|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
196-497 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 539.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 196 FFARLKRSLLKTKENLGSGFISLFRG-KKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKE 274
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 275 EMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIA 354
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 355 QHTGADSASVIFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKL 434
Cdd:COG0552 161 QKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAKV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446963391 435 FHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFARE 497
Cdd:COG0552 241 FNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
187-498 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 535.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 187 EQEKPTKEGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAE 266
Cdd:PRK10416 7 KKKKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 267 ALYGLLKEEMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQ 346
Cdd:PRK10416 87 ELKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 347 RNNIPVIAQHTGADSASVIFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQ 426
Cdd:PRK10416 167 RVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQ 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446963391 427 NAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFARED 498
Cdd:PRK10416 247 NALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
223-494 |
1.73e-142 |
|
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: 410.11 E-value: 1.73e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 223 KIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAK-----VDEPLNVEGKTPFVI 297
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEdllknTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 298 LMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARNI 377
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 378 DVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGV 457
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446963391 458 IFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALF 494
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
295-493 |
5.92e-122 |
|
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: 354.95 E-value: 5.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 295 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 374
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 375 RNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 454
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 446963391 455 GGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEAL 493
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
294-494 |
1.16e-107 |
|
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: 318.20 E-value: 1.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 294 PFVILMVGVNGVGKTTTIGKLARQF-EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAA 372
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLkLKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 373 KARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGT 452
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446963391 453 AKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALF 494
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
295-493 |
2.90e-105 |
|
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: 312.17 E-value: 2.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 295 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 374
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 375 RNIDVLIADTAGRLQNKSHLMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 454
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446963391 455 GGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEAL 493
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
295-493 |
7.82e-99 |
|
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: 295.82 E-value: 7.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 295 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 374
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 375 RNIDVLIADTAGRLQNKSHLMEELKKIVRvmkkldVEAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 454
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKE------VESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446963391 455 GGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEAL 493
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
173-495 |
5.09e-84 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 262.99 E-value: 5.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 173 SPAEEDQPVEEIAQEQEKPTKEGFFARLKRSLLKTKENlgsgfislfrgkkidDDLFEELEEQLLIADVGVETTRKIITN 252
Cdd:PRK14974 26 EEAPEAEEEEEEEDEEEKKEKPGFFDKAKITEIKEKDI---------------EDLLEELELELLESDVALEVAEEILES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 253 LTE---GASRKQLRDAEAL-YGLLKEEMGEILAKV---DEPLNVEGKT-PFVILMVGVNGVGKTTTIGKLARQFEQQGKS 324
Cdd:PRK14974 91 LKEklvGKKVKRGEDVEEIvKNALKEALLEVLSVGdlfDLIEEIKSKGkPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 325 VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELKKIVRV 404
Cdd:PRK14974 171 VVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 405 MKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPF 484
Cdd:PRK14974 251 TK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPF 324
|
330
....*....|.
gi 446963391 485 KADDFIEALFA 495
Cdd:PRK14974 325 DPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
239-487 |
1.98e-79 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 253.79 E-value: 1.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 239 ADVGVETTRKIITNLTEGAS----RKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKL 314
Cdd:COG0541 41 ADVNLKVVKDFIERVKERALgeevLKSLTPGQQVIKIVHDELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 315 ARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARNIDVLIADTAGRLQNKSHL 394
Cdd:COG0541 121 AKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 395 MEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGV 474
Cdd:COG0541 201 MDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGT 274
|
250
....*....|...
gi 446963391 475 GERIEDLRPFKAD 487
Cdd:COG0541 275 GEKLDDLEPFHPD 287
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
296-487 |
3.82e-69 |
|
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: 219.39 E-value: 3.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 296 VILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKAR 375
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 376 NIDVLIADTAGRLQNKSHLMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKG 455
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|..
