|
Name |
Accession |
Description |
Interval |
E-value |
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
1-428 |
0e+00 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 744.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 1 MFENLTDRLSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVKIVQA 80
Cdd:COG0541 1 MFENLSERLQGAFKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERALGEEVLKSLTPGQQVIKIVHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 81 ELESLMGAANEDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKeRKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFF 160
Cdd:COG0541 81 ELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLK-KKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 161 PSDLSQKPVDIANAAIKEAKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDAL 240
Cdd:COG0541 160 PEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQDAVNVAKAFNEAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 241 PLTGVILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILGMGDVLSLIEQAEATlDKDKADKLA 320
Cdd:COG0541 240 GLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMASRILGMGDVLSLIEKAQEA-IDEEEAEKL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 321 KKLKKGKGFDLEDFRDQLQQMKNMGGLGGLMDKLPNIGgvNLAQMGNAQgAAEKQFKQMEAIINSMTPAERRDPELISGS 400
Cdd:COG0541 319 AKKLKKGKFDLEDFLEQLQQMKKMGPLKKLLGMLPGMG--KLKQLKDLD-IDEKELKRIEAIINSMTPEERRNPDIINGS 395
|
410 420
....*....|....*....|....*...
gi 1785561338 401 RKRRIAMGSGTQVQDIGRLIKQHKQMQK 428
Cdd:COG0541 396 RKRRIAKGSGTTVQDVNRLLKQFEQMKK 423
|
|
| ffh |
TIGR00959 |
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the ... |
2-432 |
0e+00 |
|
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the protein component that forms the bacterial (and organellar) signal recognition particle together with a 4.5S RNA. Ffh is a GTPase homologous to eukaryotic SRP54 and also to the GTPase FtsY (TIGR00064) that is the receptor for the signal recognition particle. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273364 [Multi-domain] Cd Length: 428 Bit Score: 585.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 2 FENLTDRLSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVKIVQAE 81
Cdd:TIGR00959 1 FESLSERLQRIFKKLSGRGTITEKNIKEALREIRLALLEADVNLQVVKDFIKKVKEKALGQEVLKSLSPGQQFIKIVHEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 82 LESLMGAANEDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFP 161
Cdd:TIGR00959 81 LVAILGGENAELNLAKKPPTVILMVGLQGSGKTTTCGKLAYYLKKKQGKKVLLVACDLYRPAAIEQLKVLGQQVGVPVFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 162 SDLSQKPVDIANAAIKEAKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALP 241
Cdd:TIGR00959 161 LGKGQSPVEIARRALEYAKENGFDVVIVDTAGRLQIDEELMEELAAIKEILNPDEILLVVDAMTGQDAVNTAKTFNERLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 242 LTGVILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILGMGDVLSLIEQAEaTLDKDKADKLAK 321
Cdd:TIGR00959 241 LTGVVLTKLDGDARGGAALSVRSVTGKPIKFIGVGEKIDDLEPFHPERMASRILGMGDILSLVEKAQ-EVVDEEEAKKLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 322 KLKKGKGFDLEDFRDQLQQMKNMGGLGGLMDKLPNIGGVnLAQMGNAQgAAEKQFKQMEAIINSMTPAERRDPELISGSR 401
Cdd:TIGR00959 320 EKMKKGQFDLEDFLEQLRQIKKMGPLSSLLKMIPGMGGV-KPSLSDAD-LDEKQFKRIEAIISSMTPEERRNPKILNPSR 397
|
410 420 430
....*....|....*....|....*....|.
