| 133472 |
cd01949 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
true |
false |
true |
157 |
7e-47 |
183.56 |
99.36 |
4,303,1,67,371,68,49,422,117,13,436,130,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 304 DWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVkRSADFVARYGGE 383
cd01949 2 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSL-RESDLVARLGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 384 EFVVILPETTATGAGIVAANVMEAVAALELPHAGSPHkqVSVSVGIAYAHPDiGAEPSELVRSADRALYTAKRDGRNCVR 463
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFFIDGEEIR--VTASIGIAEYPED-GEDLEELLRRADKALYQAKRSGRNRVV 157
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
0 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
1e-45 |
179.36 |
100.00 |
4,300,0,73,374,73,46,420,120,15,436,135,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 301 VYVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVKRSaDFVARY 380
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRS-DLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 381 GGEEFVVILPETTATGAGIVAANVMEAVAALELPHAGSPH-KQVSVSVGIAYAHPDiGAEPSELVRSADRALYTAKRDGR 459
pfam00990 80 GGDEFAILLPDTSLEGAQELAERIRRLLAALKIPHTLSGLpLYVTISIGIAAYPND-GEDAEDLLKRADQALYQAKNQGR 158
|
..
gi 94970869 460 NC 461
pfam00990 159 NR 160
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
9e-45 |
176.37 |
98.18 |
3,301,2,69,371,71,64,436,135,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 302 YVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVkRSADFVARYG 381
TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV-RGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 382 GEEFVVILPETTATGAGIVAANVMEAVAALELPHAGSPHKQVSVSVGIAYAHPDiGAEPSELVRSADRALYTAKRDGRNC 461
TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAGRNR 160
|
....
gi 94970869 462 VRVA 465
TIGR00254 161 VVVA 164
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
9e-43 |
169.74 |
99.39 |
4,299,1,74,374,75,46,422,121,13,436,134,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 300 LVYVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVKRSaDFVAR 379
smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPG-DLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 380 YGGEEFVVILPETTATGAGIVAANVMEAVAALELPHAGSPHkqVSVSVGIAYAHPDiGAEPSELVRSADRALYTAKRDGR 459
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLY--LTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGR 157
|
....*.
gi 94970869 460 NCVRVA 465
smart00267 158 NQVAVY 163
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 32381 |
COG2199 |
COG2199 |
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms] |
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction... |
false |
false |
false |
181 |
8e-40 |
159.90 |
99.45 |
3,282,1,88,371,89,38,411,127,54 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 283 LAAVLGERDRLHERLTGLVYVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKL 362
COG2199 2 LLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 363 GSVMAASVkRSADFVARYGGEEFVVILPETTATGAGIVAANVMEAVAalELPHAGSPHKQVSVSVGIAYAHPDIGAEPSE 442
COG2199 82 ARRLRSNL-REGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALE--EPFFLGGEELRVTVSIGVALYPEDGSDDAEL 158
|
170 180
....*....|....*....|...
