|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
3-324 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 532.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 3 FFKKLKDAIVKKSEEVTQKFTEGLSKTRDMMVEKVQDLVRrYKKIDENFFDELEEILITADVGVNTVMDLIDDLKGEVRK 82
Cdd:PRK10416 1 FFSWLKKKKKEKKEGWFERLKKGLSKTRENFGEGINGLFA-KKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 83 HKIENALDLQPILSEKLVALLKNEDNqttSLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAA 162
Cdd:PRK10416 80 KNLKDPEELKELLKEELAEILEPVEK---PLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 163 AIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQREIPDAPHEV 242
Cdd:PRK10416 157 AIEQLQVWGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 243 LLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHALFKG 322
Cdd:PRK10416 237 LLVLDATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGG 316
|
..
gi 1690706344 323 LI 324
Cdd:PRK10416 317 ED 318
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
20-322 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 523.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 20 QKFTEGLSKTRDMMVEKVQDLVRRYKKIDENFFDELEEILITADVGVNTVMDLIDDLKGEVRKHKIENALDLQPILSEKL 99
Cdd:COG0552 3 ERLKEGLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 100 VALLKNEDNqttSLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVV 179
Cdd:COG0552 83 LEILDPVDK---PLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 180 RQNQGSDPAAVIYDALQEAKNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQREIPDAPHEVLLVLDATTGQNALNQAK 259
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1690706344 260 VFGETTKVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHALFKG 322
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGE 302
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
46-320 |
7.61e-143 |
|
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: 404.72 E-value: 7.61e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 46 KIDENFFDELEEILITADVGVNTVMDLIDDLKGEVRKHKIENALDLQPILSEKLVALLKNEDNQTTSL--NIEEGRLNVI 123
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDLelIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 124 LFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKNRNV 203
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 204 DILLCDTAGRLQNKVGLMDELAKVFRVVQREIPDAPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAKGGI 283
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1690706344 284 VIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHALF 320
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
121-319 |
8.72e-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: 348.41 E-value: 8.72e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 121 NVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKN 200
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 201 RNVDILLCDTAGRLQNKVGLMDELAKVFRVVQREIPDAPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAK 280
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1690706344 281 GGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHAL 319
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
121-319 |
2.40e-106 |
|
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: 309.09 E-value: 2.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 121 NVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKN 200
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 201 RNVDILLCDTAGRLQNKVGLMDELAKVFRVVqreipdAPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAK 280
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVV------APDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1690706344 281 GGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHAL 319
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
121-321 |
5.17e-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: 308.18 E-value: 5.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 121 NVILFVGVNGVGKTTTIGKMAHMFRQQG-KKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAK 199
Cdd:smart00962 2 GVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 200 NRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTA 279
Cdd:smart00962 82 ARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1690706344 280 KGGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHALFK 321
Cdd:smart00962 156 KGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
2-320 |
1.35e-87 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 266.45 E-value: 1.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 2 SFFKKLKDAIVKKSEEVTQKFTEGLSKTRDMMVEKVQDLVRR--YKKIDE----NFFDELEEILITADVGVNTVMDLIDD 75
Cdd:PRK14974 11 KFVEKVEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKakITEIKEkdieDLLEELELELLESDVALEVAEEILES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 76 LKGEVRKHKIENALDLQPILSEKLVALLKNEDNQTTSLNIEEGRLN-----VILFVGVNGVGKTTTIGKMAHMFRQQGKK 150
Cdd:PRK14974 91 LKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSVGDLFDLIEEIKSkgkpvVIVFVGVNGTGKTTTIAKLAYYLKKNGFS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 151 VLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKNRNVDILLCDTAGRLQNKVGLMDELAKVFRV 230
Cdd:PRK14974 171 VVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 231 VQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKMDDLQQF 310
Cdd:PRK14974 251 TK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPF 324
|
330
....*....|
gi 1690706344 311 DPEQFVHALF 320
Cdd:PRK14974 325 DPDWFVDKLL 334
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
42-316 |
2.85e-84 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 260.72 E-value: 2.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 42 RRYKKIDENFFDE-LEEI---LITADVGVNTVMDLIDDLKGEVRKHKIENALDlqP------ILSEKLVALLKNEdnqTT 111
Cdd:COG0541 17 RGKGRLTEENIKEaLREVrraLLEADVNLKVVKDFIERVKERALGEEVLKSLT--PgqqvikIVHDELVELLGGE---NE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 112 SLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVI 191
Cdd:COG0541 92 ELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 192 YDALQEAKNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIV 271
Cdd:COG0541 172 KRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1690706344 272 LTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFV 316
Cdd:COG0541 246 LTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMA 290
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
121-319 |
3.67e-84 |
|
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: 252.68 E-value: 3.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 121 NVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKN 200
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 201 RNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAK 280
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVES------PDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1690706344 281 GGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHAL 319
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
121-313 |
3.12e-72 |
|
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: 222.09 E-value: 3.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 121 NVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKN 200
Cdd:cd18539 1 TVILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 201 RNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAK 280
Cdd:cd18539 81 EGFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDAR 154
|
170 180 190
....*....|....*....|....*....|...