gi 1785561338 402 KRRIAMGSGTQVQDIGRLIKQHKQMQKMMKK 432
Cdd:TIGR00959 398 RKRIAAGSGTTVQDVNKLIKRFEQMKKMMKK 428
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
5-433 |
5.90e-155 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 446.58 E-value: 5.90e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 5 LTDRLSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVKIVQAELES 84
Cdd:PRK00771 1 LGESLRDALKKLAGKSRIDEKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGLTPREHVIKIVYEELVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 85 LMGAANEDLNLSAVPpAVVLMAGLQGAGKTTTAGKLARFLKeRKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDL 164
Cdd:PRK00771 81 LLGEETEPLVLPLKP-QTIMLVGLQGSGKTTTAAKLARYFK-KKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 165 SQKPVDIANAAIKEAKLKfiDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTG 244
Cdd:PRK00771 159 NKDAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAKAFHEAVGIGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 245 VILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILGMGDVLSLIEQAEATlDKDKADKLAKKLK 324
Cdd:PRK00771 237 IIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLLGMGDLESLLEKVEEA-LDEEEEEKDVEKM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 325 KGKGFDLEDFRDQLQQMKNMGGLGGLMDKLPNIGGvnlaQMGNAQ-GAAEKQFKQMEAIINSMTPAERRDPELISGSRKR 403
Cdd:PRK00771 316 MKGKFTLKDMYKQLEAMNKMGPLKQILQMLPGLGG----KLPDEAlEVTEEKLKKYKAIMDSMTEEELENPEIINASRIR 391
|
410 420 430
....*....|....*....|....*....|
gi 1785561338 404 RIAMGSGTQVQDIGRLIKQHKQMQKMMKKF 433
Cdd:PRK00771 392 RIARGSGTTVEDVRELLKYYKMMKKAMKQL 421
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
101-294 |
8.37e-113 |
|
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: 329.94 E-value: 8.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 101 AVVLMAGLQGAGKTTTAGKLARFLKeRKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAK 180
Cdd:cd18539 1 TVILLVGLQGSGKTTTAAKLALYLK-KKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 181 LKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAAL 260
Cdd:cd18539 80 EEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARGGAAL 159
|
170 180 190
....*....|....*....|....*....|....
gi 1785561338 261 SVRAITGKPIKFIGMGEKSEALEPFHPERIASRI 294
Cdd:cd18539 160 SIRHVTGKPIKFIGVGEKIEDLEPFHPDRMASRI 193
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
100-296 |
8.99e-106 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 312.04 E-value: 8.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 100 PAVVLMAGLQGAGKTTTAGKLARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEA 179
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 180 KLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAA 259
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGTAKGGAA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1785561338 260 LSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILG 296
Cdd:smart00962 161 LSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
102-294 |
3.69e-95 |
|
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: 284.82 E-value: 3.69e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLARFLKeRKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAKL 181
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLK-KKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 182 KFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAALS 261
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKGGAALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1785561338 262 VRAITGKPIKFIGMGEKSEALEPFHPERIASRI 294
Cdd:pfam00448 161 IVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
101-294 |
4.89e-89 |
|
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: 269.24 E-value: 4.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 101 AVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAK 180
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKK-VLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 181 LKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAAL 260
Cdd:cd03115 80 LEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAKGGAAL 159
|
170 180 190
....*....|....*....|....*....|....
gi 1785561338 261 SVRAITGKPIKFIGMGEKSEALEPFHPERIASRI 294
Cdd:cd03115 160 SIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
1-296 |
1.35e-80 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 251.48 E-value: 1.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 1 MFENLTDRLSQTLRH--------VTGKAKLTEDnikdTLREVRMALLEADVALPVVKDFVNSVKERAVGtevsRSLTPGQ 72
Cdd:COG0552 1 FFERLKEGLSKTRSGlgeklkslFSGKKKIDED----LLEELEELLIEADVGVETTEEIIEELRERVKR----KKLKDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 73 AFVKIVQAELESLMGAANEDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKErKKKSVMVVSADVYRPAAIKQLEMLA 152
Cdd:COG0552 73 ELKEALKEELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKA-EGKSVLLAAGDTFRAAAIEQLEVWG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 153 GEVGVTFFPSDLSQKPVDIANAAIKEAKLKFIDVVIVDTAGRLHIDEEMMGEI--------KALHAAinPVETLFVVDAM 224
Cdd:COG0552 152 ERVGVPVIAQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELkkikrvikKLDPDA--PHEVLLVLDAT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785561338 225 TGQDAANTAKAFGDALPLTGVILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILG 296
Cdd:COG0552 230 TGQNALSQAKVFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFG 301
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
4-429 |
8.35e-79 |
|
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: 251.29 E-value: 8.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 4 NLTDRLSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVKIVQAELE 83
Cdd:TIGR01425 4 QLGSSLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 84 SLMGAANEDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSD 163
Cdd:TIGR01425 84 NLVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFK-PALVCADTFRAGAFDQLKQNATKAGIPFYGSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 164 LSQKPVDIANAAIKEAKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLT 243
Cdd:TIGR01425 163 EESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVEVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 244 GVILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILGMGDVLSLIEQAEaTLDKDKADKLAKKL 323
Cdd:TIGR01425 243 SVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLGMGDLKGLIDKVQ-DLALNDEEKTLIEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 324 KKGKGFDLEDFRDQLQQMKNMGGLGGLMDKLPNIGGvNLAQMGNAQGAAEKqFKQMEAIINSMTPAERRDPELI---SGS 400
Cdd:TIGR01425 322 LKEGTFTLRDWYEQFQNLLKMGPLGNIMSMIPGLSH-PMMSKGNEEETSAK-IKVFMTIMDSMTDRELDSTAKTmlkDPS 399
|
410 420
....*....|....*....|....*....