gi 446963391 456 GVIFSVADQFGIPIRYIGVGERIEDLRPFKAD 487
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
274-490 |
1.46e-61 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 207.75 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 274 EEMGEILAKvDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVI 353
Cdd:PRK00771 76 EELVKLLGE-ETEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 354 AQHTGADSASVIFDAIQAAKarNIDVLIADTAGRLQNKSHLMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAK 433
Cdd:PRK00771 155 GDPDNKDAVEIAKEGLEKFK--KADVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAK 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446963391 434 LFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFI 490
Cdd:PRK00771 227 AFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
295-493 |
9.62e-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: 182.01 E-value: 9.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 295 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 374
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 375 RNIDVLIADTAGRLQNKSHLMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 454
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446963391 455 GGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEAL 493
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
295-493 |
5.79e-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: 5.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 295 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 374
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 375 RNIDVLIADTAGRLQNKSHLMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAV----------GLTGI 444
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN------PDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446963391 445 TLTKLDgTA--KGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEAL 493
Cdd:cd17876 155 VLTKFD-TIddKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
239-498 |
2.60e-40 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 150.37 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 239 ADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPlNVEGKTP-----FVILMVGVNGVGKTTTIGK 313
Cdd:TIGR01425 41 SDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELCNLVDP-GVEAFTPkkgktCVIMFVGLQGAGKTTTCTK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 314 LARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARNIDVLIADTAGRLQNKSH 393
Cdd:TIGR01425 120 LAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 394 LMEELKKIVRVMKkldveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIG 473
Cdd:TIGR01425 200 LFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIG 273
|
250 260
....*....|....*....|....*
gi 446963391 474 VGERIEDLRPFKADDFIEALFARED 498
Cdd:TIGR01425 274 TGEHVDEFEIFDAEPFVSKLLGMGD 298
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
239-498 |
4.79e-40 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 148.09 E-value: 4.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 239 ADVGVETTRKIITNLTEGAsrkqlrDAEALYGLLKEEMGEILAKVDEPLNVEGKtpfVILMVGVNGVGKTTTIGKLARQF 318
Cdd:COG1419 118 AGVSPELARELLEKLPEDL------SAEEAWRALLEALARRLPVAEDPLLDEGG---VIALVGPTGVGKTTTIAKLAARF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 319 -EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIfdaiqaAKARNIDVLIADTAGRLQNKSHLMEE 397
Cdd:COG1419 189 vLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 398 LKKIvrvmkkLDVEAPHEVMLTIDAST-GQNAVSQAKLFhEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGE 476
Cdd:COG1419 263 LKAL------LDAGPPIEVYLVLSATTkYEDLKEIVEAF-SSLGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQ 335
|
250 260
....*....|....*....|...
gi 446963391 477 RI-EDLRPFKADDFIEALFARED 498
Cdd:COG1419 336 RVpEDIEVADPERLARLLLGGLE 358
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
296-493 |
1.80e-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: 122.27 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 296 VILMVGVNGVGKTTTIGKLARQFE-QQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAqhtgADSASVIFDAIqaAKA 374
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDPEDLADAL--ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 375 RNIDVLIADTAGRLQNKSHLMEELKKIvrvmkkLDVEAPHEVMLTIDAST-GQNAVSQAKLFhEAVGLTGITLTKLDGTA 453
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKEL------LGAGEDIEVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDETT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446963391 454 KGGVIFSVADQFGIPIRYIGVGERI-EDLRPFKADDFIEAL 493
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
244-498 |
2.38e-26 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 110.75 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 244 ETTRKIITNLTEGASRKQLRDAEALYGLLKEEmgeILAKVDEPLNVEGktpfVILMVGVNGVGKTTTIGKLARQF--EQQ 321
Cdd:PRK05703 178 EIAEKLLKLLLEHMPPRERTAWRYLLELLANM---IPVRVEDILKQGG----VVALVGPTGVGKTTTLAKLAARYalLYG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 322 GKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSAsvifDAIQAAKARNIdVLIaDTAGRLQNKSHLMEELKKI 401
Cdd:PRK05703 251 KKKVALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELA----KALEQLRDCDV-ILI-DTAGRSQRDKRLIEELKAL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 402 VRvmkklDVEAPHEVMLTIdASTGQNAVSQAKLFH-EAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERI-E 479
Cdd:PRK05703 325 IE-----FSGEPIDVYLVL-SATTKYEDLKDIYKHfSRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpD 398
|
250
....*....|....*....
