| 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 |
2e-30 |
128.86 |
100.00 |
3,303,0,106,411,106,23,434,130,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 304 TDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHEDSVARLAGD 383
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94967990 384 DFVALFPYVDANRALTSLDRFKSTLEnaQLRLHDGKEITLTGACGLSDWKP-GMSAEDLLDSALKACGEAKAKGRNSVA 461
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIE--EPFFIDGEEIRVTASIGIAEYPEdGEDLEELLRRADKALYQAKRSGRNRVV 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 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
3e-27 |
118.12 |
97.55 |
3,303,4,106,411,110,21,432,132,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 304 TDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHEDSVARLAGD 383
smart00267 5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 384 DFVALFPYVDANRALTSLDRFKSTLEnaQLRLHDGKEITLTGACGLSDW-KPGMSAEDLLDSALKACGEAKAKGRNSVAV 462
smart00267 85 EFALLLPETSLEEAIALAERILQQLR--EPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQVAV 162
|
.
gi 94967990 463 A 463
smart00267 163 Y 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-27 |
116.76 |
98.90 |
3,284,2,125,411,127,25,436,154,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 285 FRDVSDRKALEKQIQRDGTTDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFG 364
COG2199 3 LRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 365 TILRATLRHEDSVARLAGDDFVALFPYVDANRALTSLDRFKSTLEnaQLRLHDGKEITLTGACGLSDWKPGM--SAEDLL 442
COG2199 83 RRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALE--EPFFLGGEELRVTVSIGVALYPEDGsdDAELLL 160
|
170 180
....*....|....*....|.
gi 94967990 443 DSALKACGEAKAKGRNSVAVA 463
COG2199 161 RRADLALYRAKRAGRNRVVVF 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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
5e-24 |
107.33 |
98.75 |
3,303,2,106,409,109,23,432,133,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 304 TDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHEDSVARLAGD 383
pfam00990 3 HDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94967990 384 DFVALFPYVDANRALTSLDRFKSTLE-NAQLRLHDGKEITLTGACGLSDW-KPGMSAEDLLDSALKACGEAKAKGRNS 459
pfam00990 83 EFAILLPDTSLEGAQELAERIRRLLAaLKIPHTLSGLPLYVTISIGIAAYpNDGEDAEDLLKRADQALYQAKNQGRNR 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 |
2e-20 |
95.48 |
98.79 |
2,302,2,134,436,137,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 303 TTDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHEDSVARLAG 382
TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 383 DDFVALFPYVDANRALTSLDRFKSTLENAQLRLHDGKEITLTGACGLSDWKPGM-SAEDLLDSALKACGEAKAKGRNSVA 461
TIGR00254 83 EEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAKKAGRNRVV 162
|
...
gi 94967990 462 VAA 464
TIGR00254 163 VAD 165
|
|
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 |
| 32385 |
COG2203 |
FhlA |
FOG: GAF domain [Signal transduction mechanisms] |
FOG: GAF domain [Signal transduction mechanisms] |
true |
false |
false |
175 |
1e-10 |
62.72 |
99.43 |
4,8,1,55,64,56,15,79,83,56,135,140,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 9 EAARQQELTSFQILDTPPDSSFDNLVALAAEICEAPISTVTFIDSDRQWFKAKLGvESDQTPREQSFCAHA--------- 79
COG2203 2 EEALLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGLLDGALVA-EAAEAGLEQLIDELFglvilpacl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 80 ---ILKPNEFMVVPDAAKDPRFEDNPLVTGEPNIRFYAAAPLVSKGLGLGALCIIDRQP-RTLKPFQESALRTLASQAAQ 155
COG2203 81 igiALREGRPVVVEDILQDPRFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPrRQWSEEELELLEELAEQVAI 160
|
170
....*....|....*
gi 94967990 156 LMELHRQRAMAENHR 170
COG2203 161 AIERARLYEELQEAE 175
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 110584 |
pfam01590 |
GAF |
GAF domain |
GAF domain |
false |
false |
false |
153 |
4e-10 |
61.49 |
98.69 |
