|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
45-346 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 570.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 45 FFARLKKGLLKTRQNLGSGFLGLFTG-KKIDDDLFDELEEQLLIADVGVDTTRKIIDNLTAHASRKELKDAEALYSKLRE 123
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 124 EMSDILAGVDKPLVIEDKKPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVA 203
Cdd:COG0552 81 ELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 204 QHTGADPASVIFDAIQSAKAKGVDVLIADTAGRLQNKAHLMEELKKIVRVMKKLDEEAPHEIMLTLDASTGQNAVSQAKL 283
Cdd:COG0552 161 QKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAKV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2440851348 284 FNDAVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEALFARE 346
Cdd:COG0552 241 FNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
36-347 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 565.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 36 EQEKPKKEGFFARLKKGLLKTRQNLGSGFLGLFTGKKIDDDLFDELEEQLLIADVGVDTTRKIIDNLTAHASRKELKDAE 115
Cdd:PRK10416 7 KKKKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 116 ALYSKLREEMSDILAGVDKPLVIEDKKPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGE 195
Cdd:PRK10416 87 ELKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 196 RNRIPVVAQHTGADPASVIFDAIQSAKAKGVDVLIADTAGRLQNKAHLMEELKKIVRVMKKLDEEAPHEIMLTLDASTGQ 275
Cdd:PRK10416 167 RVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQ 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2440851348 276 NAVSQAKLFNDAVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEALFAREE 347
Cdd:PRK10416 247 NALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
72-343 |
6.49e-144 |
|
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: 407.80 E-value: 6.49e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 72 KIDDDLFDELEEQLLIADVGVDTTRKIIDNLTAHASRKELKDAEALYSKLREEMSDILA-----GVDKPLVIEDKKPYVI 146
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKedllkNTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 147 LMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKAKGV 226
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 227 DVLIADTAGRLQNKAHLMEELKKIVRVMKKLDEEAPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAKGGV 306
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 2440851348 307 IFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEALF 343
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
144-342 |
1.35e-119 |
|
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: 343.01 E-value: 1.35e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 144 YVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKA 223
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 224 KGVDVLIADTAGRLQNKAHLMEELKKIVRVMKKLDEEAPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAK 303
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2440851348 304 GGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEAL 342
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
143-343 |
3.69e-107 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 311.65 E-value: 3.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 143 PYVILMVGVNGVGKTTTIGKLARQYQSEG-KTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSA 221
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 222 KAKGVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGT 301
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2440851348 302 AKGGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEALF 343
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
145-342 |
7.94e-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: 300.23 E-value: 7.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKAK 224
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 225 GVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAKG 304
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKG 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2440851348 305 GVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEAL 342
Cdd:pfam00448 156 GAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
144-342 |
4.05e-99 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 291.20 E-value: 4.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 144 YVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKA 223
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 224 KGVDVLIADTAGRLQNKAHLMEELKKIVRVmkkldeEAPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAK 303
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2440851348 304 GGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEAL 342
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
14-344 |
1.32e-92 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 279.55 E-value: 1.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 14 EAQDIVALRDEVLSEQEEPKQTEQEKPKKEGFFARLKKGLLKtrqnlgsgflglftGKKIDDDLfDELEEQLLIADVGVD 93
Cdd:PRK14974 18 EKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAKITEIK--------------EKDIEDLL-EELELELLESDVALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 94 TTRKIIDNLTA-----HASRKELKDaEALYSKLREEMSDILaGVDKPLVIED-----KKPYVILMVGVNGVGKTTTIGKL 163
Cdd:PRK14974 83 VAEEILESLKEklvgkKVKRGEDVE-EIVKNALKEALLEVL-SVGDLFDLIEeikskGKPVVIVFVGVNGTGKTTTIAKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 164 ARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKAKGVDVLIADTAGRLQNKAHL 243
Cdd:PRK14974 161 AYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 244 MEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGI 323
Cdd:PRK14974 241 MDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGV 314
|
330 340
....*....|....*....|.