gi 446963391 480 DLRPFKADDFIEALFARED 498
Cdd:PRK05703 399 DIKVANPEELVRLLLGGFN 417
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
296-495 |
2.42e-14 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 75.61 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 296 VILMVGVNGVGKTTTIGKLA-RQFEQQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADsasvIFDAIQAAK 373
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAaRCVAREGADqLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 374 ARNIdVLIaDTAGRLQNKSHLMEELKKIVrvmkklDVEAPHEVMLTID-ASTGQ--NAVSQAKLFHEAVGLTGITLTKLD 450
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLC------GVGRPVRRLLLLNaASHGDtlNEVVHAYRHGAGEDVDGCIITKLD 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446963391 451 GTAKGGVIFSVADQFGIPIRYIGVGERI-EDLRPFKADDFIEALFA 495
Cdd:PRK14723 335 EATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAFA 380
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
293-419 |
3.10e-14 |
|
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: 70.09 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 293 TPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQvwgqrnNIPVIAQHTGADSASVIFDAIQAA 372
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446963391 373 KARNIDVLIADTAGRLQNKSHLMEELKKIV-RVMKKLDVEAPHEVMLT 419
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEElRLLLLLKSEKNLTVILT 122
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
270-480 |
2.20e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 72.33 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 270 GLLKEEMGeiLAKVDePLNVEGktpfVILMVGVNGVGKTTTIGKLARQFEQQ--GKSVMLAAGDTFRAAAVEQLQVWGQR 347
Cdd:PRK12727 333 GLLSKRLP--VAPVD-PLERGG----VIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQ 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 348 NNIPViaqHTgADSASVIFDAIQaaKARNIDVLIADTAGRLQNKSHLMEELK--KIVRVMKKLdveaphevmLTIDASTG 425
Cdd:PRK12727 406 LGIAV---HE-ADSAESLLDLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTSL---------LVLPANAH 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446963391 426 QNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIED 480
Cdd:PRK12727 471 FSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPD 525
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
260-386 |
2.29e-13 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 70.44 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 260 KQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKtPFVILMVGVNGVGKTTTIGKLARQF--EQQGKSVMLAAGDTFRAAA 337
Cdd:TIGR03499 161 PEDADAEDAWRWLREALEGMLPVKPEEDPILEQ-GGVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446963391 338 VEQLQVWGQRNNIPVIAQHTGADsasvifdaIQAAKARNID---VLIaDTAG 386
Cdd:TIGR03499 240 VEQLKTYAEILGIPVKVARDPKE--------LREALDRLRDkdlILI-DTAG 282
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
182-483 |
7.68e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 70.15 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 182 EEIAQEQEKPTKEGFFARLKRSL---LKTKENLGSGFISLFRGKKIDDdlfeeleeqLLIADVgvettrkiitnltEGAS 258
Cdd:PRK12726 111 ERKTQEEELSAMRLELAALNRELavkMREEREQNSDFVKFLKGRGISD---------TYVADF-------------MQAG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 259 RKQLRDAEALYglLKEEMGEILAKVDEPLNVEGKTPF----VILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFR 334
Cdd:PRK12726 169 RKQFKQVETAH--LDDITDWFVPYLSGKLAVEDSFDLsnhrIISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 335 AAAVEQLQVWGQRNNIPVIAqhtgADSASVIFDAIQAAKARN-IDVLIADTAGRlqnkSHLMEElkKIVRVMKKLDVEAP 413
Cdd:PRK12726 247 SGAVEQFQGYADKLDVELIV----ATSPAELEEAVQYMTYVNcVDHILIDTVGR----NYLAEE--SVSEISAYTDVVHP 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446963391 414 HEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIED--LRP 483