4,24,0,30,54,37,26,81,63,28,109,105,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 25 PPDSSFDNLVALAAEICEAPISTVTFIDSD-------RQWFKAKLGVESDQTPREQSFCAHAIlKPNEFMVVPDAAKDPR 97
pfam01590 1 DLEELLQTILEELRELLGADRCAILLADADglllylvAGDGLSDIPLAARGLPLGGGVVGEVI-AGGNPIVVPDVQDDPR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94967990 98 FEDNPLVTGEPN--------------IRFYAAAPLVSKGLGLGALCIIDRQPRTLKPFQESALRTLASQAAQ 155
pfam01590 80 FRDLTALAEELPapvgchehylrglgIRSCLAVPLLGGGKLIGVLVLHSTSPRAFTEEELELLQALADQVAI 151
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 128379 |
smart00065 |
GAF |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
false |
false |
false |
149 |
5e-06 |
47.76 |
96.64 |
5,26,2,28,54,37,24,79,61,19,99,80,34,133,115,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 27 DSSFDNLVALAAEICEAPISTVTFIDSD-------RQWFKAKLGVESDQTPREQSFCAHaILKPNEFMVVPDAAKDPRFe 99
smart00065 3 EELLQTILEELRQLLGADRVLIYLVDEDdrgelvlVAADGLTLPLLGLRYPLGEGLAGR-VAETGRPLNIPDVEADPVF- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94967990 100 DNPLVTGEPNIRFYAAAPLVSKGLGLGALCIIDR-QPRTLKPFQESALRTLASQAAQLMELHRQRA 164
smart00065 81 ALDLLGRYQGVRSFLAVPLVADGELVGVLALHNKdSPRPFTEEDEELLQALANQLAIALANAQLYE 146
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 29035 |
cd00130 |
PAS |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most... |
true |
true |
true |
103 |
0.001 |
39.87 |
100.00 |
4,179,0,40,230,40,7,237,51,46,283,98,5 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 180 LAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLhfkpvqpdgfpIPTEDLP----SYKALATGEPQRNVIFGI 255
cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDL-----------IHPEDREelreRLENLLSGGEPVTLEVRL 69
|
90 100 110
....*....|....*....|....*....|....
gi 94967990 256 TRPNKTEIWIESNASVLNDPVHGECAVI-SFRDV 288
cd00130 70 RRKDGSVIWVLVSLTPIRDEGGEVIGLLgVVRDI 103
|
|
cl02459 |
141436 |
PAS |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most... |
2 |
| 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 |
7e-23 |
103.85 |
45.75 |
4,274,235,24,298,266,117,415,384,21,436,406,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 275 PVHGECAVISFRDVSDRKALEKQI-------QRDGTTDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAM 347
COG3706 236 PIEEGELRARLRRQLRRKRYERQLreslerlQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 348 VAKHGPHAADSALKHFGTILRATLRHEDSVARLAGDDFVALFPYVDANRALTSLDRFKSTLENAQLRL-HDGKEITLTGA 426
COG3706 316 NDTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHeLSREPLEVTIS 395
|
170 180 190
....*....|....*....|....*....|....*....
gi 94967990 427 CGLSDWKPGM-SAEDLLDSALKACGEAKAKGRNSVAVAA 464
COG3706 396 IGVAEGKPGEdSIEELLKRADKALYKAKASGRNRVVVKR 434
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
2e-17 |
85.74 |
35.67 |
3,303,293,117,420,411,14,434,426,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 304 TDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHEDSVARLAGD 383
PRK09581 294 TDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYGGE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 384 DFVALFPYVDANRALTSLDRFKSTLENAQLRLHDGKE-ITLTGACGLSDWKP-GMSAEDLLDSALKACGEAKAKGRNSVA 461
PRK09581 374 EFVVVMPDTDIEVAIAVAERIRRKIAEEPFAISDGKErLNVTVSIGVAELRPsGESIEALIKRADKALYEAKNTGRNRVV 453
|
...
gi 94967990 462 VAA 464
PRK09581 454 ALA 456
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
5e-17 |
84.37 |
16.31 |
5,280,666,133,413,803,4,417,808,7,427,815,7,436,822,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 281 AVISFRDVSDRKALEKQIQRDGTTDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSAL 360
PRK09776 667 SVLVFQDVTESRAMLRQLSYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 361 KHFGTILRATLRHEDSVARLAGDDFVALFPYVDANRALTSLDRFKSTLENAQL----RLHD-GKEITLTgacGLSDWKPg 435
PRK09776 747 RELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYRFpwegRVYRvGASAGIT---AIDDNNH- 822
|
170 180
....*....|....*....|....*..
