|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
130-431 |
7.17e-167 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 471.51 E-value: 7.17e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 130 GLTKTRHRLRDRFNAFLAnFRSVDEEFFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKADVSRVIVQKMAEIYy 209
Cdd:PRK10416 23 GLSKTRENFGEGINGLFA-KKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEELKELLKEELAEIL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 210 qdsQNQDYHLNIDVQRPlNVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHA 289
Cdd:PRK10416 101 ---EPVEKPLNIEEKKP-FVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERVGVPVIAQK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 290 AGSDPASVVYDALQLAQQEHANVLLVDTAGRLQNNTNLMKELEKIKRIITREIPDAPHEVLLVIDATTGQNALVQAKQFQ 369
Cdd:PRK10416 177 EGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQNALSQAKAFH 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468566259 370 KATQVTGLVLAKLDGSSQGGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGLFSQLF 431
Cdd:PRK10416 257 EAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
130-429 |
1.58e-166 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 469.89 E-value: 1.58e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 130 GLTKTRHRLRDRFNAFLANFRSVDEEFFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKADVSRVIVQKMAEIYY 209
Cdd:COG0552 8 GLSKTRSGLGEKLKSLFSGKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKEELLEILD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 210 QDSQNqdyhLNIDVQRPlNVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHA 289
Cdd:COG0552 88 PVDKP----LAIEEKKP-FVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVIAQK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 290 AGSDPASVVYDALQLAQQEHANVLLVDTAGRLQNNTNLMKELEKIKRIITREIPDAPHEVLLVIDATTGQNALVQAKQFQ 369
Cdd:COG0552 163 EGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAKVFN 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 370 KATQVTGLVLAKLDGSSQGGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGLFSQ 429
Cdd:COG0552 243 EAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGE 302
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
152-427 |
6.99e-129 |
|
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: 373.52 E-value: 6.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 152 VDEEFFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKADVSRVIVQKMAEIYYQDS-QNQDYHLNIDVQRPlNVI 230
Cdd:TIGR00064 2 DDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlKNTDLELIVEENKP-NVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 231 LFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQEHA 310
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 311 NVLLVDTAGRLQNNTNLMKELEKIKRIITREIPDAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQGGI 390
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 2468566259 391 VLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGLF 427
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
228-426 |
2.59e-110 |
|
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: 322.98 E-value: 2.59e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQ 307
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 308 EHANVLLVDTAGRLQNNTNLMKELEKIKRIITREIPDAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQ 387
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468566259 388 GGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGL 426
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
228-427 |
3.62e-98 |
|
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: 292.01 E-value: 3.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLK-KDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQ 306
Cdd:smart00962 2 GVILLVGPNGVGKTTTIAKLAARLKlKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 307 QEHANVLLVDTAGRLQNNTNLMKELEKIKRIItreipdAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSS 386
Cdd:smart00962 82 ARGYDVVLIDTAGRLHNDENLMEELKKIKRVI------KPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468566259 387 QGGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGLF 427
Cdd:smart00962 156 KGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
228-426 |
2.50e-96 |
|
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: 287.13 E-value: 2.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQ 307
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 308 EHANVLLVDTAGRLQNNTNLMKELEKIKRIItreipdAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQ 387
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVV------APDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468566259 388 GGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGL 426
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
154-428 |
4.05e-81 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 253.74 E-value: 4.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 154 EEFFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKADVSRVIVQKMAE-IYYQDSQNQDYHLNIDVQ---RPLnV 229
Cdd:PRK14974 64 EDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEaLLEVLSVGDLFDLIEEIKskgKPV-V 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 230 ILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQEH 309
Cdd:PRK14974 143 IVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 310 ANVLLVDTAGRLQNNTNLMKELEKIKRIItreipdAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQGG 389
Cdd:PRK14974 223 IDVVLIDTAGRMHTDANLMDELKKIVRVT------KPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGG 296
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468566259 390 IVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGLFS 428
Cdd:PRK14974 297 AALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
228-426 |
1.78e-73 |
|
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: 228.80 E-value: 1.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQ 307
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 308 EHANVLLVDTAGRLQNNTNLMKELEKIKRIITreipdaPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQ 387
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEVES------PDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468566259 388 GGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGL 426
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
219-424 |
2.45e-73 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 236.07 E-value: 2.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 219 LNIDVQRPlNVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVV 298
Cdd:COG0541 93 LNLAKKPP-TVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 299 YDALQLAQQEHANVLLVDTAGRLQNNTNLMKELEKIKRIITreipdaPHEVLLVIDATTGQNALVQAKQFQKATQVTGLV 378
Cdd:COG0541 172 KRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2468566259 379 LAKLDGSSQGGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQ 424
Cdd:COG0541 246 LTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMAS 291
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
228-420 |
1.06e-66 |
|
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: 211.30 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQ 307
Cdd:cd18539 1 TVILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 308 EHANVLLVDTAGRLQNNTNLMKELEKIKRIITreipdaPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQ 387
Cdd:cd18539 81 EGFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDAR 154
|
170 180 190
....*....|....*....|....*....|...