gi 94970869 443 LVRSADRALYTAKRDGRNCVRVA 465
COG2199 159 LLRRADLALYRAKRAGRNRVVVF 181
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 113982 |
pfam05231 |
MASE1 |
MASE1 |
MASE1 |
true |
false |
false |
298 |
2e-10 |
62.08 |
50.00 |
2,26,18,120,146,141,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 27 LTLTRGEDRVAAIWLSNGVLVVLLLSKGKTPTLPLVMIGFLANLLANRVAGDQWLQASSLAAINALEVVIAYALLTRRGR 106
pfam05231 19 LALALVSSGIAAIWLPTGLRLAALLLFGRRYWPGILLGDVLASLFLGLLSGLGLLLALLILLVNALEALLAVALLRRLLP 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94970869 107 EVDLRDPSGLGRFVLWGAIVAPLICSLLGTTVVVASRGGD---FQATLRVWFLADALGMAVIAPVLFVF 172
pfam05231 99 GRHRLQLLFWLRFLLAAAIIAALLLAIIGLALLLLLGLLPlapFAESWLTWWLGSATGVLVLAPLLLLL 167
|
|
cl01367 |
120595 |
MASE1 |
MASE1 |
MASE1 |
-1 |
| 33250 |
COG3447 |
COG3447 |
Predicted integral membrane sensor domain [Signal transduction mechanisms] |
Predicted integral membrane sensor domain [Signal transduction mechanisms] |
false |
false |
false |
308 |
2e-07 |
52.20 |
53.25 |
4,25,32,75,100,111,14,117,125,24,141,151,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 26 GLTLTRGEDRVAAIWLSNGVLVVLLLSKGKTPTLPLVMIGFLANLLANRVAGDQWLQASSLAAINALEVVIAYAL----L 101
COG3447 33 SLELSQFGTQLAPLWFPTSIMMGAFYRHAGRMWPGIALSCSLGNIAASILLFSTSSLNMAITTINILEAVVGAVLlrklL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 102 TRRGREVDLRDPSglgRFVLWGAIVAPLICSLLGTTVVVA--SRGGDFQATLRVWFLADALGMAVIAPVLFVFLKDHVLT 179
COG3447 113 PWYNPLQNLQDWL---RFLLGGAIVPPLLGAIIGSVLLVVlgTPGDDFSEAWFTWWLGDAIGILALAPLGIVIRPNWLRR 189
|
....*..
gi 94970869 180 ELFGREK 186
COG3447 190 HRLLRLQ 196
|
|
cl01367 |
120595 |
MASE1 |
MASE1 |
MASE1 |
-1 |
| 33501 |
COG3706 |
PleD |
Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal transduction mechanisms] |
Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal... |
false |
true |
false |
435 |
5e-39 |
157.00 |
38.85 |
4,294,263,76,371,339,45,416,385,21,438,406,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 295 ERLTGLVYVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVkRSA 374
COG3706 264 ERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTV-RGL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 375 DFVARYGGEEFVVILPETTATGAGIVAANVMEAVAALELPHA-GSPHKQVSVSVGIAYAHPDIGaEPSELVRSADRALYT 453
COG3706 343 DLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHElSREPLEVTISIGVAEGKPGED-SIEELLKRADKALYK 421
|
170
....*....|.
gi 94970869 454 AKRDGRNCVRV 464
COG3706 422 AKASGRNRVVV 432
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
4e-34 |
140.82 |
34.57 |
6,303,294,67,371,361,38,409,401,12,422,413,8,430,422,4,436,426,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 304 DWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVkRSADFVARYGGE 383
PRK09581 295 DGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNI-RGTDLIARYGGE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 384 EFVVILPETTATGAGIVAANVMEAVA--ALELPHAGSPHKqVSVSVGIA-YAHPdiGAEPSELVRSADRALYTAKRDGRN 460
PRK09581 374 EFVVVMPDTDIEVAIAVAERIRRKIAeePFAISDGKERLN-VTVSIGVAeLRPS--GESIEALIKRADKALYEAKNTGRN 450
|
..
gi 94970869 461 CV 462
PRK09581 451 RV 452
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
8e-31 |
130.21 |
57.68 |
5,293,122,29,324,151,46,371,197,47,419,244,15,436,259,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 294 HERLTGLVYVDWLTDLPNRRHFDMRFNSEwrRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVkRS 373
PRK09894 123 IYLLTIRSNMDVLTGLPGRRVLDESFDHQ--LRNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWT-RP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 374 ADFVARYGGEEFVVILPETTATGAGIVAANVMEAVAALELPHAGSpHKQVSVSVGIAYAHPdiGAEPSELVRSADRALYT 453
PRK09894 200 YETVYRYGGEEFIIILKAATDEEACRAGERIRQLIANQAITHSEG-RINITATFGVTRAFP--EEPLDEVIGRADRAMYE 276
|
170
....*....|....*
gi 94970869 454 AKRDGRNCVRVALEQ 468
PRK09894 277 GKQAGRNRVMFIDEQ 291
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
1e-23 |
106.13 |
48.25 |
5,279,191,13,295,204,75,371,279,43,416,322,21,438,343,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 280 SFPLAAVLGERDRlheRLTGLVYVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCL 359
PRK10245 192 SYQTATKLAEHKR---RLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 360 AKLGSVMAASVkRSADFVARYGGEEFVVILPETTATGAGIVAANVMEAVAALELPhaGSPHKQVSVSVGIAYAHPDIGaE 439
PRK10245 269 VALTRQLQITL-RGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP--NAPQVTLRISVGVAPLNPQMS-H 344
|
170 180
....*....|....*....|....*.