gi 94967990 436 mSAEDLLDSALKACGEAKAKGRNSVAV 462
PRK09776 823 -QASEVMSQADIACYAAKNAGRGRVTV 848
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
9e-12 |
66.66 |
66.21 |
5,275,94,13,288,108,12,300,128,26,328,154,85,414,239,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 276 VHGECAVISFRDV-SDRKALEKQIQR--------DGTTDPLTGLPNRAAFLNYVGKAIAAasRYKHPMSVCVASLDDLKA 346
PRK09894 95 AEGHWQDADFDAFqEGLLSFTAALTDykiylltiRSNMDVLTGLPGRRVLDESFDHQLRN--REPLNLYLALLDIDRFKL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 347 MVAKHGPHAADSALKHFGTILRATLRHEDSVARLAGDDFVALFPYVDANRALTSLDRFKSTLENAQLrLHDGKEITLTGA 426
PRK09894 173 VNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEEFIIILKAATDEEACRAGERIRQLIANQAI-THSEGRINITAT 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 94967990 427 CGLSDWKPGMSAEDLLDSALKACGEAKAKGRNSVAVA 463
PRK09894 252 FGVTRAFPEEPLDEVIGRADRAMYEGKQAGRNRVMFI 288
|
|
|
|
|
|
|
-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 |
3e-10 |
61.58 |
25.79 |
4,291,217,101,392,320,8,400,331,31,436,362,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 292 KALEKQIQRDGTTDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATL 371
COG5001 218 RRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 372 RHEDSVARLAGDDFVALFPYV--DANRALTS---LDRFKSTLENAQLRLHDGKEITLTGACGLSDwkpgmSAEDLLDSAL 446
COG5001 298 GAPILAARLGGDEFALIIPALedDALRVAGAralCESLQAPYDLRGVRVQVGASIGIAPFPSGAD-----TSEQLFERAD 372
|
170
....*....|....*.
gi 94967990 447 KACGEAKAKGRNSVAV 462
COG5001 373 YALYHAKQNGKGAAVL 388
|
|
|
|
|
|
|
-1 |
| 138539 |
PRK11360 |
PRK11360 |
sensory histidine kinase AtoS; Provisional |
sensory histidine kinase AtoS; Provisional |
false |
true |
false |
607 |
2e-08 |
55.85 |
19.11 |
6,175,265,44,225,309,8,236,317,25,262,342,13,276,355,4,280,361,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 176 VMETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLhfkpvqPDGFPIPTedlPSYKALATGEPQRNVIFGI 255
PRK11360 266 IIENAADGIIAIDRQGDITTMNPAAEVITGYQRHELVGQPYSML------FDNTQFYS---PVLDTLEHGTEHVALEISF 336
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 94967990 256 TRPNKTeIWIESNASVLNDPvHGEC--AVISFRDVSDRKALEKQIQR 300
PRK11360 337 PGRDRT-IELSVTTSRLHDT-HGEMigAVVIFSDLTARKRLQRRMAR 381
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-08 |
55.29 |
45.55 |
3,294,202,114,410,316,28,438,345,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 295 EKQIQRDGTTDPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHE 374
PRK10245 203 KRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 375 DSVARLAGDDFVALFPYVDANRALTSLDRFKSTLenAQLRLHDGKEITLTGACGLSDWKPGMSA-EDLLDSALKACGEAK 453
PRK10245 283 DVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGL--NTLRLPNAPQVTLRISVGVAPLNPQMSHyREWLKSADLALYKAK 360
|
170
....*....|.