Cdd:PRK12726 317 DLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQNITEniFRP 388
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
239-480 |
6.62e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 67.05 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 239 ADVGVETTRKIITNLTEGASRKQLrDAEALYG--LLKEEMgEILAKVDEPLNVEGktpfVILMVGVNGVGKTTTIGKLA- 315
Cdd:PRK14722 86 AGFSAQLVRMIVDNLPEGEGYDTL-DAAADWAqsVLAANL-PVLDSEDALMERGG----VFALMGPTGVGKTTTTAKLAa 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 316 RQFEQQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSAsvifdaIQAAKARNIDVLIADTAGRLQNKSHL 394
Cdd:PRK14722 160 RCVMRFGASkVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQ------LALAELRNKHMVLIDTIGMSQRDRTV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 395 MEELKKIvrvmkkLDVEAPHEVMLTIDASTGQNAVSQA-KLFHEAVG--------LTGITLTKLDGTAKGGVIFSVADQF 465
Cdd:PRK14722 234 SDQIAML------HGADTPVQRLLLLNATSHGDTLNEVvQAYRSAAGqpkaalpdLAGCILTKLDEASNLGGVLDTVIRY 307
|
250
....*....|....*
gi 446963391 466 GIPIRYIGVGERIED 480
Cdd:PRK14722 308 KLPVHYVSTGQKVPE 322
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
296-478 |
9.64e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 66.91 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 296 VILMVGVNGVGKTTTIGKLA-RQFEQQGKSVMLAAGDTFRAAAVEQLQVWgqrnnipviaqhtgADSASVIFDAIQAAK- 373
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRY--------------ADTMGMPFYPVKDIKk 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 374 -----ARNIDVLI-ADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAklfHEAVGLTGITLT 447
Cdd:PRK12724 291 fketlARDGSELIlIDTAGYSHRNLEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKA---YESLNYRRILLT 367
|
170 180 190
....*....|....*....|....*....|.
gi 446963391 448 KLDGTAKGGVIFSVADQFGIPIRYIGVGERI 478
Cdd:PRK12724 368 KLDEADFLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
273-479 |
2.09e-11 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 65.86 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 273 KEEMGEILAKVDEPLNVEG---KTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNN 349
Cdd:PRK11889 217 EEVIEYILEDMRSHFNTENvfeKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 350 IPVIAQHtgaDSASVIFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELkkiVRVMKKLDveaPHEVMLTIDASTGQNAV 429
Cdd:PRK11889 297 FEVIAVR---DEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASMKSKDM 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446963391 430 SQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIE 479
Cdd:PRK11889 368 IEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
288-479 |
9.06e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 62.46 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 288 NVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHtgaDSASVIFD 367
Cdd:PRK06731 69 NVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 368 AIQAAKARNIDVLIADTAGRLQNKSHLMEELkkiVRVMKKLDveaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLT 447
Cdd:PRK06731 146 LTYFKEEARVDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFT 219
|
170 180 190
....*....|....*....|....*....|..
gi 446963391 448 KLDGTAKGGVIFSVADQFGIPIRYIGVGERIE 479
Cdd:PRK06731 220 KFDETASSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
294-476 |
3.89e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 58.37 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 294 PFVILMVGVNGVGKTTTIGKLARQF----EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDai 369
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 370 qaakARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKldveaPHEVMLTIDASTGQNAVSQakLFH--EAVGLTGITLT 447
Cdd:PRK12723 252 ----SKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGR-----DAEFHLAVSSTTKTSDVKE--IFHqfSPFSYKTVIFT 320
|
170 180
....*....|....*....|....*....