gi 2468566259 388 GGIVLAINDELHLPVKLVGLGEQMDDLRDFDPE 420
Cdd:cd18539 155 GGAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
154-420 |
1.87e-58 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 197.74 E-value: 1.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 154 EEFFDDLEDLLIQSDVGYEMALKISDALR----NEVKLQNAQSKADVSRVIVQKMAEIYYQDSQnqdyhLNIDVQRPlNV 229
Cdd:PRK00771 24 KEVVKDIQRALLQADVNVKLVKELSKSIKeralEEEPPKGLTPREHVIKIVYEELVKLLGEETE-----PLVLPLKP-QT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 230 ILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQeh 309
Cdd:PRK00771 98 IMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKFKK-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 310 ANVLLVDTAGRLQNNTNLMKELEKIKRIItreipdAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQGG 389
Cdd:PRK00771 176 ADVIIVDTAGRHALEEDLIEEMKEIKEAV------KPDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGG 249
|
250 260 270
....*....|....*....|....*....|.
gi 2468566259 390 IVLAINDELHLPVKLVGLGEQMDDLRDFDPE 420
Cdd:PRK00771 250 GALSAVAETGAPIKFIGTGEKIDDLERFDPD 280
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
228-420 |
2.43e-54 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 179.31 E-value: 2.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQ 307
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 308 EHANVLLVDTAGRLQNNTNLMKELEKIKRIItreipdAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQ 387
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAV------KPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|...
gi 2468566259 388 GGIVLAINDELHLPVKLVGLGEQMDDLRDFDPE 420
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHIDDLEPFDPK 187
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
229-420 |
7.88e-43 |
|
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: 149.69 E-value: 7.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVYDALQLAQQE 308
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARDQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 309 HANVLLVDTAGRLQNNTNLMKELEKikrIITREIPDApheVLLVIDATTGQNALVQAKQFQKAtqvtglvLAKLDGSSQG 388
Cdd:cd17876 82 GFDVVLIDTAGRMQNNEPLMRALAK---LIKENNPDL---VLFVGEALVGNDAVDQLKKFNQA-------LADYSPSDNP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468566259 389 ----GIVLA----IND----------ELHLPVKLVGLGEQMDDLRDFDPE 420
Cdd:cd17876 149 rlidGIVLTkfdtIDDkvgaalsmvyATGQPIVFVGTGQTYTDLKKLNVK 198
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
146-426 |
2.24e-41 |
|
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: 151.91 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 146 LANFRSVDEE----FFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKADVSRVIVQKMAE--IYYQDSQNQDYHL 219
Cdd:TIGR01425 16 MSSATVIDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEelCNLVDPGVEAFTP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 220 NIDVQrplNVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPASVVY 299
Cdd:TIGR01425 96 KKGKT---CVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDPVKIAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 300 DALQLAQQEHANVLLVDTAGRLQNNTNLMKELEKIKRIITreipdaPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVL 379
Cdd:TIGR01425 173 EGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEVGSVII 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2468566259 380 AKLDGSSQGGIVLAINDELHLPVKLVGLGEQMDDLRDFDPEIYAQGL 426
Cdd:TIGR01425 247 TKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
146-427 |
7.46e-35 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 132.68 E-value: 7.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 146 LANFRSVDEEFFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQS--KADVSRVIVQKMAEIyyqdsqnqdyhlnIDV 223
