|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
215-516 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 539.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 215 FFARLKRSLLKTKENLGSGFISLFRG-KKIDDDLFEELEEQLLIADVGVDTTRKIIANLTEGASRKQLRDAEALYGLLKE 293
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 294 EMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIA 373
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 374 QHTGADSASVIFDAIQAAKARGVDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDENAPHEVMLTIDASTGQNAVSQAKL 453
Cdd:COG0552 161 QKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAKV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333956848 454 FHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEALFARE 516
Cdd:COG0552 241 FNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
206-517 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 538.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 206 EQEKPTKEGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVDTTRKIIANLTEGASRKQLRDAE 285
Cdd:PRK10416 7 KKKKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 286 ALYGLLKEEMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQ 365
Cdd:PRK10416 87 ELKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 366 RNNIPVIAQHTGADSASVIFDAIQAAKARGVDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDENAPHEVMLTIDASTGQ 445
Cdd:PRK10416 167 RVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQ 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333956848 446 NAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEALFARED 517
Cdd:PRK10416 247 NALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
242-513 |
6.66e-140 |
|
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: 404.33 E-value: 6.66e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 242 KIDDDLFEELEEQLLIADVGVDTTRKIIANLTEGASRKQLRDAEALYGLLKEEMGEILAK-----VDEPLNVEGKTPFVI 316
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEdllknTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 317 LMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARGV 396
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 397 DVLIADTAGRLQNKSHLMEELKKIVRVMKKLDENAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGV 476
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 333956848 477 IFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEALF 513
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
314-512 |
1.75e-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: 351.87 E-value: 1.75e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 314 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 393
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDENAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 473
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 333956848 474 GGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEAL 512
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
313-513 |
2.95e-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: 315.50 E-value: 2.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 313 PFVILMVGVNGVGKTTTIGKLARQF-EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAA 391
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLkLKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 392 KARGVDVLIADTAGRLQNKSHLMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGT 471
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 333956848 472 AKGGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEALF 513
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
314-512 |
2.94e-103 |
|
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: 307.55 E-value: 2.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 314 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 393
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRLQNKSHLMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 473
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 333956848 474 GGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEAL 512
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
314-512 |
5.78e-97 |
|
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: 291.58 E-value: 5.78e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 314 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 393
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRLQNKSHLMEELKKIVRVmkkldeNAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 473
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 333956848 474 GGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEAL 512
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
258-514 |
2.68e-83 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 261.83 E-value: 2.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 258 ADVGVDTTRKIIANLTE---GASRKQLRDAEAL-YGLLKEEMGEILAKV---DEPLNVEGKT-PFVILMVGVNGVGKTTT 329
Cdd:PRK14974 77 SDVALEVAEEILESLKEklvGKKVKRGEDVEEIvKNALKEALLEVLSVGdlfDLIEEIKSKGkPVVIVFVGVNGTGKTTT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 330 IGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARGVDVLIADTAGRLQN 409
Cdd:PRK14974 157 IAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 410 KSHLMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIR 489
Cdd:PRK14974 237 DANLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPIL 310
|
250 260
....*....|....*....|....*
gi 333956848 490 YIGVGERIEDLRPFNAGDFIEALFA 514
Cdd:PRK14974 311 FLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
258-504 |
9.40e-81 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 258.03 E-value: 9.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 258 ADVGVDTTRKIIANLTEGAS----RKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIGKL 333
Cdd:COG0541 41 ADVNLKVVKDFIERVKERALgeevLKSLTPGQQVIKIVHDELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 334 ARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARGVDVLIADTAGRLQNKSHL 413
Cdd:COG0541 121 AKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 414 MEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGV 493
Cdd:COG0541 201 MDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGT 274
|
250
....*....|.
gi 333956848 494 GERIEDLRPFN 504
Cdd:COG0541 275 GEKLDDLEPFH 285
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
315-503 |
3.44e-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: 220.16 E-value: 3.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKAR 394
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 395 GVDVLIADTAGRLQNKSHLMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKG 474
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180
....*....|....*....|....*....