gi 446963391 448 KLDGTAKGGVIFSVADQFGIPIRYIGVGE 476
Cdd:PRK12723 321 KLDETTCVGNLISLIYEMRKEVSYVTDGQ 349
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
17-192 |
1.98e-07 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 53.89 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 17 QKEQTPEKETEVQNEQPVVEEI-----VQAQEPVKASEHAVEEQPQAHTEAKAETFAADVVEVTEQVAESEKAQPEAEVV 91
Cdd:PRK10811 852 DVQVEEQREAEEVQVQPVVAEVpvaaaVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVI 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 92 AQP-EPVVEETPEPVAIEREELPLSEDVNAEAVSPEEWQAEAETVEIVEAAEEEAAKEEITDEEPEAQALAAEVAEEAVM 170
Cdd:PRK10811 932 TESdVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATV 1011
|
170 180 190
....*....|....*....|....*....|.
gi 446963391 171 VVS---------PAEEDQPVEEIAQEQEKPT 192
Cdd:PRK10811 1012 EHNhatapmtraPAPEYVPEAPRHSDWQRPT 1042
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
208-280 |
4.74e-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: 47.16 E-value: 4.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446963391 208 KENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTE---GASRKQLRDAEALYGLLKEEMGEIL 280
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEkakGEVLKGLTPKQEVKKILKEELVKIL 77
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
296-481 |
2.32e-06 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 49.95 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 296 VILMVGVNGVGKTTTIGKL-ARQFEQQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPViaqHTGADSASVIFdAIQAAK 373
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLaARAVIRHGADkVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADLQL-MLHELR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 374 ARNIdVLIaDTAGRLQNKSHLMEElkkiVRVMKKLDVEAPHEVMLTIdASTGQ--NAVSQAKLFHeavGLTGITLTKLDG 451
Cdd:PRK14721 269 GKHM-VLI-DTVGMSQRDQMLAEQ----IAMLSQCGTQVKHLLLLNA-TSSGDtlDEVISAYQGH---GIHGCIITKVDE 338
|
170 180 190
....*....|....*....|....*....|.
gi 446963391 452 TAKGGVIFSVADQFGIPIRYIGVGERI-EDL 481
Cdd:PRK14721 339 AASLGIALDAVIRRKLVLHYVTNGQKVpEDL 369
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
28-185 |
5.54e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.27 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 28 VQNEQPVVEEIVQAQEPVKASE-HAVEEQPQAHTEAKAETFAADVVEVTEQVAESEKAQPEAEVVAQPEPVVEETP---E 103
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVvAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPvteQ 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 104 PVAIEREELPLSEDVNAEAVSPEEWQAEAETVEIVEAAEEEAAKEEITDEEPEAQALAAEVAEEAVMVVSPAEEDQPVEE 183
Cdd:PRK10811 928 PQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVP 1007
|
..
gi 446963391 184 IA 185
Cdd:PRK10811 1008 EA 1009
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
33-194 |
4.11e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.19 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 33 PVVEeiVQAQEPVKASEhAVEEQPQAHTEAKAETFAADVVEVTEQVAESEKAQPEAEVVAQPEPVVEETPEPVAIEREEL 112
Cdd:PRK10811 846 PVVR--PQDVQVEEQRE-AEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAA 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 113 PLSEdvNAEAVSPEEWQAEAETVEIVEAAEEEAAKEEITDEEPEAQALAAEVAEEAVMVVSPAEEDQPVEEIAQEQEKPT 192
Cdd:PRK10811 923 PVTE--QPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPE 1000
|
..
