdd:PRK14974 236 TDANLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPI 309
|
250 260
....*....|....*....|....*.
gi 914220865 499 RYIGVGEGIEDLRPFKADDFIEALFA 524
Cdd:PRK14974 310 LFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
268-516 |
7.20e-76 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 245.70 E-value: 7.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 268 ADVGVETTRKIITSLTEHAS----RKQLKDAEALYGKLKEEMSEILSTVDKPLDVSGKNPFVILMVGVNGVGKTTTIGKL 343
Cdd:COG0541 41 ADVNLKVVKDFIERVKERALgeevLKSLTPGQQVIKIVHDELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 344 ARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKARGIDVLLADTAGRLQNKAHL 423
Cdd:COG0541 121 AKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 424 MEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGV 503
Cdd:COG0541 201 MDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGT 274
|
250
....*....|...
gi 914220865 504 GEGIEDLRPFKAD 516
Cdd:COG0541 275 GEKLDDLEPFHPD 287
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
325-516 |
1.49e-65 |
|
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: 210.92 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKAR 404
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 405 GIDVLLADTAGRLQNKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKG 484
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|..
gi 914220865 485 GVIFAIADQFGIPIRYIGVGEGIEDLRPFKAD 516
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
303-519 |
1.07e-59 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 203.52 E-value: 1.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 303 EEMSEILSTvDKPLDVSGKNPFVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVV 382
Cdd:PRK00771 76 EELVKLLGE-ETEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 383 AQHTGADSASVIFDAIQAAKARgiDVLLADTAGRLQNKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAK 462
Cdd:PRK00771 155 GDPDNKDAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAK 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 914220865 463 LFNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFI 519
Cdd:PRK00771 227 AFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
324-522 |
1.77e-51 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 173.92 E-value: 1.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 324 FVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKA 403
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 404 RGIDVLLADTAGRLQNKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAK 483
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 914220865 484 GGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEAL 522
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
324-522 |
6.85e-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: 164.71 E-value: 6.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 324 FVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKA 403
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 404 RGIDVLLADTAGRLQNKAHLMEELKKIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAV----------GLTGI 473
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN------PDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 914220865 474 TLTKLDGTA-KGGVIFAIADQFGIPIRYIGVGEGIEDLRPFKADDFIEAL 522
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
276-527 |
3.22e-38 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 143.47 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 276 RKIITSLTEHASRKqlKDAEALYGKLKEEMSEILSTVDKPLDVSGKnpfVILMVGVNGVGKTTTIGKLARQF-QAEGKSV 354
Cdd:COG1419 122 PELARELLEKLPED--LSAEEAWRALLEALARRLPVAEDPLLDEGG---VIALVGPTGVGKTTTIAKLAARFvLRGKKKV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 355 MLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIfdaiqaAKARGIDVLLADTAGRLQNKAHLMEELKKIvrvm 434
Cdd:COG1419 197 ALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEELKAL---- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 435 kkLDGDAPHEVMLTLDAST-GQNAVSQAKLFNEaVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGI-EDLRP 512
Cdd:COG1419 267 --LDAGPPIEVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEV 343
|
250
....*....|....*
gi 914220865 513 FKADDFIEALFARED 527
Cdd:COG1419 344 ADPERLARLLLGGLE 358
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
272-527 |
8.42e-37 |
|
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: 141.13 E-value: 8.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 272 VETTRKIITSLTEHAS---RKQLKDAealygkLKEEMSEILSTVDKPLDVSGKNPFVILMVGVNGVGKTTTIGKLARQFQ 348
Cdd:TIGR01425 52 RNNIKKKINLEDIASGinkRKLIQDA------VFEELCNLVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 349 AEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDAIQAAKARGIDVLLADTAGRLQNKAHLMEELK 428
Cdd:TIGR01425 126 RRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 429 KIVRVMKkldgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIE 508
Cdd:TIGR01425 206 QVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVD 279
|
250
....*....|....*....
gi 914220865 509 DLRPFKADDFIEALFARED 527
Cdd:TIGR01425 280 EFEIFDAEPFVSKLLGMGD 298
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
325-522 |
5.12e-31 |
|
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).
