| 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 |
1e-54 |
208.98 |
100.00 |
2,196,0,118,317,118,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 197 TDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYGGE 276
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 277 EFVIVLPETNTTGAMQVANRIRRGVEQAKFFAGSPRQVerlTISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRNQVV 356
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFFIDGEEIRV---TASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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 |
4e-49 |
190.53 |
100.00 |
3,194,0,112,306,113,9,316,122,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 195 AFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYG 274
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 275 GEEFVIVLPETNTTGAMQVANRIRRGVEQAKF-FAGSPRQVErLTISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRN 353
pfam00990 81 GDEFAILLPDTSLEGAQELAERIRRLLAALKIpHTLSGLPLY-VTISIGIAAYPNDGEDAEDLLKRADQALYQAKNQGRN 159
|
.
gi 94971157 354 Q 354
pfam00990 160 R 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 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
2e-47 |
185.14 |
98.77 |
2,194,2,120,317,122,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 195 AFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYG 274
smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 275 GEEFVIVLPETNTTGAMQVANRIRRGVEQAKFFAGSPRQVerlTISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRNQ 354
smart00267 83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYL---TISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 94971157 355 VVTH 358
smart00267 160 VAVY 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 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
6e-45 |
176.37 |
97.58 |
2,194,1,109,304,110,52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 195 AFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYG 274
TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 275 GEEFVIVLPETNTTGAMQVANRIRRGVEQaKFFAGSPRQVERLTISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRNQ 354
TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINS-KPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
..
gi 94971157 355 VV 356
TIGR00254 161 VV 162
|
|
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 |
1e-40 |
161.82 |
99.45 |
3,176,1,133,312,134,14,326,149,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 177 VAENQLTRDYENEGLIKFAFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDV 256
COG2199 2 LLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 257 SAVLMKDLREVDTAARYGGEEFVIVLPETNTTGAMQVANRIRRGVEQAKFFAGsprQVERLTISIGIAIY-DQDAQSKRE 335
COG2199 82 ARRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFFLGG---EELRVTVSIGVALYpEDGSDDAEL 158
|
170 180
....*....|....*....|...
gi 94971157 336 LIEAADAALYQAKGQGRNQVVTH 358
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 |
| 128379 |
smart00065 |
GAF |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
true |
false |
false |
149 |
0.001 |
39.67 |
88.59 |
5,49,0,32,81,33,14,95,48,31,126,82,34,160,117,15 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 50 QLEATLNMLLDFAAEISFFEKSLVYFWEEDSE-QVKLRLAGGMDRET-AEPFVRGNIFNFWATRFGRPLLVTAGHNLLS- 126
smart00065 1 DLEELLQTILEELRQLLGADRVLIYLVDEDDRgELVLVAADGLTLPLlGLRYPLGEGLAGRVAETGRPLNIPDVEADPVf 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 94971157 127 --DAALESLGARSALIVPLVVSNKVIGSMQLFSAEH-ESFTREDAQLFWMLT 175
smart00065 81 alDLLGRYQGVRSFLAVPLVADGELVGVLALHNKDSpRPFTEEDEELLQALA 132
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 110584 |
pfam01590 |
GAF |
GAF domain |
GAF domain |
false |
false |
false |
153 |
0.003 |
38.38 |
99.35 |
4,50,1,46,96,60,14,110,78,19,129,100,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 51 LEATLNMLLDFAAEISFFEKSLVYFWEEDSEQVKLRLAGGMDRETA-------------EPFVRGNIFNFWAT----RFG 113
pfam01590 2 LEELLQTILEELRELLGADRCAILLADADGLLLYLVAGDGLSDIPLaarglplgggvvgEVIAGGNPIVVPDVqddpRFR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94971157 114 RPLLVTAGHNLLSDAA---LESLGARSALIVPLVVSNKVIGSMQLFSAEHESFTREDAQLFWMLTLVAENQL 182
pfam01590 82 DLTALAEELPAPVGCHehyLRGLGIRSCLAVPLLGGGKLIGVLVLHSTSPRAFTEEELELLQALADQVAIAL 153
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
1e-47 |
185.51 |
36.76 |
3,191,288,115,306,404,9,316,413,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 192 IKFAFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAA 271
PRK09581 289 IEMAVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIA 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 272 RYGGEEFVIVLPETNTTGAMQVANRIRRGVEQAKF-FAGSPRQVErLTISIGIAIYDQDAQSKRELIEAADAALYQAKGQ 350
PRK09581 369 RYGGEEFVVVMPDTDIEVAIAVAERIRRKIAEEPFaISDGKERLN-VTVSIGVAELRPSGESIEALIKRADKALYEAKNT 447
|
....*....