gi 1785561338 401 RKRRIAMGSGTQVQDIGRLIKQHKQMQKM 429
Cdd:TIGR01425 400 RIRRVARGSGRDIREVNELLEQYKLFAQM 428
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
21-296 |
8.06e-71 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 227.55 E-value: 8.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 21 KLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVKIVQAELESLMGAAN----EDLNLS 96
Cdd:PRK14974 57 EIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSVGDlfdlIEEIKS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 97 AVPPAVVLMAGLQGAGKTTTAGKLARFLKERKKKSVMVvSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAI 176
Cdd:PRK14974 137 KGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIA-AGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 177 KEAKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARG 256
Cdd:PRK14974 216 EHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKG 295
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1785561338 257 GAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILG 296
Cdd:PRK14974 296 GAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
1-296 |
2.32e-69 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 223.05 E-value: 2.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 1 MFENLTDRLSQT-------LRHVTGKAKLTEDnikdTLREVRMALLEADVALPVVKDFVNSVKERAVGtevsRSLTPGQA 73
Cdd:PRK10416 16 WFERLKKGLSKTrenfgegINGLFAKKKIDED----LLEELEELLIEADVGVETTEEIIEELRERVKR----KNLKDPEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 74 FVKIVQAELESLMGAANEDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYRPAAIKQLEMLAG 153
Cdd:PRK10416 88 LKELLKEELAEILEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKK-VLLAAGDTFRAAAIEQLQVWGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 154 EVGVTFFpsdlSQK----PVDIANAAIKEAKLKFIDVVIVDTAGRLHIDEEMMGEI--------KALHAAinPVETLFVV 221
Cdd:PRK10416 167 RVGVPVI----AQKegadPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELkkikrvikKADPDA--PHEVLLVL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785561338 222 DAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRILG 296
Cdd:PRK10416 241 DATTGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLG 315
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
102-294 |
1.61e-64 |
|
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: 206.27 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLARFLKeRKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAKL 181
Cdd:cd17875 2 VIMFVGLQGSGKTTTAAKLAYYYQ-KKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 182 KFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAALS 261
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAKGGGALS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1785561338 262 VRAITGKPIKFIGMGEKSEALEPFHPERIASRI 294
Cdd:cd17875 161 AVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
25-295 |
5.32e-64 |
|
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: 207.88 E-value: 5.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 25 DNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVK-IVQAELESLMGAANEDLNLSAVPPAVV 103
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEyLKEILKEDLLKNTDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 104 LMAGLQGAGKTTTAGKLARFLKErKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAKLKF 183
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKK-QGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 184 IDVVIVDTAGRLHIDEEMMGEIKAL------HAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGG 257
Cdd:TIGR00064 160 IDVVLIDTAGRLQNKVNLMDELKKIkrvikkVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGG 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785561338 258 AALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRIL 295
Cdd:TIGR00064 240 IILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
101-294 |
3.67e-61 |
|
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: 197.79 E-value: 3.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 101 AVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAK 180
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKK-VVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 181 LKFIDVVIVDTAGRLHIDEEMMGEIKALHAAIN------PVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDA 254
