| 30163 |
cd01948 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
true |
false |
true |
240 |
1e-49 |
193.12 |
99.17 |
6,460,2,38,498,41,27,525,69,7,532,82,18,550,106,29,579,137,103 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 461 LEKALAEGELRLYGQPIVDLATGRPAGVEVLLRWARGE-EVVPASRFIPVAEEAGLIPELDLYVLR-ALAQMTT------ 532
cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEeACRQLARwqaggp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 533 ALPLHVNLSPQTLLDERL------LLGLAPLKGRNLRLELTEHALASPGAEAR--LKELSCMGFPVVLDDFGQGYASLRL 604
cd01948 83 DLRLSVNLSARQLRDPDFldrlleLLAETGLPPRRLVLEITESALIDDLEEALatLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46198730 605 LVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRPAPLEE 682
cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 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 |
3e-23 |
105.36 |
97.45 |
4,292,0,24,316,31,57,373,89,22,396,111,42 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 293 HDPLTGLPNRRRLEEDFRLLRGRW-------ALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGG 365
cd01949 1 TDPLTGLPNRRAFEERLERLLARArrsgrplALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46198730 366 EFLALLPG-GAKEAEAFGQALGEALEAPLDLgEGRAFRVRVRAGVALFPDDANTLSELLRRADQALREAKKAGK 438
cd01949 81 EFAILLPGtDLEEAEELAERLRKAIEEPFFI-DGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGR 153
|
|
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 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
1e-48 |
189.73 |
98.76 |
7,460,3,34,494,39,9,504,48,21,525,70,5,530,81,20,550,107,21,571,130,111 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 461 LEKALAEGELRLYGQPIVDLATGRPAGVEVLLRW--ARGEEVVPAsRFIPVAEEAGLIPELDLYVLR-ALAQM------T 531
smart00052 4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWqhPEGGIISPD-EFIPLAEETGLIVPLGRWVLEqACQQLaewqaqG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 532 TALPLHVNLSPQTLLDERL------LLGLAPLKGRNLRLELTEHAL--ASPGAEARLKELSCMGFPVVLDDFGQGYASLR 603
smart00052 83 PPLRISINLSARQLISPDLvprvleLLEETGLPPQRLELEITESVLldDDESAVATLQRLRELGVRIALDDFGTGYSSLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46198730 604 LLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRPAPLEE 682
smart00052 163 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 241
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 32382 |
COG2200 |
Rtn |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
false |
false |
false |
256 |
7e-47 |
183.99 |
95.70 |
6,453,0,41,494,42,31,525,74,7,532,86,18,550,110,23,573,135,110 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 454 RREVLAGLEKALAEGELRLYGQPIVDLATGRPAGVEVLLRW-ARGEEVVPASRFIPVAEEAGLIPELDLYVLR-ALAQMT 531
COG2200 1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWrHPDGGLISPGEFIPLAEETGLIVELGRWVLEeACRQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 532 T-----ALPLHVNLSPQTLLDERL------LLGLAPLKGRNLRLELTEHALAS--PGAEARLKELSCMGFPVVLDDFGQG 598
COG2200 81 TwpragPLRLAVNLSPVQLRSPGLvdlllrLLARLGLPPHRLVLEITESALIDdlDTALALLRQLRELGVRIALDDFGTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 599 YASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRPA 678
COG2200 161 YSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPL 240
|
....*
gi 46198730 679 PLEEV 683
COG2200 241 PADAL 245
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 109613 |
pfam00563 |
EAL |
EAL domain |
EAL domain |
false |
false |
false |
236 |
4e-45 |
178.00 |
98.73 |
7,460,3,34,494,38,31,525,70,8,533,87,18,551,110,20,571,131,52,624,183,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 461 LEKALAEGELRLYGQPIVDLATGRPAGVEVLLRW-ARGEEVVPASRFIPVAEEAGLIPELDLYVLR-ALAQMTTA----- 533
pfam00563 4 LREALENGEFSLYFQPIVDLRTGKVLGYEALLRWqHPDGGLIPPDEFLPLAERLGLIAELDRWVLEkALAQLAEWrgnal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 534 ----LPLHVNLSPQTLLDERLL-----LGLAPLKGRNLRLELTEHAL-ASPGAEARLKELSCMGFPVVLDDFGQGYASLR 603
pfam00563 84 lppdLPLSVNLSPASLLDPSFLeallaLKQGGLPPSRLVLEITESDLdEDLRLLEALARLRSLGFRLALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46198730 604 LLVGLPFSMAKVDRGFVGGIgLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRP 677
pfam00563 164 YLSRLPPDYIKIDRSFIKDL-SDPESRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 236
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
2e-17 |
86.15 |
98.16 |
5,291,3,24,315,34,58,373,93,22,396,115,42,438,158,5 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 292 YHDPLTGLPNRRRLEEDFRLLRGR-------WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEG 364
smart00267 4 FRDPLTGLPNRRYFEEELEQELQRaqrqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 365 GEFLALLPG-GAKEAEAFGQALGEALEAPLDLgEGRAFRVRVRAGVALFPDDANTLSELLRRADQALREAKKAGK-RWTF 442
smart00267 84 DEFALLLPEtSLEEAIALAERILQQLREPIII-HGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRnQVAV 162
|
.