gi 333956848 475 GVIFSVADQFGIPIRYIGVGERIEDLRPF 503
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPF 184
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
293-509 |
1.75e-61 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 207.75 E-value: 1.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 293 EEMGEILAKvDEPLNVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVI 372
Cdd:PRK00771 76 EELVKLLGE-ETEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 373 AQHTGADSASVIFDAIQAAKARgvDVLIADTAGRLQNKSHLMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAK 452
Cdd:PRK00771 155 GDPDNKDAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAK 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 333956848 453 LFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFI 509
Cdd:PRK00771 227 AFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
314-512 |
2.23e-54 |
|
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: 181.24 E-value: 2.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 314 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 393
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRLQNKSHLMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 473
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 333956848 474 GGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEAL 512
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
314-512 |
2.15e-50 |
|
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: 171.26 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 314 FVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKA 393
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRLQNKSHLMEELKKIVrvmkklDENAPHEVMLTIDASTGQNAVSQAKLFHEAV----------GLTGI 463
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLI------KENNPDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 333956848 464 TLTKLDgTA--KGGVIFSVADQFGIPIRYIGVGERIEDLRPFNAGDFIEAL 512
Cdd:cd17876 155 VLTKFD-TIddKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
258-517 |
8.42e-40 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 147.70 E-value: 8.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 258 ADVGVDTTRKIIANLTEGAsrkqlrDAEALYGLLKEEMGEILAKVDEPLNVEGKtpfVILMVGVNGVGKTTTIGKLARQF 337
Cdd:COG1419 118 AGVSPELARELLEKLPEDL------SAEEAWRALLEALARRLPVAEDPLLDEGG---VIALVGPTGVGKTTTIAKLAARF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 338 -EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIfdaiqaAKARGVDVLIADTAGRLQNKSHLMEE 416
Cdd:COG1419 189 vLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 417 LKKIVRVMKkldenaPHEVMLTIDAST-GQNAVSQAKLFhEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGE 495
Cdd:COG1419 263 LKALLDAGP------PIEVYLVLSATTkYEDLKEIVEAF-SSLGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQ 335
|
250 260
....*....|....*....|...
gi 333956848 496 RI-EDLRPFNAGDFIEALFARED 517
Cdd:COG1419 336 RVpEDIEVADPERLARLLLGGLE 358
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
258-517 |
3.51e-38 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 144.98 E-value: 3.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 258 ADVGVDTTRKIIANLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPlNVEGKTP-----FVILMVGVNGVGKTTTIGK 332
Cdd:TIGR01425 41 SDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELCNLVDP-GVEAFTPkkgktCVIMFVGLQGAGKTTTCTK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 333 LARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARGVDVLIADTAGRLQNKSH 412
Cdd:TIGR01425 120 LAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 413 LMEELKKIVRVMKkldenaPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIG 492
Cdd:TIGR01425 200 LFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIG 273
|
250 260
....*....|....*....|....*
gi 333956848 493 VGERIEDLRPFNAGDFIEALFARED 517
Cdd:TIGR01425 274 TGEHVDEFEIFDAEPFVSKLLGMGD 298
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
315-512 |
2.19e-33 |
|
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: 125.35 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKLARQFE-QQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAqhtgADSASVIFDAIqaAKA 393