Cdd:cd17874 80 ARGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKkkdpeaPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1785561338 255 RGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIASRI 294
Cdd:cd17874 160 KGGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP_SPB |
pfam02978 |
Signal peptide binding domain; |
329-428 |
2.60e-45 |
|
Signal peptide binding domain;
Pssm-ID: 460771 [Multi-domain] Cd Length: 95 Bit Score: 152.55 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 329 FDLEDFRDQLQQMKNMGGLGGLMDKLPNIGGVNlaqmgnAQGAAEKQFKQMEAIINSMTPAERRDPELISGSRKRRIAMG 408
Cdd:pfam02978 2 FTLRDFLEQLQQIKKMGPLSKILSMIPGMGKKD------DDIDSEKKLKRIEAIIDSMTPKERDNPDIINASRKRRIARG 75
|
90 100
....*....|....*....|
gi 1785561338 409 SGTQVQDIGRLIKQHKQMQK 428
Cdd:pfam02978 76 SGTSVQEVNRLLKQFKQMKK 95
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
3-296 |
1.24e-38 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 143.47 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 3 ENLTDRLSQTLRHVTGKAKLTEDNIKDTLREvrmaLLEADVALPVVKDFVNSVKERAvgtevsrsltPGQAFVKIVQAEL 82
Cdd:COG1419 84 AELKELLEEQLSGLAGESARLPPELAELLER----LLEAGVSPELARELLEKLPEDL----------SAEEAWRALLEAL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 83 ESLMGAANEDLNLsavPPAVVLMAGLQGAGKTTTAGKLARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFF-- 160
Cdd:COG1419 150 ARRLPVAEDPLLD---EGGVIALVGPTGVGKTTTIAKLAARFVLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEva 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 161 --PSDLSQkpvdianaAIkeAKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDA-MTGQDAANTAKAFG 237
Cdd:COG1419 227 ydPEELKE--------AL--ERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVLSAtTKYEDLKEIVEAFS 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 238 DaLPLTGVILTKVDGDARGGAALSVRAITGKPIKFIGMGEK-SEALEPFHPERIASRILG 296
Cdd:COG1419 297 S-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRvPEDIEVADPERLARLLLG 355
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
102-292 |
8.20e-35 |
|
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: 128.50 E-value: 8.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAKL 181
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLLSNGFR-VLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 182 KFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDAL----------PLTGVILTKVD 251
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGIVLTKFD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785561338 252 G-DARGGAALSVRAITGKPIKFIGMGEKSEALEPFHPERIAS 292
Cdd:cd17876 161 TiDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVN 202
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
102-294 |
6.05e-31 |
|
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: 117.65 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVtffpsdlsqkPVDIAN--AAIKEA 179
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGI----------PVEVAEdpEDLADA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 180 --KLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMT-GQDAANTAKAFGdALPLTGVILTKVDGDARG 256
Cdd:cd17873 72 leRLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIEVHLVLSATTkAKDLKEIIERFS-PLGYRGLILTKLDETTSL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1785561338 257 GAALSVRAITGKPIKFIGMGEK-SEALEPFHPERIASRI 294
Cdd:cd17873 151 GSVLSVLAESQLPVSYVTTGQRvPEDIEVASPLRLARLL 189
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
5-82 |
8.07e-21 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 85.98 E-value: 8.07e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785561338 5 LTDRLSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVsrsLTPGQAFVKIVQAEL 82
Cdd:pfam02881 1 LGEKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGEKK---LKPPQEVKKILKEEL 75
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
9-86 |
7.61e-20 |
|
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: 83.37 E-value: 7.61e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785561338 9 LSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGtEVSRSLTPGQAFVKIVQAELESLM 86