Cdd:COG1419 97 LAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDLSAEEAWRalLEALARRLPVAEDPL-------------LDE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 224 QRplnVILFVGVNGAGKTTTIGKLAARLK-KDGQKVILAAADTFRAGAIEQLQVWGTKVGVqtvahaagsdPASVVYDA- 301
Cdd:COG1419 164 GG---VIALVGPTGVGKTTTIAKLAARFVlRGKKKVALITTDTYRIGAVEQLKTYARILGV----------PVEVAYDPe 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 302 -LQLAQQEHAN--VLLVDTAGRLQNNTNLMKELEKIKRiitreiPDAPHEVLLVIDATT-GQNALVQAKQFqKATQVTGL 377
Cdd:COG1419 231 eLKEALERLRDkdLVLIDTAGRSPRDPELIEELKALLD------AGPPIEVYLVLSATTkYEDLKEIVEAF-SSLGLDGL 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2468566259 378 VLAKLDGSSQGGIVLAINDELHLPVKLVGLGEQM-DDLRDFDPEIYAQGLF 427
Cdd:COG1419 304 ILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLL 354
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
34-402 |
8.05e-30 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 120.00 E-value: 8.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 34 TAAdsadtLDTPAKKSDTPNSKPTSDTSEPQEPQEQPTESTSiSDNPAPPATDSKSQTATPEQTSSTAETTTTTEEKEAN 113
Cdd:PRK05703 48 TAA-----VDEDETPKKNPVLREEKRKPAKSILSLQALLEKR-PSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 114 SQETGSIAADTAKnnpgLTKTRHRLRDRFNAFLANFRSVD--EEFFDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQ 191
Cdd:PRK05703 122 AAESKVVQKELDE----LRDELKELKNLLEDQLSGLRQVEriPPEFAELYKRLKRSGLSPEIAEKLLKLLLEHMPPRERT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 192 SKADVSRVIVqKMAEIYYQDSQNQDyhlnidvqrplNVILFVGVNGAGKTTTIGKLAAR--LKKDGQKVILAAADTFRAG 269
Cdd:PRK05703 198 AWRYLLELLA-NMIPVRVEDILKQG-----------GVVALVGPTGVGKTTTLAKLAARyaLLYGKKKVALITLDTYRIG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 270 AIEQLQVWGTKVGVqtvahaagsdPASVVYDA--LQLAQQEHAN--VLLVDTAGRLQNNTNLMKELEKIKriitrEIPDA 345
Cdd:PRK05703 266 AVEQLKTYAKIMGI----------PVEVVYDPkeLAKALEQLRDcdVILIDTAGRSQRDKRLIEELKALI-----EFSGE 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468566259 346 PHEVLLVIDATTGQNALVQA-KQFQKaTQVTGLVLAKLDGSSQGGIVLAINDELHLPV 402
Cdd:PRK05703 331 PIDVYLVLSATTKYEDLKDIyKHFSR-LPLDGLIFTKLDETSSLGSILSLLIESGLPI 387
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
229-420 |
1.23e-27 |
|
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: 108.41 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARLKKD-GQKVILAAADTFRAGAIEQLQVWGTKVGVqtvahaagsdPASVVYDALQLAQQ 307
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVLKkGKKVALITTDTYRIGAVEQLKTYAEIMGI----------PVEVAEDPEDLADA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 308 ----EHANVLLVDTAGRLQNNTNLMKELEKikrIITREIPDaphEVLLVIDATTGQNALVQ-AKQFqKATQVTGLVLAKL 382
Cdd:cd17873 72 lerlSDRDLILIDTAGRSPRDKEQLEELKE---LLGAGEDI---EVHLVLSATTKAKDLKEiIERF-SPLGYRGLILTKL 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468566259 383 DGSSQGGIVLAINDELHLPVKLVGLGEQM-DDLRDFDPE 420
Cdd:cd17873 145 DETTSLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPL 183
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
72-319 |
2.60e-18 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 84.69 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 72 ESTSISDNPAPPATDSKSQTATPEQTSSTAETTTTTEEKEANSQETGSIAADTAKNNpGLTKTRHRLRDRFNAFLANFRS 151
Cdd:TIGR03499 51 DEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEE-ELRKELEALRELLERLLAGLAW 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 152 VDEEF-FDDLEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKadVSRVIVQKMAEIYYQDsqnqdyhlniDVQRPLNVI 230
Cdd:TIGR03499 130 LQRPPeRAKLYERLLEAGVSEELARELLEKLPEDADAEDAWRW--LREALEGMLPVKPEED----------PILEQGGVI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 231 LFVGVNGAGKTTTIGKLAAR--LKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVqtvahaagsdPASVVYDA--LQLAQ 306
Cdd:TIGR03499 198 ALVGPTGVGKTTTLAKLAARfaLEHGKKKVALITTDTYRIGAVEQLKTYAEILGI----------PVKVARDPkeLREAL 267
|
250
....*....|....*