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDPEDLADAL--ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRLQNKSHLMEELKKIvrvmkkLDENAPHEVMLTIDAST-GQNAVSQAKLFhEAVGLTGITLTKLDGTA 472
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKEL------LGAGEDIEVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDETT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 333956848 473 KGGVIFSVADQFGIPIRYIGVGERI-EDLRPFNAGDFIEAL 512
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
266-501 |
7.56e-27 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 112.68 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 266 RKIIANLTEGASRKQLRDAEALYGLLKEEmgeILAKVDEPLNVEGktpfVILMVGVNGVGKTTTIGKLARQF--EQQGKS 343
Cdd:PRK05703 181 EKLLKLLLEHMPPRERTAWRYLLELLANM---IPVRVEDILKQGG----VVALVGPTGVGKTTTLAKLAARYalLYGKKK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 344 VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSAsvifDAIQAAKARGVdVLIaDTAGRLQNKSHLMEELKKIVRv 423
Cdd:PRK05703 254 VALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELA----KALEQLRDCDV-ILI-DTAGRSQRDKRLIEELKALIE- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 424 mkklDENAPHEVMLTIdASTGQNAVSQAKLFH-EAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERI-EDLR 501
Cdd:PRK05703 327 ----FSGEPIDVYLVL-SATTKYEDLKDIYKHfSRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIK 401
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
150-405 |
4.06e-14 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 72.75 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 150 AAVEEKAVePAVETPHDAHEIAEDAPISEEELVALAADPEAALETEPEEEETAPVAEQEKPTKEGFFARLKRSLlktkEN 229
Cdd:TIGR03499 48 AAIDEEEA-AAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEALRELL----ER 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 230 LGSGFislfrGKKIDDDLFEELEEQLLIADVGVDTTRKIIANLtegasrKQLRDAEALYGLLKEEMGEILAKVDEPLNVE 309
Cdd:TIGR03499 123 LLAGL-----AWLQRPPERAKLYERLLEAGVSEELARELLEKL------PEDADAEDAWRWLREALEGMLPVKPEEDPIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 310 GKtPFVILMVGVNGVGKTTTIGKLARQF--EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIfda 387
Cdd:TIGR03499 192 EQ-GGVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKELREAL--- 267
|
250
....*....|....*...
gi 333956848 388 iqaAKARGVDVLIADTAG 405
Cdd:TIGR03499 268 ---DRLRDKDLILIDTAG 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
312-427 |
1.10e-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: 68.55 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 312 TPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQvwgqrnNIPVIAQHTGADSASVIFDAIQAA 391
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALALA 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 333956848 392 KARGVDVLIADTAGRLQNKSHLMEELKKIVRVMKKL 427
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
299-509 |
4.55e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 71.56 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 299 LAKVDePLNVEGktpfVILMVGVNGVGKTTTIGKLARQFEQQ--GKSVMLAAGDTFRAAAVEQLQVWGQRNNIPViaqHT 376
Cdd:PRK12727 341 VAPVD-PLERGG----VIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 377 gADSASVIFDAIQaaKARGVDVLIADTAGRLQNKSHLMEELK--KIVRVMKKLdenaphevmLTIDASTGQNAVSQAKLF 454
Cdd:PRK12727 413 -ADSAESLLDLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTSL---------LVLPANAHFSDLDEVVRR 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 333956848 455 HEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERI-EDLRPFNAGDFI 509
Cdd:PRK12727 481 FAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLV 536
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
315-504 |
5.68e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 70.76 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKLA-RQFEQQGKSVMLAAGDTFRAAAVEQLQVWgqrnnipviaqhtgADSASVIFDAIQAAK- 392
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRY--------------ADTMGMPFYPVKDIKk 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 393 -----AR-GVDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDENAPHEVMLTIDASTGQNAVSQAklfHEAVGLTGITLT 466
Cdd:PRK12724 291 fketlARdGSELILIDTAGYSHRNLEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKA---YESLNYRRILLT 367
|
170 180 190
....*....|....*....|....*....|....*...