gi 94971157 351 GRNQVVTHA 359
PRK09581 448 GRNRVVALA 456
|
|
|
|
|
|
|
-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 |
2e-43 |
171.64 |
42.99 |
2,174,247,13,187,262,172 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 175 TLVAENQLTRDYE--NEGLIKFAFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQV 252
COG3706 248 RQLRRKRYERQLResLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 253 LRDVSAVLMKDLREVDTAARYGGEEFVIVLPETNTTGAMQVANRIRRGVEQAKFFAGSPRQVERLTISIGIAIYDQDAQS 332
COG3706 328 LRQVARRLRQTVRGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHELSREPLEVTISIGVAEGKPGEDS 407
|
170 180
....*....|....*....|....*..
gi 94971157 333 KRELIEAADAALYQAKGQGRNQVVTHA 359
COG3706 408 IEELLKRADKALYKAKASGRNRVVVKR 434
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
9e-32 |
132.53 |
57.34 |
6,183,118,23,206,142,4,213,146,88,301,235,13,317,248,12,330,260,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 184 RDYENEGLIKFAFTDFLTGLKTR-GYFEqqlELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMK 262
PRK09894 119 TDYKIYLLTIRSNMDVLTGLPGRrVLDE---SFDHQLRNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLAS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 263 DLREVDTAARYGGEEFVIVLPETNTTGAMQVANRIRRGV-EQAKFFAGSPRQVerlTISIGIAIYDQDaQSKRELIEAAD 341
PRK09894 196 WTRPYETVYRYGGEEFIIILKAATDEEACRAGERIRQLIaNQAITHSEGRINI---TATFGVTRAFPE-EPLDEVIGRAD 271
|
170
....*....|....*
gi 94971157 342 AALYQAKGQGRNQVV 356
PRK09894 272 RAMYEGKQAGRNRVM 286
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
5e-25 |
110.18 |
14.25 |
2,194,687,116,312,803,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 195 AFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYG 274
PRK09776 688 ASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 275 GEEFVIVLPETNTTGAMQVANRIRRGVEQAKFFAGSprQVERLTISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRNQ 354
PRK09776 768 GDEFGLLLPDCNVESARFIATRIISAINDYRFPWEG--RVYRVGASAGITAIDDNNHQASEVMSQADIACYAAKNAGRGR 845
|
.
gi 94971157 355 V 355
PRK09776 846 V 846
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
9e-23 |
102.89 |
24.28 |
7,188,230,29,219,259,59,279,318,13,292,332,12,305,344,4,312,348,6,318,355,36 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 189 EGLIKFAFTDFLTGLKTRGYFEQQLELEIkrAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVD 268
PRK10060 231 ERLRILANTDSITGLPNRNAIQELIDHAI--AQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 269 TAARYGGEEFvIVLPETNTTGAMQ-VANRIRRGVEQAkFFAGsprQVERLT-ISIGIAIYDQDAQSKRELIEAADAALYQ 346
PRK10060 309 TLARLGGDEF-LVLASHTSQAALEaMASRILTRLRLP-FRIG---LIEVYTgCSIGIALSPEHGDDSESLIRSADTAMYT 383
|
....*...
gi 94971157 347 AKGQGRNQ 354
PRK10060 384 AKEGGRGQ 391
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-22 |
101.51 |
41.51 |
4,197,212,108,306,320,5,312,325,2,315,327,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 198 DFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYGGEE 277
PRK10245 213 DGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 292
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94971157 278 FVIVLPETNTTGAMQVANRIRRGVEQAKfFAGSPrQVeRLTISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRNQ 354
PRK10245 293 FAVIMSGTPAESAITAMLRVHEGLNTLR-LPNAP-QV-TLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
|
|
|
|
|
|
|
-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 |
2e-21 |
98.56 |
27.15 |
4,173,207,19,193,226,95,289,321,7,297,328,59 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 174 LTLVAENQLTRDYENEGLIkFAFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGDQVL 253
COG5001 208 VTLTQRAEETRRLSDENDR-LANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 254 RDVSAVLMKDLREVDTAARYGGEEFVIVLPETNTTgAMQVANRiRRGVEQAKFFAGSPRQVERLTISIGIAIYDQDAQSK 333
COG5001 287 IEVGRRLKAFDGAPILAARLGGDEFALIIPALEDD-ALRVAGA-RALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTS 364
|
170 180
....*....|....*....|...