gi 2440851348 324 GEGIEDLRPFKADDFIEALFA 344
Cdd:PRK14974 315 GQGYDDLIPFDPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
59-336 |
5.75e-82 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 255.33 E-value: 5.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 59 NLGSGFLGLF---TGK-KIDDDLFDE-LEE---QLLIADVGVDTTRKIIDNLTAHASRKE----LKDAEALYSKLREEMS 126
Cdd:COG0541 4 NLSERLQGAFkklRGKgRLTEENIKEaLREvrrALLEADVNLKVVKDFIERVKERALGEEvlksLTPGQQVIKIVHDELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 127 DILAGVDKPLVIEDKKPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHT 206
Cdd:COG0541 84 ELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 207 GADPASVIFDAIQSAKAKGVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFND 286
Cdd:COG0541 164 GKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2440851348 287 AVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGIEDLRPFKAD 336
Cdd:COG0541 238 ALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPD 287
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
145-336 |
9.52e-70 |
|
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349786 Cd Length: 193 Bit Score: 216.31 E-value: 9.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKAK 224
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 225 GVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAKG 304
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|..
gi 2440851348 305 GVIFSIADQFGIPIRYIGIGEGIEDLRPFKAD 336
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
58-339 |
3.33e-67 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 217.77 E-value: 3.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 58 QNLGSGFLGLFTGKKIDDDLFDE----LEEQLLIADVGVDTTRKIIDNLTAHASRKE----LKDAEALYSKLREEMSDIL 129
Cdd:PRK00771 3 ESLRDALKKLAGKSRIDEKTVKEvvkdIQRALLQADVNVKLVKELSKSIKERALEEEppkgLTPREHVIKIVYEELVKLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 130 aGVDKPLVIEDKKPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGAD 209
Cdd:PRK00771 83 -GEETEPLVLPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 210 PASVIFDAIQsaKAKGVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVG 289
Cdd:PRK00771 162 AVEIAKEGLE--KFKKADVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2440851348 290 LTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFI 339
Cdd:PRK00771 234 IGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
144-342 |
1.51e-56 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 182.39 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 144 YVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKA 223
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 224 KGVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAK 303
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2440851348 304 GGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEAL 342
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
144-342 |
5.76e-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: 165.87 E-value: 5.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 144 YVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKA 223
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 224 KGVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAV----------GLTGI 293
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN------PDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2440851348 294 TLTKLDGTA-KGGVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEAL 342
Cdd:cd17876 155 VLTKFDTIDdKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
73-342 |
3.32e-45 |
|
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: 159.61 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 73 IDDD----LFDELEEQLLIADVGVDTTRKIIDNLTAHASRKELKDAEALYSKLR----EEMSDILAGVDKPLVIEDKKPY 144
Cdd:TIGR01425 22 IDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQdavfEELCNLVDPGVEAFTPKKGKTC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIFDAIQSAKAK 224
Cdd:TIGR01425 102 VIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIASEGVEKFRKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 225 GVDVLIADTAGRLQNKAHLMEELKKIVRVMKkldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAKG 304
Cdd:TIGR01425 182 KFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVIITKLDGHAKG 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 2440851348 305 GVIFSIADQFGIPIRYIGIGEGIEDLRPFKADDFIEAL 342
Cdd:TIGR01425 256 GGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
18-347 |
1.40e-41 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 148.47 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 18 IVALRDEVLSEQ---EEPKQTEQEKPKKEGFFARLK------KGLLKTRQNLGSGFLGLFTGkkidddLFDELEEQLLIA 88
Cdd:COG1419 45 VTAAVDEDEAEKapaAAAAPAAASAAAEEEELEELRrelaelKELLEEQLSGLAGESARLPP------ELAELLERLLEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 89 DVGVDTTRKIIDNLtahasrKELKDAEALYSKLREEMSDILAGVDKPLvIEDKKpyVILMVGVNGVGKTTTIGKLARQY- 167
Cdd:COG1419 119 GVSPELARELLEKL------PEDLSAEEAWRALLEALARRLPVAEDPL-LDEGG--VIALVGPTGVGKTTTIAKLAARFv 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 168 QSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIfdaiqsAKAKGVDVLIADTAGRLQNKAHLMEEL 247
Cdd:COG1419 190 LRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 248 KKIVRVMKkldeeaPHEIMLTLDAST-GQNAVSQAKLFNDaVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEG 326
Cdd:COG1419 264 KALLDAGP------PIEVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQR 336
|
330 340
....*....|....*....|..