gi 1690706344 281 GGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPE 313
Cdd:cd18539 155 GGAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
33-316 |
1.47e-68 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 220.85 E-value: 1.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 33 MVEKVQDLVRRYK---KIDENFFDE----LEEILITADVGVNTVMDLIDDLKgevrkhkiENALDLQP------------ 93
Cdd:PRK00771 1 LGESLRDALKKLAgksRIDEKTVKEvvkdIQRALLQADVNVKLVKELSKSIK--------ERALEEEPpkgltprehvik 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 94 ILSEKLVALLKNEdnqtTSLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQR 173
Cdd:PRK00771 73 IVYEELVKLLGEE----TEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 174 VGVDVVRQNQGSDPAAVIYDALQEAKNRNVDILlcDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQN 253
Cdd:PRK00771 149 IGVPFYGDPDNKDAVEIAKEGLEKFKKADVIIV--DTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQ 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1690706344 254 ALNQAKVFGETTKVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFV 316
Cdd:PRK00771 221 AKNQAKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
121-316 |
1.82e-60 |
|
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: 192.02 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 121 NVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKN 200
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 201 RNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAK 280
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1690706344 281 GGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFV 316
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
122-319 |
7.00e-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: 165.09 E-value: 7.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 122 VILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKNR 201
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARDQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 202 NVDILLCDTAGRLQNKVGLMDELAKVFRVVQreiPDApheVLLVLDATTGQNALNQAKVF----------GETTKVSGIV 271
Cdd:cd17876 82 GFDVVLIDTAGRMQNNEPLMRALAKLIKENN---PDL---VLFVGEALVGNDAVDQLKKFnqaladyspsDNPRLIDGIV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1690706344 272 LTKLDGTA-KGGIVIAIRNELNIPVKYVGLGEKMDDLQQFDPEQFVHAL 319
Cdd:cd17876 156 LTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
54-325 |
5.25e-48 |
|
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: 166.93 E-value: 5.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 54 ELEEILITADVGVNTVMDLIDDLKGEVRKHKIENALD----LQPILSEKLVALLkneDNQTTSLNIEEGRLNVILFVGVN 129
Cdd:TIGR01425 33 EICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINkrklIQDAVFEELCNLV---DPGVEAFTPKKGKTCVIMFVGLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 130 GVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDALQEAKNRNVDILLCD 209
Cdd:TIGR01425 110 GAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 210 TAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAKGGIVIAIRN 289
Cdd:TIGR01425 190 TSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKGGGALSAVA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1690706344 290 ELNIPVKYVGLGEKMDDLQQFDPEQFVHALF-----KGLID 325
Cdd:TIGR01425 264 ATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLgmgdlKGLID 304
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
12-323 |
2.86e-39 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 142.31 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 12 VKKSEEVTQKFTEGLSKTRDMMVEKVQDLVRRYKKIDENFfDELEEILITADVGVNTVMDLIDDLKGEVRKHKIENALdl 91
Cdd:COG1419 69 AAAEEEELEELRRELAELKELLEEQLSGLAGESARLPPEL-AELLERLLEAGVSPELARELLEKLPEDLSAEEAWRAL-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 92 qpilSEKLVALLKNEDNQTtslnIEEGRlnVILFVGVNGVGKTTTIGKMAHMF-RQQGKKVLLAAGDTFRAAAIEQLEVW 170
Cdd:COG1419 146 ----LEALARRLPVAEDPL----LDEGG--VIALVGPTGVGKTTTIAKLAARFvLRGKKKVALITTDTYRIGAVEQLKTY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 171 GQRVGVdvvrqnqgsdPAAVIYDA--LQEA--KNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipdaPHEVLLVL 246