gi 446963391 193 KE 194
Cdd:PRK10811 1001 VA 1002
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
209-276 |
1.63e-04 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 40.14 E-value: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446963391 209 ENLGSGFISLFRGKKIDDDLFEELEEQLLI----ADVGVETTRKIITNLTEGA-SRKQLRDAEALYGLLKEEM 276
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEALKELEEalleADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
296-481 |
2.68e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 43.42 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 296 VILMVGVNGVGKTTTIGKLARQFE-QQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASvifdAIQAAK 373
Cdd:PRK06995 258 VFALMGPTGVGKTTTTAKLAARCVmRHGASkVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADLRL----ALSELR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 374 ARNIdVLIaDTAG---RLQNKSHLMEELKKIVRVMKKLdveaphevmLTIDA-STGQ--NAVSQAklfHEAVGLTGITLT 447
Cdd:PRK06995 334 NKHI-VLI-DTIGmsqRDRMVSEQIAMLHGAGAPVKRL---------LLLNAtSHGDtlNEVVQA---YRGPGLAGCILT 399
|
170 180 190
....*....|....*....|....*....|....*
gi 446963391 448 KLDGTAKGGVIFSVADQFGIPIRYIGVGERI-EDL 481
Cdd:PRK06995 400 KLDEAASLGGALDVVIRYKLPLHYVSNGQRVpEDL 434
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
289-383 |
4.41e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 42.66 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 289 VEGKTPFVILmVGVNGVGKTTTIGKLARQFEQQGKSVMLAA--GdtfRAAAV--EQLQVWGQrnnipVIAQHTGADSASV 364
Cdd:COG0507 136 ALTTRRVSVL-TGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKRlsESTGIEAR-----TIHRLLGLRPDSG 206
|
90
....*....|....*....
gi 446963391 365 IFDAIQAAKARNIDVLIAD 383
Cdd:COG0507 207 RFRHNRDNPLTPADLLVVD 225
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
296-338 |
1.34e-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: 39.46 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446963391 296 VILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAgDTFRAAAV 338
Cdd:cd17933 14 VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
294-334 |
1.69e-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: 39.22 E-value: 1.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446963391 294 PFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFR 334
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
288-400 |
3.00e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.88 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 288 NVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLaAGDTFRAA---AVEQLQVWGQRNnipviAQHTGADSASV 364
Cdd:pfam06414 5 TTSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELhphYRELQAADPKTA-----SEYTQPDASRW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 446963391 365 IFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELKK 400
Cdd:pfam06414 79 VEKLLQHAIENGYNIILEGTLRSPDVAKKIARALKA 114
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
297-331 |
3.51e-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: 37.03 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446963391 297 ILMV--GVNGVGKTTTIGKLARQFEQQGKSVMLAAGD 331
Cdd:cd01983 2 VIAVtgGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
19-133 |
4.15e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 39.85 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 19 EQTPEKETEVQNEQPVVEEIVQAQEPVKASEHAVEEQPQAHTEAKAETfAADVVEVTEQVAESEKAQPEAE--------- 89
Cdd:PRK07994 404 ASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRARP-VNSALERLASVRPAPSALEKAPakkeayrwk 482
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446963391 90 ----VVAQPEPVVEETPEPVAIEREELP-LSEDVNAEAVSPEEWQAEAE 133
Cdd:PRK07994 483 atnpVEVKKEPVATPKALKKALEHEKTPeLAAKLAAEAIERDPWAALVS 531
|
|
| DUF3664 |
pfam12406 |
Surface protein; This family of proteins is found in eukaryotes. Proteins in this family are ... |
30-99 |
4.75e-03 |
|
Surface protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 131 and 312 amino acids in length.
Pssm-ID: 289191 [Multi-domain] Cd Length: 99 Bit Score: 36.78 E-value: 4.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446963391 30 NEQPVVEEIVQAQEPVKASEHAVEEQPQAHTEAKAETFAADVVEVTEQVAESEKAQPEAEvvAQPEPVVE 99
Cdd:pfam12406 30 SEQPAQQEPIEPQQPTQPSTEPEELQPETVTVEVPEPVTSEEPKESDQTEEQKHEEPEAS--PAPEPVDE 97
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
440-475 |
5.22e-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: 39.02 E-value: 5.22e-03
10 20 30
....*....|....*....|....*....|....*.
gi 446963391 440 GLTGITLTKLDGTAKGGVIFsVADQFGIPIRYIGVG 475
Cdd:cd03108 274 GLTELALTKLDVNAQKYIER-IEELLGVPITYISVG 308
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
301-354 |
7.55e-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: 37.63 E-value: 7.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446963391 301 GVNGVGKTTTIGKLARQFEQQGKSVML--AAGDTFRAAAVEQLQVWGQRNNIPVIA 354
Cdd:cd01672 7 GIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| |