gi 2440851348 327 I-EDLRPFKADDFIEALFAREE 347
Cdd:COG1419 337 VpEDIEVADPERLARLLLGGLE 358
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
75-347 |
1.04e-29 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 117.69 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 75 DDLFDELEEQLLIADVGVDTTRKIIDNLTAHASRKElkdaEALYSKLREEMSDILAGVDKPLVIEDKkpyVILMVGVNGV 154
Cdd:PRK05703 160 PPEFAELYKRLKRSGLSPEIAEKLLKLLLEHMPPRE----RTAWRYLLELLANMIPVRVEDILKQGG---VVALVGPTGV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 155 GKTTTIGKLARQY--QSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPAsvifDAIQSAKAKGVdVLIaD 232
Cdd:PRK05703 233 GKTTTLAKLAARYalLYGKKKVALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELA----KALEQLRDCDV-ILI-D 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 233 TAGRLQNKAHLMEELKKIVRvmkklDEEAPHEIMLTLdASTGQNAVSQA--KLFNDaVGLTGITLTKLDGTAKGGVIFSI 310
Cdd:PRK05703 307 TAGRSQRDKRLIEELKALIE-----FSGEPIDVYLVL-SATTKYEDLKDiyKHFSR-LPLDGLIFTKLDETSSLGSILSL 379
|
250 260 270
....*....|....*....|....*....|....*...
gi 2440851348 311 ADQFGIPIRYIGIGEGI-EDLRPFKADDFIEALFAREE 347
Cdd:PRK05703 380 LIESGLPISYLTNGQRVpDDIKVANPEELVRLLLGGFN 417
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
145-342 |
2.83e-29 |
|
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: 111.10 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYQ-SEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIfdaiqsAKA 223
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADAL------ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 224 KGVDVLIADTAGRLQNKAHLMEELKKIvrvmkkLDEEAPHEIMLTLDAST-GQNAVSQAKLFNdAVGLTGITLTKLDGTA 302
Cdd:cd17873 76 SDRDLILIDTAGRSPRDKEQLEELKEL------LGAGEDIEVHLVLSATTkAKDLKEIIERFS-PLGYRGLILTKLDETT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2440851348 303 KGGVIFSIADQFGIPIRYIGIGEGI-EDLRPFKADDFIEAL 342
Cdd:cd17873 149 SLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
7-235 |
1.07e-21 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 93.17 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 7 AEEQAKLEAQDIVALRDEVLSEQEEPKQTEQEKPKKEGFFARLKKGLLKTRQNLGSGFLGLftGKKIDDDLFDELEEQLL 86
Cdd:TIGR03499 67 ALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEALRELLERLLAGL--AWLQRPPERAKLYERLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 87 IADVGVDTTRKIIDNLtahasrKELKDAEALYSKLREEMSDILAGVDKPLVIEDKKPYVILmVGVNGVGKTTTIGKLARQ 166
Cdd:TIGR03499 145 EAGVSEELARELLEKL------PEDADAEDAWRWLREALEGMLPVKPEEDPILEQGGVIAL-VGPTGVGKTTTLAKLAAR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2440851348 167 Y--QSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVvaqHTGADPASVIfDAIQSAKAKGVdVLIaDTAG 235
Cdd:TIGR03499 218 FalEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPV---KVARDPKELR-EALDRLRDKDL-ILI-DTAG 282
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
57-129 |
1.38e-15 |
|
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: 70.66 E-value: 1.38e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2440851348 57 RQNLGSGFLGLFTGKKIDDDLFDELEEQLLIADVGVDTTRKIIDNLTAHASR---KELKDAEALYSKLREEMSDIL 129
Cdd:smart00963 2 SKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
102-328 |
1.03e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 68.55 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 102 LTAHASRKELKDAEALYSKLREEMSDILAGVDKPLVIE---DKKPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAA 178
Cdd:PRK11889 197 IHAYAEKLKVKFENATMITEEEVIEYILEDMRSHFNTEnvfEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFIT 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 179 GDTFRAAAVEQLQVWGERNRIPVVAQHtgaDPASVIFDAIQSAKAKGVDVLIADTAGRLQNKAHLMEELkkiVRVMKKLD 258
Cdd:PRK11889 277 TDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTYFKEEARVDYILIDTAGKNYRASETVEEM---IETMGQVE 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2440851348 259 eeaPHEIMLTLDAS-TGQNAVSQAKLFNDaVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGIE 328