Cdd:smart00963 1 LSKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKG-EVLKGLTPKQEVKKILKEELVKIL 77
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
102-296 |
1.20e-18 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 87.64 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLA-RFLKERKKKSVMVVSADVYRPAAIKQL----EMLAGEVGVTFFPSDLSQkpvdianaAI 176
Cdd:PRK05703 223 VVALVGPTGVGKTTTLAKLAaRYALLYGKKKVALITLDTYRIGAVEQLktyaKIMGIPVEVVYDPKELAK--------AL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 177 KeaKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQ--DAANTAKAFGDaLPLTGVILTKVDGDA 254
Cdd:PRK05703 295 E--QLRDCDVILIDTAGRSQRDKRLIEELKALIEFSGEPIDVYLVLSATTKyeDLKDIYKHFSR-LPLDGLIFTKLDETS 371
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1785561338 255 RGGAALSVRAITGKPIKFIGMG-EKSEALEPFHPERIASRILG 296
Cdd:PRK05703 372 SLGSILSLLIESGLPISYLTNGqRVPDDIKVANPEELVRLLLG 414
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
85-300 |
1.52e-13 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 72.72 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 85 LMGAANEDLNLSAVPP----AVVLMAGLQGAGKTTTAGKLA-RFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTF 159
Cdd:PRK12727 331 MLGLLSKRLPVAPVDPlergGVIALVGPTGAGKTTTIAKLAqRFAAQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 160 FPSDLSQKPVDIANaaikeaKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAiNPVETLFVVDAMTG-QDAANTAKAFGD 238
Cdd:PRK12727 411 HEADSAESLLDLLE------RLRDYKLVLIDTAGMGQRDRALAAQLNWLRAA-RQVTSLLVLPANAHfSDLDEVVRRFAH 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785561338 239 ALPlTGVILTKVDGDARGGAALSVRAITGKPIKFIGMGEKSEalEPFHPERIASRILGMGDV 300
Cdd:PRK12727 484 AKP-QGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVP--DDLHRANAASLVLRLEDL 542
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
102-277 |
1.85e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 68.84 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKpvdianaaIKEAKL 181
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAAKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKDIKK--------FKETLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 182 K-FIDVVIVDTAGRLHIDEEMMGEIKALHAAI---NPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGG 257
Cdd:PRK12724 297 RdGSELILIDTAGYSHRNLEQLERMQSFYSCFgekDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEADFLG 376
|
170 180
....*....|....*....|
gi 1785561338 258 AALSVRAITGKPIKFIGMGE 277
Cdd:PRK12724 377 SFLELADTYSKSFTYLSVGQ 396
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
9-193 |
1.88e-12 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 67.36 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 9 LSQTLRHVTgkAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLtpgqafvkivQAELESLMGA 88
Cdd:TIGR03499 116 LRELLERLL--AGLAWLQRPPERAKLYERLLEAGVSEELARELLEKLPEDADAEDAWRWL----------REALEGMLPV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 89 ANEDLNLSAVPPAVVLMaGLQGAGKTTTAGKLA-RFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFfpsDLSQK 167
Cdd:TIGR03499 184 KPEEDPILEQGGVIALV-GPTGVGKTTTLAKLAaRFALEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPV---KVARD 259
|
170 180
....*....|....*....|....*.
gi 1785561338 168 PVDIANAAikeAKLKFIDVVIVDTAG 193
Cdd:TIGR03499 260 PKELREAL---DRLRDKDLILIDTAG 282
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
50-296 |
8.74e-12 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 66.68 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 50 DFVNSVKERAVG-TEVSRSLTPG-QAFVKIVQAELESLMG----------AANEDLNLSAvpPAVVLMAGLQGAGKTTTA 117
Cdd:PRK12726 146 DFVKFLKGRGISdTYVADFMQAGrKQFKQVETAHLDDITDwfvpylsgklAVEDSFDLSN--HRIISLIGQTGVGKTTTL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 118 GKLA-RFLKErkKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFpsdLSQKPVDIANAAIKEAKLKFIDVVIVDTAGRLH 196
Cdd:PRK12726 224 VKLGwQLLKQ--NRTVGFITTDTFRSGAVEQFQGYADKLDVELI---VATSPAELEEAVQYMTYVNCVDHILIDTVGRNY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 197 IDEEMMGEIKALHAAINPVETLFVVDA-MTGQDAANTAKAFGDaLPLTGVILTKVDGDARGGAALSVRAITGKPIKFIGM 275
Cdd:PRK12726 299 LAEESVSEISAYTDVVHPDLTCFTFSSgMKSADVMTILPKLAE-IPIDGFIITKMDETTRIGDLYTVMQETNLPVLYMTD 377
|
250 260
....*....|....*....|....