Pssm-ID: 349782 [Multi-domain] Cd Length: 189 Bit Score: 118.81 E-value: 5.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKLARQFQAE-GKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAqhtgADSASVIFDAIqaAKA 403
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVLKkGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDPEDLADAL--ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 404 RGIDVLLADTAGRLQNKAHLMEELKKIvrvmkkLDGDAPHEVMLTLDAST-GQNAVSQAKLFnEAVGLTGITLTKLDGTA 482
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKEL------LGAGEDIEVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDETT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 914220865 483 KGGVIFAIADQFGIPIRYIGVGEGI-EDLRPFKADDFIEAL 522
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
273-527 |
7.11e-26 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 109.98 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 273 ETTRKIITSLTEHASRKQlkdaEALYGKLKEEMSEILSTVDKPLDVSGKnpfVILMVGVNGVGKTTTIGKLARQFQA--E 350
Cdd:PRK05703 178 EIAEKLLKLLLEHMPPRE----RTAWRYLLELLANMIPVRVEDILKQGG---VVALVGPTGVGKTTTLAKLAARYALlyG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 351 GKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSAsvifDAIQAAKARgiDVLLADTAGRLQNKAHLMEELKKI 430
Cdd:PRK05703 251 KKKVALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELA----KALEQLRDC--DVILIDTAGRSQRDKRLIEELKAL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 431 VRvmkklDGDAPHEVMLTLdASTGQNAVSQA--KLFNEaVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGI- 507
Cdd:PRK05703 325 IE-----FSGEPIDVYLVL-SATTKYEDLKDiyKHFSR-LPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVp 397
|
250 260
....*....|....*....|
gi 914220865 508 EDLRPFKADDFIEALFARED 527
Cdd:PRK05703 398 DDIKVANPEELVRLLLGGFN 417
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
277-415 |
1.57e-14 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 73.91 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 277 KIITSLTEHAsrKQLKDAEALYGKLKEEMSEILStVDKPLDVSGKNPFVILMVGVNGVGKTTTIGKLARQF--QAEGKSV 354
Cdd:TIGR03499 151 ELARELLEKL--PEDADAEDAWRWLREALEGMLP-VKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFalEHGKKKV 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914220865 355 MLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSAsvifDAIQAAKARgiDVLLADTAG 415
Cdd:TIGR03499 228 ALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKELR----EALDRLRDK--DLILIDTAG 282
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
309-509 |
4.92e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 71.56 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 309 LSTVDkPLDVSGknpfVILMVGVNGVGKTTTIGKLARQFQAE--GKSVMLAAGDTFRAAAVEQLQVWGERNKIAVvaqHT 386
Cdd:PRK12727 341 VAPVD-PLERGG----VIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 387 gADSASVIFDAIQaaKARGIDVLLADTAGRLQNKAHLMEELK--KIVRVMKKLdgdaphevmLTLDASTGQNAVSQAKLF 464
Cdd:PRK12727 413 -ADSAESLLDLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTSL---------LVLPANAHFSDLDEVVRR 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 914220865 465 NEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIED 509
Cdd:PRK12727 481 FAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPD 525
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
325-437 |
6.32e-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: 66.24 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVwgernkIAVVAQHTGADSASVIFDAIQAAKAR 404
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALARKL 77
|
90 100 110
....*....|....*....|....*....|...
gi 914220865 405 GIDVLLADTAGRLQNKAHLMEELKKIVRVMKKL 437
Cdd:smart00382 78 KPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
215-512 |
2.19e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 68.99 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 215 QEQERPTKEGFFARLKRSL---LKTKQNLGSGFMGLFSGKKIDDdlfeeleeqLLIADVgvettrkiitsltEHASRKQL 291
Cdd:PRK12726 115 QEEELSAMRLELAALNRELavkMREEREQNSDFVKFLKGRGISD---------TYVADF-------------MQAGRKQF 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 292 KDAEALY-GKLKEEMSEILS---TVDKPLDVSGKNpfVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAV 367
Cdd:PRK12726 173 KQVETAHlDDITDWFVPYLSgklAVEDSFDLSNHR--IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 368 EQLQVWGERNKIAVVAqhtgADSASVIFDAIQ-AAKARGIDVLLADTAGRlqnkAHLMEELKKIVRVMKkldgDAPHEVM 446
Cdd:PRK12726 251 EQFQGYADKLDVELIV----ATSPAELEEAVQyMTYVNCVDHILIDTVGR----NYLAEESVSEISAYT----DVVHPDL 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 447 LTLDASTGQNAVSQAKLFNE--AVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIED--LRP 512
Cdd:PRK12726 319 TCFTFSSGMKSADVMTILPKlaEIPIDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQNITEniFRP 388
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
326-508 |
6.51e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 67.40 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 326 ILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHtgaDSASVIFDAIQAAKARG 405
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTYFKEEAR 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 406 IDVLLADTAGRLQNKAHLMEELkkiVRVMKKLDgdaPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKGG 485
Cdd:PRK11889 321 VDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSG 394
|
170 180
....*....|....*....|...