gi 94970869 440 PSELVRSADRALYTAKRDGRNCVRVA 465
PRK10245 345 YREWLKSADLALYKAKKAGRNRTEVA 370
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
6e-22 |
100.57 |
25.64 |
7,288,224,33,325,257,7,332,266,30,363,296,43,409,339,5,414,345,17,432,362,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 289 ERDRLHERLTGLVYVDWLTDLPNRRHFDMRFNSewrrAMRSRMP--ISLMMIDVDQFKEYNDAYGHMAGDRCLAKLgSVM 366
PRK10060 225 EERRAQERLRILANTDSITGLPNRNAIQELIDH----AIAQADNnqVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV-SLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 367 AASVKRSADFVARYGGEEFVVILPETTATGAGIVAANVMEavaALELP-HAGSPHKQVSVSVGIAYaHPDIGAEPSELVR 445
PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILT---RLRLPfRIGLIEVYTGCSIGIAL-SPEHGDDSESLIR 375
|
170
....*....|....*....
gi 94970869 446 SADRALYTAKRDGRNCVRV 464
PRK10060 376 SADTAMYTAKEGGRGQFCV 394
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
4e-19 |
91.31 |
14.16 |
4,303,690,67,371,757,50,422,807,8,431,815,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 304 DWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVkRSADFVARYGGE 383
PRK09776 691 DALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSML-RSSDVLARLGGD 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 384 EFVVILPETTATGAGIVAANVMEAVAALELPHAGSPHKqVSVSVGIAyAHPDIGAEPSELVRSADRALYTAKRDGRNCVR 463
PRK09776 770 EFGLLLPDCNVESARFIATRIISAINDYRFPWEGRVYR-VGASAGIT-AIDDNNHQASEVMSQADIACYAAKNAGRGRVT 847
|
.
gi 94970869 464 V 464
PRK09776 848 V 848
|
|
|
|
|
|
|
-1 |
| 34606 |
COG5001 |
COG5001 |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms] |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF... |
false |
true |
false |
663 |
4e-19 |
90.85 |
29.86 |
6,265,190,7,272,199,102,375,301,20,397,321,17,414,339,18,433,357,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 266 VLLLQAY--LACVVATSFPLAAVLGERDRLHERLTGLVYVDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQF 343
COG5001 191 VILLTNYreFSDMVQSQVTLTQRAEETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGF 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 344 KEYNDAYGHMAGDRCLAKLGSVMAASVKRSAdFVARYGGEEFVVILPETTATgaGIVAANVMEAVAALELP-HAGSPHKQ 422
COG5001 271 KPVNDAFGHATGDRLLIEVGRRLKAFDGAPI-LAARLGGDEFALIIPALEDD--ALRVAGARALCESLQAPyDLRGVRVQ 347
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 94970869 423 VSVSVGIAYAhPDIGAEPSELVRSADRALYTAKRDGRNCVRV 464
COG5001 348 VGASIGIAPF-PSGADTSEQLFERADYALYHAKQNGKGAAVL 388
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
4e-12 |
67.94 |
22.53 |
7,270,345,42,312,391,14,334,405,37,372,442,31,404,473,16,421,489,10,434,499,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 271 AYLACVVATSFPLAAVLGERDRLHERLTGLVYVDWLTDLPNR----RHFDMRFNSEWRRAmrsrmpisLMMIDVDQFKEY 346
PRK11359 346 AFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRnnlhNYLDDLVDKAVSPV--------VYLIGVDHIQDV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 347 NDAYGHMAGDRCLAKLGSVMAASVKrSADFVARYGGEEFVVILPETTATGAGIVAANvMEAVAALELPHAGSPHkQVSVS 426
PRK11359 418 IDSLGYAWADQALLEVVNRFREKLK-PDQYLCRIEGTQFVLVSLENDVSNITQIADE-LRNVVSKPIMIDDKPF-PLTLS 494
|
170 180 190
....*....|....*....|....*....|....