Cdd:PRK11889 351 ---PDYICLTLSASmKSKDMIEIITNFKD-IHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
145-344 |
2.40e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 67.90 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQY-QSEGK-TVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADpasvIFDAIQSAK 222
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCvAREGAdQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 223 AKGVdVLIaDTAGRLQNKAHLMEELKKIVRVmkkldeEAPHEIMLTLD-ASTGQ--NAVSQAKLFNDAVGLTGITLTKLD 299
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLLNaASHGDtlNEVVHAYRHGAGEDVDGCIITKLD 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2440851348 300 GTAKGGVIFSIADQFGIPIRYIGIGEGI-EDLRPFKADDFIEALFA 344
Cdd:PRK14723 335 EATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAFA 380
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-268 |
2.90e-12 |
|
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: 63.55 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 142 KPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVwgernrIPVVAQHTGADPASVIFDAIQSA 221
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2440851348 222 KAKGVDVLIADTAGRLQNKAHLMEELKKIV-RVMKKLDEEAPHEIMLT 268
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEElRLLLLLKSEKNLTVILT 122
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
126-333 |
8.58e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 65.76 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 126 SDILAGVDKplviedKKPYVILMVGVNGVGKTTTIGKLARQYQ-SEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVaq 204
Cdd:PRK12724 212 SDLFSGTGK------NQRKVVFFVGPTGSGKTTSIAKLAAKYFlHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFY-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 205 htgadPASVIFDAIQSAKAKGVDVLIADTAGRLQNKahlMEELKKIVRVMKKLDEEAPHEIMLTLDASTGQNAVSQAKLF 284
Cdd:PRK12724 284 -----PVKDIKKFKETLARDGSELILIDTAGYSHRN---LEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKA 355
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2440851348 285 NDAVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGIedlrPF 333
Cdd:PRK12724 356 YESLNYRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQEV----PF 400
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
140-328 |
1.49e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 64.00 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 140 DKKPYVILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHtgaDPASVIFDAIQ 219
Cdd:PRK06731 72 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 220 SAKAKGVDVLIADTAGRLQNKAHLMEELkkivrvMKKLDEEAPHEIMLTLDAS-TGQNAVSQAKLFNDaVGLTGITLTKL 298
Cdd:PRK06731 149 FKEEARVDYILIDTAGKNYRASETVEEM------IETMGQVEPDYICLTLSASmKSKDMIEIITNFKD-IHIDGIVFTKF 221
|
170 180 190
....*....|....*....|....*....|
gi 2440851348 299 DGTAKGGVIFSIADQFGIPIRYIGIGEGIE 328
Cdd:PRK06731 222 DETASSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
58-125 |
2.73e-11 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 58.63 E-value: 2.73e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2440851348 58 QNLGSGFLGLFTGKKIDDDLFDE----LEEQLLIADVGVDTTRKIIDNLTAHA-SRKELKDAEALYSKLREEM 125
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
145-329 |
6.54e-11 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 63.47 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQY--QSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVvaqHTgADPASVIFDAIQSAK 222
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAESLLDLLERLR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 223 AKGVdVLIaDTAGRLQNKAHLMEELK--KIVRVMKKLdeeapheimLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDG 300
Cdd:PRK12727 428 DYKL-VLI-DTAGMGQRDRALAAQLNwlRAARQVTSL---------LVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDE 496
|
170 180
....*....|....*....|....*....