gi 94971157 334 RELIEAADAALYQAKGQGRNQVV 356
COG5001 365 EQLFERADYALYHAKQNGKGAAV 387
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
4e-15 |
77.75 |
47.42 |
7,144,207,25,171,232,10,189,242,25,215,267,77,295,344,9,304,355,30,335,385,15 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 145 VSNKVIGSMQLFSAEHESFTREDAQlfWMLTLVAENQltrdyeneGLIKFAFTDFLTGLKTRGYFEQQLElEIKRAERKR 224
PRK09966 208 VSEERIAEFHRFALDFNSLLDEMEE--WQLRLQAKNA--------QLLRTALHDPLTGLANRAAFRSGIN-TLMNNSDAR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 225 TPIAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYGGEEFVIVLPETNTTGAMQvanRIRRGVEQA 304
PRK09966 277 KTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQ---QICSALTQI 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 94971157 305 --KFFAGSPRQVERLTISIGIAIYDQDAQSKReLIEAADAALYQAKGQ 350
PRK09966 354 fnLPFDLHNGHQTTMTLSIGYAMTIEHASAEK-LQELADHNMYQAKHQ 400
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
5e-13 |
70.64 |
19.27 |
7,188,372,6,197,378,16,213,395,9,227,404,86,316,490,8,327,498,8,335,507,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 189 EGLIKFaftDFLTGLKTRGYFEQQL-ELEIKRAERkrtpiAMLMLDLDHFKTLNDTYGHHVGDQVLRDVSAVLMKDLREV 267
PRK11359 373 EQLIQF---DPMTGLPNRNNLHNYLdDLVDKAVSP-----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 268 DTAARYGGEEFVIVLPETNTTGAMQVANRIRRGVEQAKFFAGSPRQverLTISIGIAiydQDAQSKRE-LIEAADAALYQ 346
PRK11359 445 QYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFP---LTLSIGIS---YDVGKNRDyLLSTAHNAMDY 518
|
....*...
gi 94971157 347 AKGQGRNQ 354
PRK11359 519 IRKNGGNG 526
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
4e-10 |
60.67 |
24.61 |
7,193,226,57,250,287,11,264,298,6,270,305,36,310,341,8,318,350,8,327,358,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 194 FAFTDFLTGLKTRGYFEQQLELEIKRAERKRTPIAMLMLDLDHFKTLNDTYGHHVGD----QVLRDVSAVLMkdlREVDT 269
PRK11059 227 NAFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDellfELINLLSTFVQ---RYPGA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 270 A-ARYGGEEFVIVLPETNTTGAMQVANRIRRGVEQAKFfagsPRQVERLT-ISIGIAIYdQDAQSKRELIEAADAALYQA 347
PRK11059 304 LlARYSRSDFAVLLPHRSLKEADSLASQLLKAVDSLPP----PKMLDRDDfLHIGIAAY-RSGQSTEQVMEEAEMALRSA 378
|
....*.
gi 94971157 348 KGQGRN 353
PRK11059 379 QLQGGN 384
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
2e-06 |
48.54 |
26.79 |
7,173,263,8,181,277,5,186,283,13,199,304,24,224,328,64,288,393,19,310,412,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 174 LTLVAENQ------LTRDY-ENEGLIKFAFTDF--------LTGLKTRGYFEQQLELEIKRAERKrTPIAMLMLDLDHFK 238
PRK11829 264 LTLPAHHQddelgvLVRNYnRNQQLLADAYADMgrishrfpVTELPNRSLFISLLEKEIASSTRT-DHFHLLVIGIETLQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94971157 239 TLNDTYGHHVGDQVLRDVSAVLMKDLREVDTAARYGGEEFVIVLPETNTT-GAMQVANRIRRGVEQAKFFagsPRQVERL 317
PRK11829 343 EVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSfPAMQLARRIMSQVTQPLFF---DEITLRP 419
|
170 180 190
....*....|....*....|....*....|....*....
gi 94971157 318 TISIGIAIYDQDAQSKRELIEAADAALYQAKGQGRNQVV 356
PRK11829 420 SASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIM 458
|
|
|
|
|
|
|
-1 |
|