gi 914220865 486 VIFAIADQFGIPIRYIGVGEGIE 508
Cdd:PRK11889 395 ELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
325-513 |
6.54e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 67.68 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKL-ARQFQAEGKSVMLAAGDTFRAAAVEQLQVWgernkiavvaqhtgADSASVIFDAIQAAK- 402
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLaAKYFLHMGKSVSLYTTDNYRIAAIEQLKRY--------------ADTMGMPFYPVKDIKk 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 403 -----AR-GIDVLLADTAGRLQNKAHLMEELKKIVRVMKKLDGDaphEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLT 476
Cdd:PRK12724 291 fketlARdGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSV---ENLLVLSSTSSYHHTLTVLKAYESLNYRRILLT 367
|
170 180 190
....*....|....*....|....*....|....*..
gi 914220865 477 KLDGTAKGGVIFAIADQFGIPIRYIGVGEGIedlrPF 513
Cdd:PRK12724 368 KLDEADFLGSFLELADTYSKSFTYLSVGQEV----PF 400
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
325-524 |
8.44e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 67.90 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKLARQFQA-EGKS-VMLAAGDTFRAAAVEQLQVWGernKIAVVAQHTGADSASVIFdAIQAAK 402
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCVArEGADqLALLTTDSFRIGALEQLRIYG---RILGVPVHAVKDAADLRF-ALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 403 ARGIdvLLADTAGRLQNKAHLMEELKKIVRVmkkldgDAPHEVMLTLdastgqNAVSQAKLFNEAV---------GLTGI 473
Cdd:PRK14723 263 DKHL--VLIDTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLL------NAASHGDTLNEVVhayrhgageDVDGC 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 914220865 474 TLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGI-EDLRPFKADDFIEALFA 524
Cdd:PRK14723 329 IITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAFA 380
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
285-508 |
4.03e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 63.61 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 285 HASRKQLK----DAEALYGKLKEEMSEILSTVDKPLDVSGKNPFVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGD 360
Cdd:PRK06731 33 HAYAEKLKvkfeNATMITEEVIEYILEDMSSHFNTENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 361 TFRAAAVEQLQVWGERNKIAVVAQHtgaDSASVIFDAIQAAKARGIDVLLADTAGRLQNKAHLMEELkkiVRVMKKLDgd 440
Cdd:PRK06731 113 HSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEM---IETMGQVE-- 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914220865 441 aPHEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGIE 508
Cdd:PRK06731 185 -PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
268-509 |
9.71e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 60.51 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 268 ADVGVETTRKIITSLTEHASRKQLKDAEALYGKLKEEMSEILSTVDKPLDVSGknpfVILMVGVNGVGKTTTIGKLARQ- 346
Cdd:PRK14722 86 AGFSAQLVRMIVDNLPEGEGYDTLDAAADWAQSVLAANLPVLDSEDALMERGG----VFALMGPTGVGKTTTTAKLAARc 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 347 -FQAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSAsvifdaIQAAKARGIDVLLADTAGRLQNKAHLME 425
Cdd:PRK14722 162 vMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQ------LALAELRNKHMVLIDTIGMSQRDRTVSD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 426 ELKKIvrvmkkLDGDAPHEVMLTLDASTGQNAVSQA-KLFNEAVG--------LTGITLTKLDGTAKGGVIFAIADQFGI 496
Cdd:PRK14722 236 QIAML------HGADTPVQRLLLLNATSHGDTLNEVvQAYRSAAGqpkaalpdLAGCILTKLDEASNLGGVLDTVIRYKL 309
|
250
....*....|...
gi 914220865 497 PIRYIGVGEGIED 509
Cdd:PRK14722 310 PVHYVSTGQKVPE 322
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
237-309 |
1.03e-07 |
|
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species.
Pssm-ID: 214941 [Multi-domain] Cd Length: 77 Bit Score: 49.09 E-value: 1.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914220865 237 KQNLGSGFMGLFSGKKIDDDLFEELEEQLLIADVGVETTRKIITSLTEHASR---KQLKDAEALYGKLKEEMSEIL 309
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
323-507 |
1.27e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 53.75 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 323 PFVILMVGVNGVGKTTTIGKLARQF----QAEGKSVMLAAGDTFRAAAVEQLQVWGERNKIAVVAQHTGADSASVIFDai 398
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 399 qaakARGIDVLLADTAGRLQNKAHLMEELKKIVRVMKKldgDAphEVMLTLDASTGQNAVSQAKLFNEAVGLTGITLTKL 478
Cdd:PRK12723 252 ----SKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGR---DA--EFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTKL 322
|
170 180
....*....|....*....|....*....