gi 2440851348 301 TAKGGVIFSIADQFGIPIRYIGIGEGIED 329
Cdd:PRK12727 497 TGRFGSALSVVVDHQMPITWVTDGQRVPD 525
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
96-332 |
7.28e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 62.83 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 96 RKIIDNLTA---HASRKELKDAEALYsklREEMSD-ILAGVDKPLVIEDK----KPYVILMVGVNGVGKTTTIGKLARQY 167
Cdd:PRK12726 154 RGISDTYVAdfmQAGRKQFKQVETAH---LDDITDwFVPYLSGKLAVEDSfdlsNHRIISLIGQTGVGKTTTLVKLGWQL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 168 QSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADpasvIFDAIQSAK-AKGVDVLIADTAGRlqnkAHLMEE 246
Cdd:PRK12726 231 LKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVATSPAE----LEEAVQYMTyVNCVDHILIDTVGR----NYLAEE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 247 lkKIVRVMKKLDEEAPHEIMLTLDASTGQNAVSQAKLFNDAVGLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEG 326
Cdd:PRK12726 303 --SVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQN 380
|
....*...
gi 2440851348 327 IED--LRP 332
Cdd:PRK12726 381 ITEniFRP 388
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
81-329 |
3.17e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 60.89 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 81 LEEQLLIADVGVDTTRKIIDNLTAHASRKELkDAEALYSKlreemsDILAGVDKPLVIED---KKPYVILMVGVNGVGKT 157
Cdd:PRK14722 79 LTKYLFAAGFSAQLVRMIVDNLPEGEGYDTL-DAAADWAQ------SVLAANLPVLDSEDalmERGGVFALMGPTGVGKT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 158 TTIGKLARQ--YQSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASVIfdaiqsAKAKGVDVLIADTAG 235
Cdd:PRK14722 152 TTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLAL------AELRNKHMVLIDTIG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 236 RLQNKAHLMEELKKIvrvmkkLDEEAPHEIMLTLDASTGQNAVSQA-KLFNDAVG--------LTGITLTKLDGTAKGGV 306
Cdd:PRK14722 226 MSQRDRTVSDQIAML------HGADTPVQRLLLLNATSHGDTLNEVvQAYRSAAGqpkaalpdLAGCILTKLDEASNLGG 299
|
250 260
....*....|....*....|...
gi 2440851348 307 IFSIADQFGIPIRYIGIGEGIED 329
Cdd:PRK14722 300 VLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
137-327 |
7.93e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 59.53 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 137 VIEDKKPYVILMVGVNGVGKTTTIGKLARQY----QSEGKTVMLAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPAS 212
Cdd:PRK12723 168 IIDNLKKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 213 VIFDaiqsakAKGVDVLIADTAGRLQNKAHLMEELKKIVRVMKKldeeaPHEIMLTLDASTGQNAVSQAKLFNDAVGLTG 292
Cdd:PRK12723 248 EITQ------SKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGR-----DAEFHLAVSSTTKTSDVKEIFHQFSPFSYKT 316
|
170 180 190
....*....|....*....|....*....|....*
gi 2440851348 293 ITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGI 327
Cdd:PRK12723 317 VIFTKLDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
145-330 |
1.58e-05 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 46.48 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKL-ARQYQSEGKT-VMLAAGDTFRAAAVEQLQVWGernRIPVVAQHTGADPASVifdAIQSAK 222
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLaARAVIRHGADkVALLTTDSYRIGGHEQLRIYG---KLLGVSVRSIKDIADL---QLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 223 AKGVDVLIADTAGRLQNKAHLMEElkkiVRVMKKLDEEAPHEIMLtldastgqNAVSQAKLFNDAV------GLTGITLT 296
Cdd:PRK14721 267 LRGKHMVLIDTVGMSQRDQMLAEQ----IAMLSQCGTQVKHLLLL--------NATSSGDTLDEVIsayqghGIHGCIIT 334
|
170 180 190
....*....|....*....|....*....|....*
gi 2440851348 297 KLDGTAKGGVIFSIADQFGIPIRYIGIGEGI-EDL 330
Cdd:PRK14721 335 KVDEAASLGIALDAVIRRKLVLHYVTNGQKVpEDL 369
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
145-249 |
1.15e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 40.73 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAA--GdtfRAAAVeqLQvwgERNRIPV--VAQHTGADPASVIFDAIQS 220
Cdd:COG0507 142 VSVLTGGAGTGKTTTLRALLAALEALGLRVALAAptG---KAAKR--LS---ESTGIEArtIHRLLGLRPDSGRFRHNRD 213
|
90 100 110
....*....|....*....|....*....|.