Cdd:COG1419 216 ARILGV----------PVEVAYDPeeLKEAleRLRDKDLVLIDTAGRSPRDPELIEELKALLDAGP------PIEVYLVL 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1690706344 247 DATT-GQNALNQAKVFGEtTKVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKM-DDLQQFDPEQFVHALFKGL 323
Cdd:COG1419 280 SATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLLGGL 357
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
122-316 |
3.67e-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: 121.12 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 122 VILFVGVNGVGKTTTIGKMAHMFR-QQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDPAAVIYDAlqeakn 200
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADALERL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 201 RNVDILLCDTAGRLQNKVGLMDELAKVFRVvqreipDAPHEVLLVLDATTGQNALNQA----KVFGettkVSGIVLTKLD 276
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKELLGA------GEDIEVHLVLSATTKAKDLKEIierfSPLG----YRGLILTKLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1690706344 277 GTAKGGIVIAIRNELNIPVKYVGLGEKM-DDLQQFDPEQFV 316
Cdd:cd17873 146 ETTSLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLA 186
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
30-323 |
5.25e-29 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 115.76 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 30 RDMMVEKVQDLvrRYKKIDENFFDELEEILITADVGVNTVMDLIDDLkgevrkhkIENALDLQPILSEKLVALLKNE-DN 108
Cdd:PRK05703 143 KNLLEDQLSGL--RQVERIPPEFAELYKRLKRSGLSPEIAEKLLKLL--------LEHMPPRERTAWRYLLELLANMiPV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 109 QTTSLNIEEGrlnVILFVGVNGVGKTTTIGKMA--HMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVdvvrqnqgsd 186
Cdd:PRK05703 213 RVEDILKQGG---VVALVGPTGVGKTTTLAKLAarYALLYGKKKVALITLDTYRIGAVEQLKTYAKIMGI---------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 187 PAAVIYDA--LQEAKN--RNVDILLCDTAGRLQNKVGLMDELAKVFrvvqrEIPDAPHEVLLVLDATTG----QNALNQA 258
Cdd:PRK05703 280 PVEVVYDPkeLAKALEqlRDCDVILIDTAGRSQRDKRLIEELKALI-----EFSGEPIDVYLVLSATTKyedlKDIYKHF 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1690706344 259 KVFGettkVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKM-DDLQQFDPEQFVHALFKGL 323
Cdd:PRK05703 355 SRLP----LDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLLLGGF 416
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
122-325 |
5.21e-20 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 91.02 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 122 VILFVGVNGVGKTTTIGKMAHMF--RQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDV--VRQnqgsdpAAVIYDALQE 197
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCvaREGADQLALLTTDSFRIGALEQLRIYGRILGVPVhaVKD------AADLRFALAA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 198 AKNRNvdILLCDTAGRLQNKVGLMDE---LAKVFRVVQReipdaphevLLVLDATTGQNALNQ---AKVFGETTKVSGIV 271
Cdd:PRK14723 261 LGDKH--LVLIDTVGMSQRDRNVSEQiamLCGVGRPVRR---------LLLLNAASHGDTLNEvvhAYRHGAGEDVDGCI 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1690706344 272 LTKLDGTAKGGIVI--AIRNELniPVKYVGLGEKMddlqqfdPEQFVHALFKGLID 325
Cdd:PRK14723 330 ITKLDEATHLGPALdtVIRHRL--PVHYVSTGQKV-------PEHLELAQADELVD 376
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
52-212 |
1.26e-18 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 84.31 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 52 FDELEEILITADVGVNTVMDLIDDLKGEVRKHKIENALdlQPILSEKLVALLKNEDNQttslniEEGRlnVILFVGVNGV 131
Cdd:TIGR03499 136 RAKLYERLLEAGVSEELARELLEKLPEDADAEDAWRWL--REALEGMLPVKPEEDPIL------EQGG--VIALVGPTGV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 132 GKTTTIGKMA--HMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQ--RVGVDVVRqnqgsDPAAViYDALQEakNRNVDILL 207
Cdd:TIGR03499 206 GKTTTLAKLAarFALEHGKKKVALITTDTYRIGAVEQLKTYAEilGIPVKVAR-----DPKEL-REALDR--LRDKDLIL 277
|
....*
gi 1690706344 208 CDTAG 212