gi 1785561338 276 GEK-SEALepFHPER--IASRILG 296
Cdd:PRK12726 378 GQNiTENI--FRPKSrwLAERFVG 399
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
101-278 |
7.04e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 63.59 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 101 AVVLMAGLQGAGKTTTAGKLA-RFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDlsqkpvDIANAAIKEA 179
Cdd:PRK14722 138 GVFALMGPTGVGKTTTTAKLAaRCVMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVK------DGGDLQLALA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 180 KLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTA-----KAFGD---ALP-LTGVILTKV 250
Cdd:PRK14722 212 ELRNKHMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLNEVvqayrSAAGQpkaALPdLAGCILTKL 291
|
170 180
....*....|....*....|....*...
gi 1785561338 251 DGDARGGAALSVRAITGKPIKFIGMGEK 278
Cdd:PRK14722 292 DEASNLGGVLDTVIRYKLPVHYVSTGQK 319
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-212 |
5.37e-09 |
|
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: 54.69 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 99 PPAVVLMAGLQGAGKTTTAGKLARFLKeRKKKSVMVVSADVYRPAAIKQLEmlagevGVTFFPSDLSQKPVDIANAAIKE 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG-PPGGGVIYIDGEDILEEVLDQLL------LIIVGGKKASGSGELRLRLALAL 73
|
90 100 110
....*....|....*....|....*....|....
gi 1785561338 179 AKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAI 212
Cdd:smart00382 74 ARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
103-277 |
2.48e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 55.84 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 103 VLMAGLQGAGKTTTAGKLARFLkERKKKSVMVVSADVYRPAAIKQLEMLAGEVGvtffpsdlsQKPVDIANAAIKEAKLK 182
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQF-HGKKKTVGFITTDHSRIGTVQQLQDYVKTIG---------FEVIAVRDEAAMTRALT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 183 F------IDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDA-MTGQDAANTAKAFGDaLPLTGVILTKVDGDAR 255
Cdd:PRK11889 314 YfkeearVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSAsMKSKDMIEIITNFKD-IHIDGIVFTKFDETAS 392
|
170 180
....*....|....*....|..
gi 1785561338 256 GGAALSVRAITGKPIKFIGMGE 277
Cdd:PRK11889 393 SGELLKIPAVSSAPIVLMTDGQ 414
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
102-309 |
9.89e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 54.42 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKL-ARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVtffpsdlsqkPV----DIANAAI 176
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLaARCVAREGADQLALLTTDSFRIGALEQLRIYGRILGV----------PVhavkDAADLRF 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 177 KEAKLKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAAN-TAKAF--GDALPLTGVILTKVDGD 253
Cdd:PRK14723 257 ALAALGDKHLVLIDTVGMSQRDRNVSEQIAMLCGVGRPVRRLLLLNAASHGDTLNeVVHAYrhGAGEDVDGCIITKLDEA 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785561338 254 ARGGAALSVRAITGKPIKFIGMGEK-SEALEPFHPERIASRILGMGDVLSLIEQAEA 309
Cdd:PRK14723 337 THLGPALDTVIRHRLPVHYVSTGQKvPEHLELAQADELVDRAFATPRRGALFAPSEA 393
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
103-277 |
3.70e-07 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 51.29 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 103 VLMAGLQGAGKTTTAGKLArFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFPSDLSQKPVDIANAAIKEAKlk 182
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMA-WQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEEAR-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 183 fIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDA-MTGQDAANTAKAFGDaLPLTGVILTKVDGDARGGAALS 261
Cdd:PRK06731 155 -VDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSAsMKSKDMIEIITNFKD-IHIDGIVFTKFDETASSGELLK 232
|
170
....*....|....*.