gi 333956848 467 KLDGTAKGGVIFSVADQFGIPIRYIGVGERIedlrPFN 504
Cdd:PRK12724 368 KLDEADFLGSFLELADTYSKSFTYLSVGQEV----PFD 401
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
315-514 |
2.46e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 69.44 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKLA-RQFEQQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADsasvIFDAIQAAK 392
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAaRCVAREGADqLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 393 ARGVdVLIaDTAGRLQNKSHLMEELKKIVRVMKKLdenapHEVMLTIDASTGQ--NAVSQAKLFHEAVGLTGITLTKLDG 470
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGVGRPV-----RRLLLLNAASHGDtlNEVVHAYRHGAGEDVDGCIITKLDE 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 333956848 471 TAKGGVIFSVADQFGIPIRYIGVGERI-EDLRPFNAGDFIEALFA 514
Cdd:PRK14723 336 ATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAFA 380
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
315-502 |
8.18e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 67.07 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAqhtgADSASVIFDAIQ-AAKA 393
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQyMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 394 RGVDVLIADTAGRlqnkSHLMEElkKIVRVMKKLDENAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAK 473
Cdd:PRK12726 284 NCVDHILIDTVGR----NYLAEE--SVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTR 357
|
170 180 190
....*....|....*....|....*....|.
gi 333956848 474 GGVIFSVADQFGIPIRYIGVGERIED--LRP 502
Cdd:PRK12726 358 IGDLYTVMQETNLPVLYMTDGQNITEniFRP 388
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
292-498 |
9.61e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 67.01 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 292 KEEMGEILAKVDEPLNVEG---KTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNN 368
Cdd:PRK11889 217 EEVIEYILEDMRSHFNTENvfeKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 369 IPVIAQHtgaDSASVIFDAIQAAKARGVDVLIADTAGRLQNKSHLMEELkkiVRVMKKLDenaPHEVMLTIDASTGQNAV 448
Cdd:PRK11889 297 FEVIAVR---DEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEM---IETMGQVE---PDYICLTLSASMKSKDM 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 333956848 449 SQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIE 498
Cdd:PRK11889 368 IEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
17-172 |
1.65e-11 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 66.99 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 17 QKEQAETEAEQQEQHVTEQPAATEARVEPDSQTQTTAQETTHSLAESEkfADDVVAVSESVIHEEKESAQPETVETSVEA 96
Cdd:PRK10811 849 RPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVE--EPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 97 EPEAV--------KPTAAQAEEWLPEQEENRA---PVALAPEVVAEPQPEASPETIVEEDViEEAAVEEKAVEPAVETPH 165
Cdd:PRK10811 927 QPQVItesdvavaQEVAEHAEPVVEPQDETADieeAAETAEVVVAEPEVVAQPAAPVVAEV-AAEVETVTAVEPEVAPAQ 1005
|
....*..
gi 333956848 166 DAHEIAE 172
Cdd:PRK10811 1006 VPEATVE 1012
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
307-498 |
4.84e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 63.23 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 307 NVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHtgaDSASVIFD 386
Cdd:PRK06731 69 NVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 387 AIQAAKARGVDVLIADTAGRLQNKSHLMEELkkivrvMKKLDENAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLT 466
Cdd:PRK06731 146 LTYFKEEARVDYILIDTAGKNYRASETVEEM------IETMGQVEPDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFT 219
|
170 180 190
....*....|....*....|....*....|..
gi 333956848 467 KLDGTAKGGVIFSVADQFGIPIRYIGVGERIE 498
Cdd:PRK06731 220 KFDETASSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
266-499 |
1.23e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 63.20 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 266 RKIIANLTEGASRKQLrDAEALYG--LLKEEMgEILAKVDEPLNVEGktpfVILMVGVNGVGKTTTIGKLA-RQFEQQGK 342
Cdd:PRK14722 94 RMIVDNLPEGEGYDTL-DAAADWAqsVLAANL-PVLDSEDALMERGG----VFALMGPTGVGKTTTTAKLAaRCVMRFGA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 343 S-VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSAsvifdaIQAAKARGVDVLIADTAGRLQNKSHLMEELKKIv 421
Cdd:PRK14722 168 SkVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQ------LALAELRNKHMVLIDTIGMSQRDRTVSDQIAML- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 422 rvmkkLDENAPHEVMLTIDASTGQNAVSQA-KLFHEAVG--------LTGITLTKLDGTAKGGVIFSVADQFGIPIRYIG 492
Cdd:PRK14722 241 -----HGADTPVQRLLLLNATSHGDTLNEVvQAYRSAAGqpkaalpdLAGCILTKLDEASNLGGVLDTVIRYKLPVHYVS 315
|
....*..