gi 46198730 443 Y 443
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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
2e-17 |
86.14 |
98.75 |
6,291,1,21,315,22,7,322,36,5,327,44,46,373,94,22,396,116,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 292 YHDPLTGLPNRRRLEEDFRLLrgrWALCRLD-------LVDLY---EVNEAYGREAGDALLARTSRRLQALLPREGRLYR 361
pfam00990 2 AHDPLTGLPNRRYFEEELEQE---LQRAQRRqsplallLLDLDnfkRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 362 LEGGEFLALLPG----GAKEAEAFGQALGEALEAPLDLgEGRAFRVRVRAGVALFPDDANTLSELLRRADQALREAKKAG 437
pfam00990 79 LGGDEFAILLPDtsleGAQELAERIRRLLAALKIPHTL-SGLPLYVTISIGIAAYPNDGEDAEDLLKRADQALYQAKNQG 157
|
..
gi 46198730 438 KR 439
pfam00990 158 RN 159
|
|
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 |
3e-17 |
85.56 |
88.95 |
4,291,20,25,316,52,57,373,110,65,438,176,5 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 292 YHDPLTGLPNRRRLEEDFRLLRGRW-------ALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEG 364
COG2199 21 LHDPLTGLPNRRAFEERLERALARArrhgeplALLLLDLDHFKQINDTYGHAAGDEVLREVARRLRSNLREGDLVARLGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 365 GEFLALLPG-GAKEAEAFGQALGEALEAPLDLGEGRAFRVRVRAGVALFPDDANTLSELLRRADQALREAKKAGK-RWTF 442
COG2199 101 DEFAVLLPGtSLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDDAELLLRRADLALYRAKRAGRnRVVV 180
|
.
gi 46198730 443 Y 443
COG2199 181 F 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 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
1e-10 |
63.51 |
98.18 |
6,291,2,21,315,23,7,322,37,4,326,44,54,380,99,11,391,111,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 292 YHDPLTGLPNRRRLEEDFRLLrgrWALCRLD-------LVDL---YEVNEAYGREAGDALLARTSRRLQALLPREGRLYR 361
TIGR00254 3 VRDPLTGLYNRRYLEEMLDSE---LKRARRFqrsfsvlMIDIdnfKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 362 LEGGEFLALLPGGAKEAEA-FGQALGEALEA-PLDLGEGRAFRVRVRAGVALFPDDANTLSELLRRADQALREAKKAGKR 439
TIGR00254 80 YGGEEFVVILPGTPLEDALsKAERLRDAINSkPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 46198730 440 WTFYS 444
TIGR00254 160 RVVVA 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 |
| 110584 |
pfam01590 |
GAF |
GAF domain |
GAF domain |
true |
false |
false |
153 |
2e-10 |
63.03 |
97.39 |
4,142,1,11,153,17,17,173,34,49,222,97,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 143 LHKVCALLVEE-----GYALAWVGEARPTGEVVpreAAGAVGYLEGIRVRWDEAPEGQGPTGRALRSGRPQVLRSVEEDP 217
pfam01590 2 LEELLQTILEElrellGADRCAILLADADGLLL---YLVAGDGLSDIPLAARGLPLGGGVVGEVIAGGNPIVVPDVQDDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46198730 218 RYAPW--------------RERAQVFGFASSAAFPLRVEGRVWGSLNVYAPEEDAFDEEEVRLLEDLARLIG 275
pfam01590 79 RFRDLtalaeelpapvgchEHYLRGLGIRSCLAVPLLGGGKLIGVLVLHSTSPRAFTEEELELLQALADQVA 150
|
|
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 |
4e-09 |
58.54 |
70.47 |
5,165,31,25,195,56,23,220,79,12,232,92,24,256,117,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 166 TGEVVPREAAGAVGYLEGIRVRWDEapegqGPTGRALRSGRPQVLRSVEEDPRyaPWRERAQVFGFA-SSAAFPLRVEGR 244
smart00065 32 RGELVLVAADGLTLPLLGLRYPLGE-----GLAGRVAETGRPLNIPDVEADPV--FALDLLGRYQGVrSFLAVPLVADGE 104
|
90 100 110
....*....|....*....|....*....|..