gi 2440851348 221 AKAKGVDVLIADTAG--RLQNKAHLMEELKK 249
Cdd:COG0507 214 NPLTPADLLVVDEASmvDTRLMAALLEALPR 244
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
145-330 |
1.58e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 40.33 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYqsegktVM--------LAAGDTFRAAAVEQLQVWGERNRIPVVAQHTGADPASvifd 216
Cdd:PRK06995 258 VFALMGPTGVGKTTTTAKLAARC------VMrhgaskvaLLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADLRL---- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 217 AIQSAKAKGVdVLIaDTAGrlqnkahlmeelkkivrvMKKLDEEAPHEI-MLtldASTGQ--------NAVSQAKLFNDA 287
Cdd:PRK06995 328 ALSELRNKHI-VLI-DTIG------------------MSQRDRMVSEQIaML---HGAGApvkrllllNATSHGDTLNEV 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2440851348 288 V------GLTGITLTKLDGTAKGGVIFSIADQFGIPIRYIGIGEGI-EDL 330
Cdd:PRK06995 385 VqayrgpGLAGCILTKLDEAASLGGALDVVIRYKLPLHYVSNGQRVpEDL 434
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
145-187 |
1.89e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 38.30 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2440851348 145 VILMVGVNGVGKTTTIGKLARQYQSEGKTVMLAAgDTFRAAAV 187
Cdd:cd17933 14 VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR 55
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
145-217 |
4.37e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 37.29 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 145 VILMVGVNGVGKTTtigkLARQYQSEGKTVMLAAgDTFRAAAV-------EQLQVWGER--NRIPVVAQHTGADPASVIF 215
Cdd:pfam13671 1 LILLVGLPGSGKST----LARRLLEELGAVRLSS-DDERKRLFgegrpsiSYYTDATDRtyERLHELARIALRAGRPVIL 75
|
..
gi 2440851348 216 DA 217
Cdd:pfam13671 76 DA 77
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
289-329 |
4.44e-03 |
|
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.
Pssm-ID: 349762 Cd Length: 316 Bit Score: 38.63 E-value: 4.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2440851348 289 GLTGITLTKLDGTAKGGVIFsIADQFGIPIRYIGIGEGIED 329
Cdd:cd03108 274 GLTELALTKLDVNAQKYIER-IEELLGVPITYISVGPDREQ 313
|
|
| Peptidase_C15 |
cd00501 |
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ... |
138-236 |
5.69e-03 |
|
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.
Pssm-ID: 238279 Cd Length: 194 Bit Score: 37.63 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440851348 138 IEDKKPYVILMVGVNGVGKTTTIGKLARQYqsegktvmlaagDTFRAAAVEQLQVWGErnriPVVAQHTGADPASVIFDA 217
Cdd:cd00501 56 IEEHKPDLVIHVGLAGGRSTITIERVAINI------------DDARIPDNEGNQPIDE----PIVPGGPAAYFSTLPVKA 119
|
90 100
....*....|....*....|
gi 2440851348 218 I-QSAKAKGVDVLIADTAGR 236
Cdd:cd00501 120 IvKALREAGIPARVSNDAGT 139
|
|
| |