Cdd:TIGR03499 278 IDTAG 282
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
115-309 |
6.74e-17 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 81.57 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 115 IEEGrlNVILFVGVNGVGKTTTIGKMAHMFRQQ--GKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDpaavIY 192
Cdd:PRK12727 347 LERG--GVIALVGPTGAGKTTTIAKLAQRFAAQhaPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAES----LL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 193 DALQeaKNRNVDILLCDTAGRLQNKVGLMDELA--KVFRVVQReipdaphevLLVLDATTGQNALNQ-AKVFGeTTKVSG 269
Cdd:PRK12727 421 DLLE--RLRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTS---------LLVLPANAHFSDLDEvVRRFA-HAKPQG 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1690706344 270 IVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKM-DDLQQ 309
Cdd:PRK12727 489 VVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHR 529
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
7-306 |
8.62e-17 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 80.54 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 7 LKDAIVKKSEE-VTQKFTEGLSKTRDMMVEKVQDLVRRYKKIDENFFDELEEILITADVGVNTVMDLIDDLKGEVRKHKI 85
Cdd:PRK14722 30 VADAVKARIERiVNDTVMQELGSLRELMEEQFAGLMWNERQRRNPVHGALTKYLFAAGFSAQLVRMIVDNLPEGEGYDTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 86 ENALD-LQPILSEKLvALLKNEDNQttslnIEEGrlNVILFVGVNGVGKTTTIGKMAH--MFRQQGKKVLLAAGDTFRAA 162
Cdd:PRK14722 110 DAAADwAQSVLAANL-PVLDSEDAL-----MERG--GVFALMGPTGVGKTTTTAKLAArcVMRFGASKVALLTTDSYRIG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 163 AIEQLEVWGQRVGVDVVRQNQGSDpaavIYDALQEAKNRNvdILLCDTAGRLQNKVGLMDELAKVFRVvqreipDAPHEV 242
Cdd:PRK14722 182 GHEQLRIFGKILGVPVHAVKDGGD----LQLALAELRNKH--MVLIDTIGMSQRDRTVSDQIAMLHGA------DTPVQR 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1690706344 243 LLVLDATTGQNALNQ---------AKVFGETTKVSGIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKMDD 306
Cdd:PRK14722 250 LLLLNATSHGDTLNEvvqayrsaaGQPKAALPDLAGCILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
115-321 |
1.00e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 71.52 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 115 IEEGrlNVILFVGVNGVGKTTTIGKMAH--MFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQGSDpaavIY 192
Cdd:PRK14721 188 IEQG--GVYALIGPTGVGKTTTTAKLAAraVIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIAD----LQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 193 DALQEAKNRNvdILLCDTAGRLQNKVGLMDELAKvfrvvqreIPDAPHEV--LLVLDATTGQNALNQAKVFGETTKVSGI 270
Cdd:PRK14721 262 LMLHELRGKH--MVLIDTVGMSQRDQMLAEQIAM--------LSQCGTQVkhLLLLNATSSGDTLDEVISAYQGHGIHGC 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1690706344 271 VLTKLDGTAKGGIVI--AIRNELNIpvKYVGLGEKM-DDLQQFDPEQFVHALFK 321
Cdd:PRK14721 332 IITKVDEAASLGIALdaVIRRKLVL--HYVTNGQKVpEDLHEANSRYLLHRIFK 383
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
119-250 |
1.82e-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: 67.01 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 119 RLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEvwgqrvGVDVVRQNQGSDPAAVIYDALQEA 198
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1690706344 199 KNRNVDILLCDTAGRLQNKVGLMDELAKVFrvVQREIPDAPHEVLLVLDATT 250
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEE--LRLLLLLKSEKNLTVILTTN 124
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
79-287 |
8.21e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 68.94 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 79 EVRKHKIENAldlQPILSEKLVA-LLKNEDNQTTSLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGD 157
Cdd:PRK11889 202 EKLKVKFENA---TMITEEEVIEyILEDMRSHFNTENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 158 TFRAAAIEQLEVWGQRVGVDVVR-QNQGSDPAAVIYDAlQEAKnrnVDILLCDTAGRLQNKVGLMDELAKVFRVVQreip 236
Cdd:PRK11889 279 HSRIGTVQQLQDYVKTIGFEVIAvRDEAAMTRALTYFK-EEAR---VDYILIDTAGKNYRASETVEEMIETMGQVE---- 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1690706344 237 daPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAKGGIVIAI 287