gi 333956848 493 VGERIED 499
Cdd:PRK14722 316 TGQKVPE 322
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
25-180 |
3.42e-09 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 59.67 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 25 AEQQEQHVTEQPAATEARVEPDSQTQTTAQETTHSLAESEKFADDVVAVsESVIHEEKESAQPETVETsveAEPEAVKPT 104
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVE-EPVVVAEPQPEEVVVVET---THPEVIAAP 923
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333956848 105 AAQAEEWLPEQEENRA-PVALAPEVVAEPQPEASPETIVEEDVIEEAAVEEKAVEPAVETPHDAHEIAEDAPISEEE 180
Cdd:PRK10811 924 VTEQPQVITESDVAVAqEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPE 1000
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
313-495 |
4.25e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 58.37 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 313 PFVILMVGVNGVGKTTTIGKLARQF----EQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDai 388
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 389 qaakARGVDVLIADTAGRLQNKSHLMEELKKIVRVMKKldenaPHEVMLTIDASTGQNAVSQakLFH--EAVGLTGITLT 466
Cdd:PRK12723 252 ----SKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGR-----DAEFHLAVSSTTKTSDVKE--IFHqfSPFSYKTVIFT 320
|
170 180
....*....|....*....|....*....
gi 333956848 467 KLDGTAKGGVIFSVADQFGIPIRYIGVGE 495
Cdd:PRK12723 321 KLDETTCVGNLISLIYEMRKEVSYVTDGQ 349
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
61-208 |
6.93e-09 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 58.51 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 61 AESEKFADDVVAVSESVIHEEKESAQPETVETS--VEAEPEAVKPTAAQAEewlPEQEENRAPVALAPEVVAEPQPEAsP 138
Cdd:PRK10811 853 VQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvVEAVAEVVEEPVVVAE---PQPEEVVVVETTHPEVIAAPVTEQ-P 928
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333956848 139 ETIVEEDVIEEAAVEEKAvEPAVETPHDAHEIAEDAPISEEELV---ALAADPEAALETEPEEEETAPVAEQE 208
Cdd:PRK10811 929 QVITESDVAVAQEVAEHA-EPVVEPQDETADIEEAAETAEVVVAepeVVAQPAAPVVAEVAAEVETVTAVEPE 1000
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
70-213 |
9.92e-08 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 55.05 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 70 VVAVSESVIHEEKE----SAQPETVETSVEAEPEAVKPTAAQAEEwlPEQEENRAPVALAPEVVAEPQPEASPETIVEED 145
Cdd:PRK10811 847 VVRPQDVQVEEQREaeevQVQPVVAEVPVAAAVEPVVSAPVVEAV--AEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPV 924
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333956848 146 VIEEAAVEEKAVEPAVETPHDAHEIAEDAP-ISEEELVALAADPEAALETEPEEEETAPVAEQEKPTKE 213
Cdd:PRK10811 925 TEQPQVITESDVAVAQEVAEHAEPVVEPQDeTADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVET 993
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
315-513 |
3.61e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 52.64 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKL-ARQFEQQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPViaqHTGADSASVifdAIQAAK 392
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLaARAVIRHGADkVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADL---QLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 393 ARGVDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDEnaphevMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTA 472
Cdd:PRK14721 267 LRGKHMVLIDTVGMSQRDQMLAEQIAMLSQCGTQVKH------LLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 333956848 473 KGGVIFSVADQFGIPIRYIGVGERI-EDLRPFNAGDFIEALF 513
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
227-299 |
3.86e-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: 47.55 E-value: 3.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333956848 227 KENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVDTTRKIIANLTE---GASRKQLRDAEALYGLLKEEMGEIL 299
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEkakGEVLKGLTPKQEVKKILKEELVKIL 77
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
228-295 |
7.73e-05 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 40.91 E-value: 7.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333956848 228 ENLGSGFISLFRGKKIDDDLFEELEEQLLI----ADVGVDTTRKIIANLTEGA-SRKQLRDAEALYGLLKEEM 295
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEALKELEEalleADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
307-419 |
6.21e-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: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 307 NVEGKTPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLaAGDTFRAA---AVEQLQVWGQRNnipviAQHTGADSASV 383
Cdd:pfam06414 5 TTSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRI-DPDDFRELhphYRELQAADPKTA-----SEYTQPDASRW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 333956848 384 IFDAIQAAKARGVDVLIADTAGRLQNKSHLMEELKK 419
Cdd:pfam06414 79 VEKLLQHAIENGYNIILEGTLRSPDVAKKIARALKA 114
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
308-402 |
1.07e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 41.50 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 308 VEGKTPFVILmVGVNGVGKTTTIGKLARQFEQQGKSVMLAA--GdtfRAAAV--EQLQVWGQrnnipVIAQHTGADSASV 383
Cdd:COG0507 136 ALTTRRVSVL-TGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKRlsESTGIEAR-----TIHRLLGLRPDSG 206
|
90
....*....|....*....