gi 94970869 427 VGIAYahpDIGAEPSELVRSADRALYTAKRDGRN 460
PRK11359 495 IGISY---DVGKNRDYLLSTAHNAMDYIRKNGGN 525
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
8e-11 |
63.57 |
14.07 |
6,25,34,18,43,54,21,66,75,31,98,106,5,103,113,26,132,139,52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 26 GLTLTRGEDRVAAIWLSN--GVLVVLLLSKGKTPTLPLVMIgfLANLLANRVAGDQWLQASSLAAINALEVVIAyALLTR 103
PRK09776 35 SLELSRFPTTLAPLWFPTaiMMVAFLRHPGRMWPGILLSCS--LGNIAANILLFSTSSLNLTWTTINLVEAVVG-AVLLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 104 --RGREVDLRDPSGLGRFVLWGAIVAPLicsLLGTTVVVASRGGDFQATLRVWFLADALGMAVIAPVLFVFLKDHVLTEL 181
PRK09776 112 klLPWYNPLQNLADWLRLALGSAIVPPL---LGGALVVLLTPGDDFLRAWLIWVLSEAIGMLALVPLGLLFKPHYLLRHR 188
|
...
gi 94970869 182 FGR 184
PRK09776 189 NPR 191
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
2e-07 |
52.33 |
37.59 |
8,289,245,12,310,257,10,321,267,42,370,309,6,376,321,13,389,336,24,414,360,3,420,363,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 290 RDRLHERLTGLVyvdwltdlpNRRHFDMRFNsEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGsvmaas 369
PRK09966 246 RTALHDPLTGLA---------NRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIA------ 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 370 vKRSADF------VARYGGEEFVVIL--PETTATGAGIVAANVMEAVAALELpHAGsphKQVSVSVGIAYAHPDIGAEPS 441
PRK09966 310 -KRLAEFgglrhkAYRLGGDEFAMVLydVQSESEVQQICSALTQIFNLPFDL-HNG---HQTTMTLSIGYAMTIEHASAE 384
|
170
....*....|....
gi 94970869 442 ELVRSADRALYTAK 455
PRK09966 385 KLQELADHNMYQAK 398
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
7e-07 |
50.65 |
24.14 |
5,302,229,75,377,305,42,419,351,1,426,352,8,436,360,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 303 VDWLTDLPNRRHFDMRFNSEWRRAMRSRMPISLMMIDVDQFKEYNDAYGHMAGDRCLAKLGSVMAASVKRSADFV-ARYG 381
PRK11059 230 LDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFELINLLSTFVQRYPGALlARYS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94970869 382 GEEFVVILPETTATGAGIVAANVMEAVAALELPHAGSP----HkqvsvsVGIAYAHPdiGAEPSELVRSADRALYTAKRD 457
PRK11059 310 RSDFAVLLPHRSLKEADSLASQLLKAVDSLPPPKMLDRddflH------IGIAAYRS--GQSTEQVMEEAEMALRSAQLQ 381
|
...
gi 94970869 458 GRN 460
PRK11059 382 GGN 384
|
|
|
|
|
|
|
-1 |
|