Cdd:PRK11889 351 --PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKI 399
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
78-295 |
3.05e-12 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 65.92 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 78 GEVRKHKIENAldlQPILSEKLVALLKNEDNQTTSLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGD 157
Cdd:PRK06731 36 AEKLKVKFENA---TMITEEVIEYILEDMSSHFNTENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 158 TFRAAAIEQLEVWGQRVGVDVVRQNqgsDPAAVIYDALQEAKNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQreipd 237
Cdd:PRK06731 113 HSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVE----- 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1690706344 238 aPHEVLLVLDATTGQNALNQAKVFGETTKVSGIVLTKLDGTAKGGIVIAIRNELNIPV 295
Cdd:PRK06731 185 -PDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPI 241
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
16-319 |
9.61e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 65.31 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 16 EEVTQKFTEGLSKTRDMMVEKVQDLVRRYKK--------IDENFFDELEEILITADVGVNTVMDLIDDLKGEVRKHKIEn 87
Cdd:PRK12723 67 EDEKRKILQSIKKEENSSIEDVLKEVKSLKNelahkkeeINHPTILKIEDILRENDFSESYIKDINEFIKKEFSLSDLD- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 88 alDLQPILSEKLVALLKNEdnQTTSLNIEEGRLNVILFVGVNGVGKTTTIGKMAHMF----RQQGKKVLLAAGDTFRAAA 163
Cdd:PRK12723 146 --DYDKVRDSVIIYIAKTI--KCSGSIIDNLKKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 164 IEQLEVWGQRVGVDVvrqnqgsdPAAVIYDALQE--AKNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQREIpdaphE 241
Cdd:PRK12723 222 KKQIQTYGDIMGIPV--------KAIESFKDLKEeiTQSKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGRDA-----E 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 242 VLLVLDATTG----QNALNQAKVFGETTkvsgIVLTKLDGTAKGGIVIAIRNELNIPVKYVGLGEKM-DDLQQFDPEQFV 316
Cdd:PRK12723 289 FHLAVSSTTKtsdvKEIFHQFSPFSYKT----VIFTKLDETTCVGNLISLIYEMRKEVSYVTDGQIVpHNISIAEPLTFI 364
|
...
gi 1690706344 317 HAL 319
Cdd:PRK12723 365 KKI 367
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
45-103 |
9.86e-12 |
|
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: 59.87 E-value: 9.86e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1690706344 45 KKIDENFFDELEEILITADVGVNTVMDLIDDLKGEVRKHKIENALD---LQPILSEKLVALL 103
Cdd:smart00963 16 EKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGEVLKGLTPkqeVKKILKEELVKIL 77
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
122-306 |
7.34e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 62.83 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 122 VILFVGVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVrqnQGSDPAAvIYDALQEAKNR 201
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELI---VATSPAE-LEEAVQYMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 202 N-VDILLCDTAGRLQNKVGLMDELAKVFRVVqreipdapHEVLLVLDATTGQNALNQAKVFGETTK--VSGIVLTKLDGT 278
Cdd:PRK12726 284 NcVDHILIDTVGRNYLAEESVSEISAYTDVV--------HPDLTCFTFSSGMKSADVMTILPKLAEipIDGFIITKMDET 355
|
170 180
....*....|....*....|....*...
gi 1690706344 279 AKGGIVIAIRNELNIPVKYVGLGEKMDD 306
Cdd:PRK12726 356 TRIGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
126-303 |
3.34e-10 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 60.75 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 126 VGVNGVGKTTTIGKMAHMF--RQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDV--VRQnqgsdpAAVIYDALQEAKNR 201
Cdd:PRK06995 262 MGPTGVGKTTTTAKLAARCvmRHGASKVALLTTDSYRIGGHEQLRIYGKILGVPVhaVKD------AADLRLALSELRNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 202 NvdILLCDTAG---RLQNKVGLMDELAKVFRVVQReipdaphevLLVLDATTGQNALN---QA-KVFGettkVSGIVLTK 274
Cdd:PRK06995 336 H--IVLIDTIGmsqRDRMVSEQIAMLHGAGAPVKR---------LLLLNATSHGDTLNevvQAyRGPG----LAGCILTK 400
|
170 180 190
....*....|....*....|....*....|.