gi 1785561338 262 VRAITGKPIKFIGMGE 277
Cdd:PRK06731 233 IPAVSSAPIVLMTDGQ 248
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
102-262 |
1.53e-06 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 50.33 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 102 VVLMAGLQGAGKTTTAGKL-ARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVtffpSDLSQKpvDIANAAIKEAK 180
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLaARAVIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGV----SVRSIK--DIADLQLMLHE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 181 LKFIDVVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAANTAKAFGDALPLTGVILTKVDGDARGGAAL 260
Cdd:PRK14721 267 LRGKHMVLIDTVGMSQRDQMLAEQIAMLSQCGTQVKHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAASLGIAL 346
|
..
gi 1785561338 261 SV 262
Cdd:PRK14721 347 DA 348
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
100-277 |
6.41e-06 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 48.36 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 100 PAVVLMAGLQGAGKTTTAGKLARFL---KERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVtffpsdlsqkPVDiANAAI 176
Cdd:PRK12723 174 KRVFILVGPTGVGKTTTIAKLAAIYginSDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGI----------PVK-AIESF 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 177 KEAK-----LKFIDVVIVDTAGRLHIDEEMMGEIKA-LHAAINPVETLFVVDAMTgqDAANTAKAFGDALPL--TGVILT 248
Cdd:PRK12723 243 KDLKeeitqSKDFDLVLVDTIGKSPKDFMKLAEMKElLNACGRDAEFHLAVSSTT--KTSDVKEIFHQFSPFsyKTVIFT 320
|
170 180
....*....|....*....|....*....
gi 1785561338 249 KVDGDARGGAALSVRAITGKPIKFIGMGE 277
Cdd:PRK12723 321 KLDETTCVGNLISLIYEMRKEVSYVTDGQ 349
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
104-262 |
1.49e-05 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 47.27 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 104 LMaGLQGAGKTTTAGKL-ARFLKERKKKSVMVVSADVYRPAAIKQLEMLAGEVGVTFFP----SDLSQkpvdianaAIKE 178
Cdd:PRK06995 261 LM-GPTGVGKTTTTAKLaARCVMRHGASKVALLTTDSYRIGGHEQLRIYGKILGVPVHAvkdaADLRL--------ALSE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 179 AKLKFIdvVIVDTAGRLHIDEEMMGEIKALHAAINPVETLFVVDAMTGQDAAN-TAKAFGDAlPLTGVILTKVDGDARGG 257
Cdd:PRK06995 332 LRNKHI--VLIDTIGMSQRDRMVSEQIAMLHGAGAPVKRLLLLNATSHGDTLNeVVQAYRGP-GLAGCILTKLDEAASLG 408
|
....*
gi 1785561338 258 AALSV 262
Cdd:PRK06995 409 GALDV 413
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
110-274 |
1.58e-05 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 46.18 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 110 GAGKTTTAGKLARFLKERKKKsVMVVSADV-------------YRPAAIKQLEMLAGEV--------------GVTFFPS 162
Cdd:pfam01656 9 GVGKTTLAANLARALARRGLR-VLLIDLDPqsnnssveglegdIAPALQALAEGLKGRVnldpillkeksdegGLDLIPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 163 DLS------QKPVDIANAAIKEAkLKFI----DVVIVDTAGRLHidEEMMGEIKALHAAINPV--ETLFVVDAM-TGQDA 229
Cdd:pfam01656 88 NIDlekfekELLGPRKEERLREA-LEALkedyDYVIIDGAPGLG--ELLRNALIAADYVIIPLepEVILVEDAKrLGGVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1785561338 230 ANTAKAFGDA-LPLTGVILTKVDGDARGGAALSVRAITGKPIKFIG 274
Cdd:pfam01656 165 AALVGGYALLgLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLG 210
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
100-249 |
2.87e-04 |
|
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: 40.11 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 100 PAVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADvyrpaaikqlemlagevgvtffpsdlsqkpvdianaaikea 179
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYK-VLLIDLD----------------------------------------- 38