gi 914220865 479 DGTAKGGVIFAIADQFGIPIRYIGVGEGI 507
Cdd:PRK12723 323 DETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
325-510 |
8.41e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 51.49 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKL-ARQFQAEGKS-VMLAAGDTFRAAAVEQLQVWGernKIAVVAQHTGADSASVifdAIQAAK 402
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLaARAVIRHGADkVALLTTDSYRIGGHEQLRIYG---KLLGVSVRSIKDIADL---QLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 403 ARGIDVLLADTAGRLQNKAHLMEELkkivrVMKKLDGDAPHEVMLTldastgqNAVSQAKLFNEAV------GLTGITLT 476
Cdd:PRK14721 267 LRGKHMVLIDTVGMSQRDQMLAEQI-----AMLSQCGTQVKHLLLL-------NATSSGDTLDEVIsayqghGIHGCIIT 334
|
170 180 190
....*....|....*....|....*....|....*
gi 914220865 477 KLDGTAKGGVIFAIADQFGIPIRYIGVGEGI-EDL 510
Cdd:PRK14721 335 KVDEAASLGIALDAVIRRKLVLHYVTNGQKVpEDL 369
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
325-510 |
2.81e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 43.42 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 325 VILMVGVNGVGKTTTIGKLARQFqaegksVM--------LAAGDTFRAAAVEQLQVWGernKIAVVAQHTGADSASVifd 396
Cdd:PRK06995 258 VFALMGPTGVGKTTTTAKLAARC------VMrhgaskvaLLTTDSYRIGGHEQLRIYG---KILGVPVHAVKDAADL--- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 397 AIQAAKARGIDVLLADTAGRLQNKAHLMEElkkivrvMKKLDG-DAPHEVMLTLdastgqNAVSQAKLFNEAV------G 469
Cdd:PRK06995 326 RLALSELRNKHIVLIDTIGMSQRDRMVSEQ-------IAMLHGaGAPVKRLLLL------NATSHGDTLNEVVqayrgpG 392
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 914220865 470 LTGITLTKLDGTAKGGVIFAIADQFGIPIRYIGVGEGI-EDL 510
Cdd:PRK06995 393 LAGCILTKLDEAASLGGALDVVIRYKLPLHYVSNGQRVpEDL 434
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
240-305 |
2.96e-04 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 39.37 E-value: 2.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914220865 240 LGSGFMGLFSG----KKIDDDLFEELEEQLLI----ADVGVETTRKIITSLTEHA-SRKQLKDAEALYGKLKEEM 305
Cdd:pfam02881 1 LGEKLSSLFKGlrgkGKIDEEDLEEALKELEEalleADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
321-367 |
3.95e-04 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 41.00 E-value: 3.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 914220865 321 KNPFVILmVGVNGVGKTTTIGKLARQFQAEGKSVMLAAgDTFRAAAV 367
Cdd:cd17933 11 RNRVSVL-TGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
319-429 |
6.60e-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: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914220865 319 SGKNPFVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLaAGDTFRAAAVEQLQVWGERNKIAvvAQHTGADSASVIFDAI 398
Cdd:pfam06414 7 SQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELHPHYRELQAADPKTA--SEYTQPDASRWVEKLL 83
|
90 100 110
....*....|....*....|....*....|.
gi 914220865 399 QAAKARGIDVLLADTAGRLQNKAHLMEELKK 429
Cdd:pfam06414 84 QHAIENGYNIILEGTLRSPDVAKKIARALKA 114
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
469-509 |
1.55e-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: 1.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 914220865 469 GLTGITLTKLDGTAKGGVIFaIADQFGIPIRYIGVGEGIED 509
Cdd:cd03108 274 GLTELALTKLDVNAQKYIER-IEELLGVPITYISVGPDREQ 313
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
318-367 |
1.58e-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: 41.12 E-value: 1.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 914220865 318 VSGKNPFVILmVGVNGVGKTTTIGKLARQFQAEGKSVMLAA--GdtfRAAAV 367
Cdd:COG0507 136 ALTTRRVSVL-TGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKR 183
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
330-383 |
2.79e-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: 39.17 E-value: 2.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 914220865 330 GVNGVGKTTTIGKLARQFQAEGKSVML--AAGDTFRAAAVEQLQVWGERNKIAVVA 383
Cdd:cd01672 7 GIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
323-363 |
8.37e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 37.30 E-value: 8.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 914220865 323 PFVILMVGVNGVGKTTTIGKLARQFQAEGKSVMLAAGDTFR 363
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| |