gi 2468566259 307 QEHAN--VLLVDTAG 319
Cdd:TIGR03499 268 DRLRDkdLILIDTAG 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
226-357 |
3.31e-15 |
|
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: 72.41 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 226 PLNVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQvwgtkvGVQTVAHAAGSDPASVVYDALQLA 305
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2468566259 306 QQEHANVLLVDTAGRLQNNTNLMKELEKIKRiiTREIPDAPHEVLLVIDATT 357
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEEL--RLLLLLKSEKNLTVILTTN 124
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
229-413 |
2.87e-14 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 73.99 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAAR--LKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDPasvvydALQLAQ 306
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDL------QLALAE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 307 QEHANVLLVDTAGRLQNNTNLMKELEKIKRiitreiPDAPHEVLLVIDATTGQNALVQAKQFQKAT---------QVTGL 377
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQIAMLHG------ADTPVQRLLLLNATSHGDTLNEVVQAYRSAagqpkaalpDLAGC 286
|
170 180 190
....*....|....*....|....*....|....*.
gi 2468566259 378 VLAKLDGSSQGGIVLAINDELHLPVKLVGLGEQMDD 413
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
229-414 |
3.26e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 71.56 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARL--KKDGQKVILAAADTFRAGAIEQLQVWGTKVGVqtVAHAAGSDPasvvyDALQLAQ 306
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGI--AVHEADSAE-----SLLDLLE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 307 Q-EHANVLLVDTAGRLQNNTNLMKELEKIKriitreipdAPHEV--LLVIDATTGQNALVQAKQFQKATQVTGLVLAKLD 383
Cdd:PRK12727 425 RlRDYKLVLIDTAGMGQRDRALAAQLNWLR---------AARQVtsLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLD 495
|
170 180 190
....*....|....*....|....*....|..
gi 2468566259 384 GSSQGGIVLAINDELHLPVKLVGLGEQM-DDL 414
Cdd:PRK12727 496 ETGRFGSALSVVVDHQMPITWVTDGQRVpDDL 527
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
229-410 |
5.71e-13 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 70.99 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAAR--LKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVqtvahaagsdPASVVYDA--LQL 304
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARcvAREGADQLALLTTDSFRIGALEQLRIYGRILGV----------PVHAVKDAadLRF 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 305 AQQEHAN--VLLVDTAGRLQNNTNLMKELEKIKRIitreipDAPHEVLLVIDATTGQNAL---VQAKQFQKATQVTGLVL 379
Cdd:PRK14723 257 ALAALGDkhLVLIDTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLLNAASHGDTLnevVHAYRHGAGEDVDGCII 330
|
170 180 190
....*....|....*....|....*....|.
gi 2468566259 380 AKLDGSSQGGIVLAINDELHLPVKLVGLGEQ 410
Cdd:PRK14723 331 TKLDEATHLGPALDTVIRHRLPVHYVSTGQK 361
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
163-432 |
3.00e-11 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 65.09 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 163 LLIQSDVgyEMALKISDALRNEVKLQNAQ--SKADVSRVIVQKMAEIYYQDsqnqdyhlNIdVQRPLNVILFVGVNGAGK 240
Cdd:PRK11889 186 MLEQNDV--EQYFIHAYAEKLKVKFENATmiTEEEVIEYILEDMRSHFNTE--------NV-FEKEVQTIALIGPTGVGK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 241 TTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHaagSDPASVVYDALQLAQQEHANVLLVDTAGR 320
Cdd:PRK11889 255 TTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAV---RDEAAMTRALTYFKEEARVDYILIDTAGK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 321 LQNNTNLMKEL-EKIKRIitreipdAPHEVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQGGIVLAINDELH 399
Cdd:PRK11889 332 NYRASETVEEMiETMGQV-------EPDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSS 404
|
250 260 270
....*....|....*....|....*....|....*.