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785561338 180 klkfiDVVIVDTAGRLHIDEEMMGeIKALHAAINPVETLFVVDAMTG--QDAANTAKA---FGDALPLTGVILTK 249
Cdd:cd01983 39 -----DYVLIDGGGGLETGLLLGT-IVALLALKKADEVIVVVDPELGslLEAVKLLLAlllLGIGIRPDGIVLNK 107
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
8-256 |
3.85e-04 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 42.10 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 8 RLSQTLRHVTGKAKLTEDNIKDTLREVRMALLEADVALPVVKDFVNSVKERAVGTEVSRSLTPGQAFVKIVQAELESLMG 87
Cdd:COG0489 1 ALLAALELLLLREEAQALLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLLLLLLLALALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 88 AANEDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYRPAAIKQL---------EMLAGEV--- 155
Cdd:COG0489 81 LLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKR-VLLIDADLRGPSLHRMLglenrpglsDVLAGEAsle 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 156 ---------GVTFFPS-DLSQKPVDIA-----NAAIKEAKLKFiDVVIVDTA-GRLHIDEEMMGEIKAlhaainpvETLF 219
Cdd:COG0489 160 dviqpteveGLDVLPAgPLPPNPSELLaskrlKQLLEELRGRY-DYVIIDTPpGLGVADATLLASLVD--------GVLL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1785561338 220 VVDA--MTGQDAANTAKAFGDA-LPLTGVILTKVDGDARG 256
Cdd:COG0489 231 VVRPgkTALDDVRKALEMLEKAgVPVLGVVLNMVCPKGER 270
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
91-142 |
4.59e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 41.19 E-value: 4.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1785561338 91 EDLNLSAVPPAVVLMAGLQGAGKTTTAGKLARFLKERkkKSVMVVSADVYRP 142
Cdd:pfam06414 2 DDKTTSQERPKAILLGGQPGAGKTELARALLDELGRQ--GNVVRIDPDDFRE 51
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
100-141 |
1.92e-03 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 39.30 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1785561338 100 PAVVLMAGLQGAGKTTTAGKLARFLKERKKKsVMVVSADVYR 141
Cdd:COG0529 16 GFVVWFTGLSGSGKSTLANALERRLFERGRH-VYLLDGDNVR 56
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
102-154 |
4.73e-03 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 37.62 E-value: 4.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1785561338 102 VVLMAGLQGAGKTTTAGKLARFLkerkkkSVMVVSADVYRPAAIKQLeMLAGE 154
Cdd:cd02021 1 IIVVMGVSGSGKSTVGKALAERL------GAPFIDGDDLHPPANIAK-MAAGI 46
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
100-141 |
5.81e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 37.30 E-value: 5.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1785561338 100 PAVVLMAGLQGAGKTTTAGKLARFLkERKKKSVMVVSADVYR 141
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKL-FEQGRSVYVLDGDNVR 42
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
99-141 |
6.06e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.12 E-value: 6.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1785561338 99 PPAVVLMAGLQGAGKTTTAGKLArflkerkkKSVMVVSADVYR 141
Cdd:COG4639 1 MLSLVVLIGLPGSGKSTFARRLF--------APTEVVSSDDIR 35
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
101-255 |
8.29e-03 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 37.92 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 101 AVVLMAGlqGAGKTTTAGKLARFLKERKKKsVMVVSADV---------YRPAAIKQ--LEMLAGEV------------GV 157
Cdd:COG1192 5 AVANQKG--GVGKTTTAVNLAAALARRGKR-VLLIDLDPqgnltsglgLDPDDLDPtlYDLLLDDApledaivpteipGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785561338 158 TFFPS--DLSQKPVDIANAAIKEAKLKFI--------DVVIVDTAGRLHIdeeMMgeIKALHAA---INPVET-LFVVDA 223
Cdd:COG1192 82 DLIPAniDLAGAEIELVSRPGRELRLKRAlapladdyDYILIDCPPSLGL---LT--LNALAAAdsvLIPVQPeYLSLEG 156
|
170 180 190
....*....|....*....|....*....|....
gi 1785561338 224 MTG--QDAANTAKAFGDALPLTGVILTKVDGDAR 255
Cdd:COG1192 157 LAQllETIEEVREDLNPKLEILGILLTMVDPRTR 190
|
|
| |