gi 94967990 454 AKGRNSVAVAA 464
PRK10245 361 KAGRNRTEVAA 371
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
2e-07 |
52.42 |
13.73 |
3,303,238,25,330,263,60,392,323,6 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 304 TDPLTGLPNRAAFLNYVGKAIAAASryKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATLRHEDSVARLAGD 383
PRK10060 239 TDSITGLPNRNAIQELIDHAIAQAD--NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGD 316
|
90
....*....|....*
gi 94967990 384 DFVALFPyvDANRAL 398
PRK10060 317 EFLVLAS--HTSQAA 329
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
2e-07 |
52.15 |
20.40 |
5,289,363,40,333,403,73,407,476,8,416,484,14,431,498,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 290 DRKALEKQIQRDGTTDPLTGLPNRAAFLNYVGKAIAAASRykhpMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRA 369
PRK11359 364 EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVS----PVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 370 TLRHEDSVARLAGDDFVALFPYVDANRALTSLDRFKStLENAQLRLhDGKEITLTGACGLSdWKPGMSAEDLLDSALKAC 449
PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRN-VVSKPIMI-DDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAM 516
|
170
....*....|
gi 94967990 450 GEAKAKGRNS 459
PRK11359 517 DYIRKNGGNG 526
|
|
|
|
|
|
|
-1 |
| 110021 |
pfam00989 |
PAS |
PAS fold |
PAS fold |
true |
true |
false |
112 |
4e-05 |
44.70 |
100.00 |
5,170,0,49,230,49,9,239,62,36,275,101,7,284,108,4 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 171 RFLHTVMETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLhfkpvqpdgfpIPTEDLPSY----KALATGE 246
pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDL-----------IPEDDDAVAellrQALLQGE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 94967990 247 PQRNVIFGITRPNKTEIWIESNASVLNDP---VHGECAVisFRDV 288
pfam00989 70 ESRGFEVSFRVSDGRPRHVEVRASPVRDAggeILGFLGV--LRDI 112
|
|
|
|
|
|
|
-1 |
| 34605 |
COG5000 |
NtrY |
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms] |
Signal transduction histidine kinase involved in nitrogen fixation and metabolism... |
false |
true |
false |
712 |
6e-05 |
43.79 |
17.28 |
3,154,353,65,230,418,48,280,466,10 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 155 QLMELHRQRAMAENHRRFLHTVMETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLhfkpvqpdgfpIPTE 234
COG5000 354 QQEALERAKDALEQRRRFLEAVLSGLTAGVIGFDNRGCITTVNPSAEQILGKPFDQLLGQSLSAI-----------APEL 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 94967990 235 DLPSYKALATGEPQRNVIFGITRPNKTEIWIESNASVLNDPVHGecAVISFRDVSD 290
COG5000 423 EEVFAEAGAAARTDKRVEVKLAREGEERTLNVQATREPEDNGNG--YVVTFDDITD 476
|
|
|
|
|
|
|
-1 |
| 33622 |
COG3829 |
RocR |
Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains [Transcription / Signal transduction mechanisms] |
Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains [... |
false |
true |
false |
560 |
7e-05 |
43.74 |
26.79 |
8,150,101,14,169,115,45,219,160,9,233,169,19,253,188,7,262,195,16,280,211,20,303,231,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 151 SQAAQLMELHRQRAmaenhRRFLHTVMETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQtfsmlHFKPVQPDGfp 230
COG3829 102 SEALELIEENLRQL-----RQRLEAILDSIDDGLLVVDEDGIIIYYNKAYAKLLGLSPEEVLGK-----HLLDVVSAG-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 231 iptEDLPSYKALATGEPQRNVIfGITRPNKteIWIESNASVLNDPVHGecAVISFRDVSDRKALEKQIQRdgtTDPLTGL 310
COG3829 170 ---EDSTLLEVLRTGKPIRDVV-QTYNGNK--IIVNVAPVYADGQLIG--VVGISKDVSELERLTRELEE---SEGLLRL 238
|
170
....*....|...
gi 94967990 311 PNRAAFLNYVGKA 323
COG3829 239 KAKYTFDDIIGES 251
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
8e-05 |
43.85 |
39.56 |
4,291,237,29,321,266,47,368,315,6,376,321,77 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 292 KALEKQIQRDGTTDPLTGLPNRAAFLNYVgKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILR--A 369
PRK09966 238 QAKNAQLLRTALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAefG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 370 TLRHEdsVARLAGDDFVALFPYVDANRALTSLDRFKSTLENAQLRLHDGKEITLTGACGLSDWKPGMSAEDLLDSALKAC 449
PRK09966 317 GLRHK--AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNM 394
|
....