gi 2468566259 400 LPVKLvglgeqMDDLRDFDPEIY---AQGLFSQLFQ 432
Cdd:PRK11889 405 APIVL------MTDGQDVKKNIHiatAEHLAKQMLQ 434
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
138-208 |
2.17e-10 |
|
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: 56.41 E-value: 2.17e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468566259 138 LRDRFNAFLANFRS---VDEEFFDDLEDLLIQSDVGYEMALKISDALRNEVK---LQNAQSKADVSRVIVQKMAEIY 208
Cdd:smart00963 1 LSKALGKLLGELFLtekDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKgevLKGLTPKQEVKKILKEELVKIL 77
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
229-411 |
3.57e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 61.52 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARLK-KDGQKVILAAADTFRAGAIEQLQVWGTKVGVqtvahaagsdPASVVYDALQLAQ- 306
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAAKYFlHMGKSVSLYTTDNYRIAAIEQLKRYADTMGM----------PFYPVKDIKKFKEt 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 307 --QEHANVLLVDTAGRLQNNtnlMKELEKIKRIITREIPDAPHEVLLVIDATTG-QNALVQAKQFQkATQVTGLVLAKLD 383
Cdd:PRK12724 295 laRDGSELILIDTAGYSHRN---LEQLERMQSFYSCFGEKDSVENLLVLSSTSSyHHTLTVLKAYE-SLNYRRILLTKLD 370
|
170 180
....*....|....*....|....*...
gi 2468566259 384 GSSQGGIVLAINDELHLPVKLVGLGEQM 411
Cdd:PRK12724 371 EADFLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
163-432 |
8.42e-10 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 59.37 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 163 LLIQSDVGYEMALKISDALRneVKLQNAQskadvsrVIVQKMAEIYYQDSQNqdyHLNID--VQRPLNVILFVGVNGAGK 240
Cdd:PRK06731 21 MLEQNDVEQYFIHAYAEKLK--VKFENAT-------MITEEVIEYILEDMSS---HFNTEnvFEKEVQTIALIGPTGVGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 241 TTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHaagSDPASVVYDALQLAQQEHANVLLVDTAGR 320
Cdd:PRK06731 89 TTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAV---RDEAAMTRALTYFKEEARVDYILIDTAGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 321 lqnNTNLMKELEKIKRIITREIPDApheVLLVIDATTGQNALVQAKQFQKATQVTGLVLAKLDGSSQGGIVLAINDELHL 400
Cdd:PRK06731 166 ---NYRASETVEEMIETMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSA 239
|
250 260 270
....*....|....*....|....*....|....*
gi 2468566259 401 PVKLvglgeqMDDLRDFDPEIY---AQGLFSQLFQ 432
Cdd:PRK06731 240 PIVL------MTDGQDVKKNIHiatAEHLAKQMLQ 268
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
229-413 |
1.40e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 59.75 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVahaAGSDPASVVYDALQLAQQE 308
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELI---VATSPAELEEAVQYMTYVN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 309 HANVLLVDTAGRlqnntNLMKElEKIKRIitREIPDAPHEVLLVIDATTGQNALVQAKQFQKATQ--VTGLVLAKLDGSS 386
Cdd:PRK12726 285 CVDHILIDTVGR-----NYLAE-ESVSEI--SAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEipIDGFIITKMDETT 356
|
170 180
....*....|....*....|....*..
gi 2468566259 387 QGGIVLAINDELHLPVKLVGLGEQMDD 413
Cdd:PRK12726 357 RIGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
233-319 |
8.37e-09 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 57.28 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 233 VGVNGAGKTTTIGKLAAR--LKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVqTVaHAagsdpasvVYDA--LQLAQQE 308
Cdd:PRK06995 262 MGPTGVGKTTTTAKLAARcvMRHGASKVALLTTDSYRIGGHEQLRIYGKILGV-PV-HA--------VKDAadLRLALSE 331
|
90
....*....|...