gi 1690706344 275 LDGTAKGGIV--IAIRNELniPVKYVGLGEK 303
Cdd:PRK06995 401 LDEAASLGGAldVVIRYKL--PLHYVSNGQR 429
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
117-276 |
4.29e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 60.36 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 117 EGRLNVILFVGVNGVGKTTTIGKMA-HMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVrqnqgsdPAAVIYDAL 195
Cdd:PRK12724 220 KNQRKVVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFY-------PVKDIKKFK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 196 QEAKNRNVDILLCDTAGRLQNKVGLMDELAKVFRVVQREipDAPhEVLLVLDATTG-QNALNQAKVFgETTKVSGIVLTK 274
Cdd:PRK12724 293 ETLARDGSELILIDTAGYSHRNLEQLERMQSFYSCFGEK--DSV-ENLLVLSSTSSyHHTLTVLKAY-ESLNYRRILLTK 368
|
..
gi 1690706344 275 LD 276
Cdd:PRK12724 369 LD 370
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
41-99 |
9.47e-09 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 51.31 E-value: 9.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1690706344 41 VRRYKKIDENFFDE----LEEILITADVGVNTVMDLIDDLK-GEVRKHKIENALDLQPILSEKL 99
Cdd:pfam02881 12 LRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLReKAVGEKKLKPPQEVKKILKEEL 75
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
117-249 |
1.25e-04 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 42.17 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 117 EGRLNVILFVGVN-GVGKTTTIGKMAHMFRQQGKKVLLAAGDtFRAAAIEQLEVWGQRVGV-DVVRQNqgsdpaAVIYDA 194
Cdd:cd05387 16 DAGPKVIAVTSASpGEGKSTVAANLAVALAQSGKRVLLIDAD-LRRPSLHRLLGLPNEPGLsEVLSGQ------ASLEDV 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1690706344 195 LQEAKNRNVDILlcdTAG-------------RLQNkvgLMDELAKVFRVVqreIPDAPhEVLLVLDAT 249
Cdd:cd05387 89 IQSTNIPNLDVL---PAGtvppnpsellsspRFAE---LLEELKEQYDYV---IIDTP-PVLAVADAL 146
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
123-209 |
2.47e-04 |
|
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: 41.49 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 123 ILFVGVNGVGKTTTIGKMAHMFRQQGKKVLL--AAGDTFRAAAIEQLEVWGQRVGVDVV----------RQNQgsdpAAV 190
Cdd:cd01672 3 IVFEGIDGAGKTTLIELLAERLEARGYEVVLtrEPGGTPIGEAIRELLLDPEDEKMDPRaelllfaadrAQHV----EEV 78
|
90
....*....|....*....
gi 1690706344 191 IYDALQEAKnrnvdILLCD 209
Cdd:cd01672 79 IKPALARGK-----IVLSD 92
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
111-276 |
2.89e-04 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 41.27 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 111 TSLNIEEGRLNVILFVGVN-GVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNQgsdpaA 189
Cdd:TIGR01007 8 TNIQFSGAEIKVLLITSVKpGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSGT-----T 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 190 VIYDALQEAKNRNVDILlcdTAGR--------LQNK--VGLMDELAKVFRVVQREIP------DAP------HEVLLVLD 247
Cdd:TIGR01007 83 DLSDAICDTNIENLDVI---TAGPvppnptelLQSSnfKTLIETLRKRFDYIIIDTPpigtvtDAAiiaracDASILVTD 159
|
170 180 190
....*....|....*....|....*....|..
gi 1690706344 248 A-TTGQNALNQAKVFGETT--KVSGIVLTKLD 276
Cdd:TIGR01007 160 AgKIKKREVKKAKEQLEQAgsNFLGVVLNKVD 191
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
119-295 |
4.82e-03 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 38.24 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 119 RLNVILFV-GVNGVGKTTTIGKMAHMFRQQGKKVLLAAGDTFRAAAIEQLEVWGQRVGVDVVRQNqgsdpaAVIYDALQE 197
Cdd:COG0489 91 LLEVIAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGE------ASLEDVIQP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690706344 198 AKNRNVDILlcdTAGRL-QNKVGLM---------DELAKVFRVVqreIPDAPHeVLLVLDATTGQNALNQAkvfgettkv 267
Cdd:COG0489 165 TEVEGLDVL---PAGPLpPNPSELLaskrlkqllEELRGRYDYV---IIDTPP-GLGVADATLLASLVDGV--------- 228
|
170 180 190
....*....|....*....|....*....|
gi 1690706344 268 sgIVLTKLDGTAKGGIVIAIR--NELNIPV 295
Cdd:COG0489 229 --LLVVRPGKTALDDVRKALEmlEKAGVPV 256
|
|
| |