gi 333956848 384 IFDAIQAAKARGVDVLIAD 402
Cdd:COG0507 207 RFRHNRDNPLTPADLLVVD 225
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
315-500 |
1.32e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 41.11 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKL-ARQFEQQGKS-VMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSasvifdAIQAAK 392
Cdd:PRK06995 258 VFALMGPTGVGKTTTTAKLaARCVMRHGASkVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADL------RLALSE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 393 ARGVDVLIADTAGRLQNKSHLMEELKKIVRVmkkldeNAPHEVMLTIDA-STGQ--NAVSQAklfHEAVGLTGITLTKLD 469
Cdd:PRK06995 332 LRNKHIVLIDTIGMSQRDRMVSEQIAMLHGA------GAPVKRLLLLNAtSHGDtlNEVVQA---YRGPGLAGCILTKLD 402
|
170 180 190
....*....|....*....|....*....|..
gi 333956848 470 GTAKGGVIFSVADQFGIPIRYIGVGERI-EDL 500
Cdd:PRK06995 403 EAASLGGALDVVIRYKLPLHYVSNGQRVpEDL 434
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
315-357 |
1.83e-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: 39.07 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 333956848 315 VILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAgDTFRAAAV 357
Cdd:cd17933 14 VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
313-353 |
2.06e-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: 38.84 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 333956848 313 PFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFR 353
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVR 42
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
316-350 |
4.80e-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: 4.80e-03
10 20 30
....*....|....*....|....*....|....*..
gi 333956848 316 ILMV--GVNGVGKTTTIGKLARQFEQQGKSVMLAAGD 350
Cdd:cd01983 2 VIAVtgGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
459-494 |
5.58e-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: 5.58e-03
10 20 30
....*....|....*....|....*....|....*.
gi 333956848 459 GLTGITLTKLDGTAKGGVIFsVADQFGIPIRYIGVG 494
Cdd:cd03108 274 GLTELALTKLDVNAQKYIER-IEELLGVPITYISVG 308
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
320-373 |
8.13e-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: 8.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 333956848 320 GVNGVGKTTTIGKLARQFEQQGKSVML--AAGDTFRAAAVEQLQVWGQRNNIPVIA 373
Cdd:cd01672 7 GIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
315-427 |
8.34e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.55 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956848 315 VILMVGVNGVGKTTTIGKLARQFEQQGKS---VMLAAGDT---FRAAAVEQLQVwgqrnnipviaQHTGADSASVIFDAI 388
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfVDLPSGTSpkdLLRALLRALGL-----------PLSGRLSKEELLAAL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 333956848 389 QAA--KARGVDVLIADTAGRLQNKshLMEELKKIVRVMKKL 427
Cdd:pfam13401 76 QQLllALAVAVVLIIDEAQHLSLE--ALEELRDLLNLSSKL 114
|
|
| |