gi 2468566259 309 --HANVLLVDTAG 319
Cdd:PRK06995 332 lrNKHIVLIDTIG 344
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
229-392 |
2.99e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 55.34 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAAR--LKKDGQKVILAAADTFRAGAIEQLQVWGTKVGVQTVAHAAGSDpasvvydaLQLAQ 306
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIAD--------LQLML 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 307 QE--HANVLLVDTAGRLQNNTNLMKEL-------EKIKRiitreipdaphevLLVIDATTGQNALVQAKQFQKATQVTGL 377
Cdd:PRK14721 265 HElrGKHMVLIDTVGMSQRDQMLAEQIamlsqcgTQVKH-------------LLLLNATSSGDTLDEVISAYQGHGIHGC 331
|
170
....*....|....*
gi 2468566259 378 VLAKLDGSSQGGIVL 392
Cdd:PRK14721 332 IITKVDEAASLGIAL 346
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
138-204 |
4.16e-08 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 50.16 E-value: 4.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468566259 138 LRDRFNAFLANFRS---VDEEFFDD----LEDLLIQSDVGYEMALKISDALR-NEVKLQNAQSKADVSRVIVQKM 204
Cdd:pfam02881 1 LGEKLSSLFKGLRGkgkIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLReKAVGEKKLKPPQEVKKILKEEL 75
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
160-409 |
9.75e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 50.67 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 160 LEDLLIQSDVGYEMALKISDALRNEVKLQNAQSKADV-SRVIVQKMAEIYYQDSQnqdyhlnIDVQRPlNVILFVGVNGA 238
Cdd:PRK12723 114 IEDILRENDFSESYIKDINEFIKKEFSLSDLDDYDKVrDSVIIYIAKTIKCSGSI-------IDNLKK-RVFILVGPTGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 239 GKTTTIGKLAARL---KKDGQKVI-LAAADTFRAGAIEQLQVWGTKVGVqtvahaagsdPASVV--YDAL--QLAQQEHA 310
Cdd:PRK12723 186 GKTTTIAKLAAIYginSDDKSLNIkIITIDNYRIGAKKQIQTYGDIMGI----------PVKAIesFKDLkeEITQSKDF 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 311 NVLLVDTAGRlqNNTNLMKeLEKIKRIITREIPDAphEVLLVIDATTG----QNALVQAKQFQKATqvtgLVLAKLDGSS 386
Cdd:PRK12723 256 DLVLVDTIGK--SPKDFMK-LAEMKELLNACGRDA--EFHLAVSSTTKtsdvKEIFHQFSPFSYKT----VIFTKLDETT 326
|
250 260
....*....|....*....|...
gi 2468566259 387 QGGIVLAINDELHLPVKLVGLGE 409
Cdd:PRK12723 327 CVGNLISLIYEMRKEVSYVTDGQ 349
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
228-339 |
4.78e-05 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 42.42 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVG-VNGAGKTTTIGKLAARLKKDGQKVILAAADTFragaieqlqvwgtkVGVQTVAHAagSDPASVVYDALQLAQ 306
Cdd:cd01983 1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY--------------VLIDGGGGL--ETGLLLGTIVALLAL 64
|
90 100 110
....*....|....*....|....*....|....*
gi 2468566259 307 QEHANVLLV--DTAGRLQNNTNLMKELEKIKRIIT 339
Cdd:cd01983 65 KKADEVIVVvdPELGSLLEAVKLLLALLLLGIGIR 99
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
230-260 |
2.04e-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: 42.26 E-value: 2.04e-04
10 20 30
....*....|....*....|....*....|.
gi 2468566259 230 ILFVGVNGAGKTTTIGKLAARLKKDGQKVIL 260
Cdd:cd01672 3 IVFEGIDGAGKTTLIELLAERLEARGYEVVL 33
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
218-260 |
1.93e-03 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 38.92 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2468566259 218 HLNIDVQRPlNVILFVGVNGAGKTTTIGKLAARLKKDGQKVIL 260
Cdd:cd03230 18 DISLTVEKG-EIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV 59
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
13-94 |
1.97e-03 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 40.48 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 13 TAAQTEASPQAAPdkdSDQPATAADSADTLDTPAKKSDTPNSKPTSDTSEPQEPQEQPTESTSISDNPAPPATDSKSQTA 92
Cdd:PHA03269 34 SAATQKPDPAPAP---HQAASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKP 110
|
..
gi 2468566259 93 TP 94
Cdd:PHA03269 111 DA 112
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
5-96 |
2.48e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 39.96 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 5 DIFKKKTNTAAQTEASPQAAPDKDSDQPATAADSADTL-----DTPAKKSDTPNSKPTSDTSEPQEPQEQPTESTSISDN 79
Cdd:PRK13108 335 AEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEreqpgDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEP 414
|
90
....*....|....*..