gi 94967990 450 GEAK 453
PRK09966 395 YQAK 398
|
|
|
|
|
|
|
-1 |
| 117025 |
pfam08448 |
PAS_4 |
PAS fold |
PAS fold |
false |
true |
false |
110 |
4e-04 |
41.63 |
99.09 |
6,177,1,50,231,51,6,239,57,14,255,71,20,276,91,4,280,97,13 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 178 ETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLHFKPVQPDgfpiPTEDLPsyKALATGEPQRNVIFgiTR 257
pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAAR----LERALR--RALEGEEPIDFLEE--LL 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 94967990 258 PNKTEIWIESNASVLNDPvHGEC--AVISFRDVSDRKA 293
pfam08448 74 LNGEERHYELRLTPLRDP-DGEVigVLVISRDITERRR 110
|
|
|
|
|
|
|
-1 |
| 129332 |
TIGR00229 |
sensory_box |
PAS domain S-box |
PAS domain S-box |
false |
true |
false |
124 |
5e-04 |
41.11 |
95.97 |
4,170,2,49,230,51,13,243,68,9,252,78,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 171 RFLHTVMETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLhfkpvqpdgfpIPTEDLPSYKALA----TGE 246
TIGR00229 3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLEL-----------IPEEDREEVRERIerllEGE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 94967990 247 PQRNVI-FGITRPNKTEIWIESNASVLNDPVHGECAVISFRDVSDRKALE 295
TIGR00229 72 REPYSEeRRVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKQAE 121
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
6e-04 |
40.98 |
17.77 |
8,163,129,13,177,142,60,241,202,12,254,214,6,261,220,9,270,230,20,294,250,4,299,254,17 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 164 AMAENHRRFLHTVmETLAEGVIVRDSQRRLLAHNTMASVLLGTELKDMVGQTFSMLHFKPVQPDGFPIPTEDLPsykaLA 243
PRK11359 130 AQKEQTRQLIIAV-DHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLL----WK 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94967990 244 TGEPQRNVIFgITRPNKtEIWIESNAS-VLNDPVHGECAVISFRDVSDrkalEKQIqRDGTTDPLTGLPNRAAF 316
PRK11359 205 TARDQDEFLL-LTRTGE-KIWIKASISpVYDVLAHLQNLVMTFSDITE----ERQI-RQLEGNILAAMCSSPPF 271
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
6e-04 |
40.52 |
24.12 |
5,299,228,32,332,260,17,352,277,64,419,341,8,427,351,34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 300 RDGTTDPLTGLPNRAAFLNYVGKAIAAASRYKhPMSVCVASLDDLKAMVAkhgPHAADSALKHFGTILRATLRHEDSVAR 379
PRK13561 229 ENAMRFPVSDLPNKALLMALLEQVVARKQTTA-LMIITCETLRDTAGVLK---EAQREILLLTLVEKLKSVLSPRMVLAQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 380 LAGDDFVALFPYVDANRALTSLDRFKSTLENAQLRLHdgkEITLTGAC--GLSDWKPGMSAEDLLDSALKACGEAKAKGR 457
PRK13561 305 ISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQ---RIQLRPSCsiGIAMFYGDLTAEQLYSRAVSAAFTARRKGK 381
|
....
gi 94967990 458 NSVA 461
PRK13561 382 NQIQ 385
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
0.001 |
39.87 |
24.14 |
5,304,230,67,371,298,6,377,305,13,394,318,33,427,353,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967990 305 DPLTGLPNRAAFLNYVGKAIAAASRYKHPMSVCVASLDDLKAMVAKHGPHAADSALKHFGTILRATL-RHEDSV-ARLAG 382
PRK11059 231 DAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFELINLLSTFVqRYPGALlARYSR 310
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94967990 383 DDFVALFPyvdaNRALTSLDRFKSTLENAQLRLHDGKEITLTGAC--GLSDWKPGMSAEDLLDSALKACGEAKAKGRNS 459
PRK11059 311 SDFAVLLP----HRSLKEADSLASQLLKAVDSLPPPKMLDRDDFLhiGIAAYRSGQSTEQVMEEAEMALRSAQLQGGNS 385
|
|
|
|
|
|
|
-1 |
| 33405 |
COG3605 |
PtsP |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms] |
Signal transduction protein containing GAF and PtsI domains [Signal transduction... |
false |
true |
false |
756 |
0.002 |
39.13 |
8.73 |
2,90,88,12,103,100,54 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94967990 91 DAAKDPRFEDNPlVTGEPNIRFYAAAPLVSKGLGLGALCIIDRQPRTLKPFQESALRTLASQAAQLM 157
COG3605 89 DAQSHPSFKYLP-ETGEERYHSFLGVPIIRRGRLLGVLVVQQRELRQYDEDEVEFLVTLAMQLAEIV 154
|
|
|
|
|
|
|
-1 |
|