gi 2468566259 80 PAPPATDSKSQTATPEQ 96
Cdd:PRK13108 415 EVPEKAAPIPDPAKPDE 431
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
237-262 |
2.57e-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: 39.96 E-value: 2.57e-03
10 20
....*....|....*....|....*.
gi 2468566259 237 GAGKTTTIGKLAARLKKDGQKVILAA 262
Cdd:COG0507 150 GTGKTTTLRALLAALEALGLRVALAA 175
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
229-269 |
2.78e-03 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 38.23 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAADTFRAG 269
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHG 41
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
228-338 |
3.00e-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: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 228 NVILFVGVNGAGKTTTIGKLAARLKKDGQKVILAAAdTFRAgAIEQLQVwgTKVGVQTVAHAAGSDP--ASVVYDALQLA 305
Cdd:cd17933 13 RVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAP-TGKA-AKRLSES--TGIEASTIHRLLGINPggGGFYYNEENPL 88
|
90 100 110
....*....|....*....|....*....|....*
gi 2468566259 306 QqehANVLLVDTAGRLQNNT--NLMKELEKIKRII 338
Cdd:cd17933 89 D---ADLLIVDEASMVDTRLmaALLSAIPAGARLI 120
|
|
| Metaviral_G |
pfam09595 |
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
11-95 |
3.35e-03 |
|
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.
Pssm-ID: 462833 [Multi-domain] Cd Length: 183 Bit Score: 38.40 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 11 TNTAAQTEASPQAAPDKDSDQPATAADSADTLD----------TPAKKSDTPN--SKPTSDTSEPQEPQ--------EQP 70
Cdd:pfam09595 73 AAKEAPSESEDAPDIDPNNQHPSQDRSEAPPLEpaaktkpsehEPANPPDASNrlSPPDASTAAIREARtfrkpstgKRN 152
|
90 100
....*....|....*....|....*
gi 2468566259 71 TESTSISDNPAPPATDSKSQTATPE 95
Cdd:pfam09595 153 NPSSAQSDQSPPRANHEAIGRANPF 177
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
13-138 |
4.50e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 39.51 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 13 TAAQTEASPQAAP-DKDSDQPA---TAADSADTLDTPAKKSDTPN-SKPTSDTSEPQEPQEQPTESTSisdNPAPPATDS 87
Cdd:pfam05109 482 TSGASPVTPSPSPrDNGTESKApdmTSPTSAVTTPTPNATSPTPAvTTPTPNATSPTLGKTSPTSAVT---TPTPNATSP 558
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2468566259 88 KSQTATPEQTSSTAETTTTTEEKEANSQETGSIAADTAKNNPGLTKTRHRL 138
Cdd:pfam05109 559 TPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTL 609
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
218-316 |
5.87e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 38.02 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468566259 218 HLNIDVqRPLNVILFVGVNGAGKTTTIGKLAARLK-KDGQKVILAAADTF--RAGAIEQLQVWGTKVGVQTVAHAAG-SD 293
Cdd:COG2401 48 DLNLEI-EPGEIVLIVGASGSGKSTLLRLLAGALKgTPVAGCVDVPDNQFgrEASLIDAIGRKGDFKDAVELLNAVGlSD 126
|
90 100 110
....*....|....*....|....*....|....*
gi 2468566259 294 PASVV--YDALQLAQQ----------EHANVLLVD 316
Cdd:COG2401 127 AVLWLrrFKELSTGQKfrfrlalllaERPKLLVID 161
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
229-258 |
8.39e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 37.08 E-value: 8.39e-03
10 20 30
....*....|....*....|....*....|
gi 2468566259 229 VILFVGVNGAGKTTTIGKLAARLKKDGQKV 258
Cdd:COG1763 3 VLGIVGYSGSGKTTLLEKLIPELKARGLRV 32
|
|
| Tmk |
COG0125 |
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ... |
230-260 |
8.58e-03 |
|
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 439895 [Multi-domain] Cd Length: 206 Bit Score: 37.44 E-value: 8.58e-03
10 20 30
....*....|....*....|....*....|.
gi 2468566259 230 ILFVGVNGAGKTTTIGKLAARLKKDGQKVIL 260
Cdd:COG0125 6 IVFEGIDGSGKSTQIKLLAEYLEARGYDVVL 36
|
|
| |