gi 46198730 245 VWGSLNVYAPEE-DAFDEEEVRLLEDLARLIG 275
smart00065 105 LVGVLALHNKDSpRPFTEEDEELLQALANQLA 136
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 32385 |
COG2203 |
FhlA |
FOG: GAF domain [Signal transduction mechanisms] |
FOG: GAF domain [Signal transduction mechanisms] |
false |
false |
false |
175 |
2e-07 |
52.71 |
82.86 |
4,134,14,19,153,34,25,178,61,78,256,140,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 135 QAAGEGDLLHKVCALLVEE-GYALAWVGEARPTGEVVPREAAGAV--GYLEGIRVRWDEAPEGQGPTGRALRSGRPQVLR 211
COG2203 15 QDLDLEEILQAALELLAELlGADRGLIYLLDEDGLLDGALVAEAAeaGLEQLIDELFGLVILPACLIGIALREGRPVVVE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46198730 212 SVEEDPRYAPWRERAQVFGFASSAAFPLRVEGRVWGSLNVYAPEE-DAFDEEEVRLLEDLARLIG 275
COG2203 95 DILQDPRFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPrRQWSEEELELLEELAEQVA 159
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
6e-04 |
41.62 |
56.08 |
6,537,103,24,561,129,16,577,146,7,588,153,30,618,184,30,649,214,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 538 VNLSPQTLLDERLLLGLAPLKGRN--LRLELTEHALASPGAE-ARLKELScmgfPVVLDDFGQGYASLRLLVGLPFSMAK 614
PRK11596 104 VNIDGPTLIALRQQPKILRLIERLpwLRFELVEHIRLPKDSTfASMCEFG----PLWLDDFGTGMANFSALSEVRYDYIK 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46198730 615 VDRG-FVGGIGLDPKAEAALKAVLALSRELEIALVaEGVEREDQWAWLRSVGYSLGQGYLWGRPAPLE 681
PRK11596 180 VARElFVMLRQSPEGRTLFSQLLHLMNRYCRGVIV-EGVETPEEWRDVQRSPAFAAQGYFLSRPAPFD 246
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 32139 |
COG1956 |
COG1956 |
GAF domain-containing protein [Signal transduction mechanisms] |
GAF domain-containing protein [Signal transduction mechanisms] |
false |
false |
false |
163 |
0.002 |
39.87 |
73.62 |
4,142,36,33,177,69,9,191,78,36,232,114,42 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 143 LHKVCALLVEEGYALAWVGEARPTGEVVPREAAgaVGYLEGIRVrwdeaPEGQGPTGRALRSGRPQVLRSVEEDPRYAPW 222
COG1956 37 LANASALLKERLPDVNWVGFYLLEGDELVLGPF--QGKVACVRI-----PFGKGVCGTAAATGETVRVDDVHAFPGHIAC 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 46198730 223 RERAQvfgfaSSAAFPLRVEGRVWGSLNVYAPEEDAFDEEEVRLLEDLARLI 274
COG1956 110 DAASN-----SEIVVPIFKDGKLIGVLDIDSPTPGRFDEEDEAGLEKLAALL 156
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-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 |
1e-50 |
196.78 |
61.99 |
10,293,230,22,315,259,64,379,325,30,410,355,28,438,384,61,499,446,25,524,472,8,532,483,22,554,511,25,579,538,103 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 294 DPLTGLPNRRRLEEDFRLLRGR-------WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGGE 366
COG5001 231 DSLTGLPNRRRFFAELDARLAAarqsgrrLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDGAPILAARLGGDE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 367 FLALLPGGAKEAE--AFGQALGEALEAPLDLGEGRAFRVRVRAGVaLFPDDANTLSELLRRADQALREAKKAGK-RWTFY 443
COG5001 311 FALIIPALEDDALrvAGARALCESLQAPYDLRGVRVQVGASIGIA-PFPSGADTSEQLFERADYALYHAKQNGKgAAVLF 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 444 SLGLGEAVRERREVLAGLEKALAEGELRLYGQPIVDLATGRPAGVEVLLRWARGEE-VVPASRFIPVAEEAGLIPELDLY 522
COG5001 390 DARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIgPVPPDVFIGIAERSGQIVELTRL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 523 VL-RALAQMTT---ALPLHVNLSPQTLLDERLLLGL------APLKGRNLRLELTEHALASPGAEAR--LKELSCMGFPV 590
COG5001 470 LLaKALREARAwpmDVRVSINLSARDLASMENVRRLlaivseSCIAPHRLDFEITETAIVCDFDQARdaLAALHELGVRT 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 591 VLDDFGQGYASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQ 670
COG5001 550 ALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQ 629
|
410
....*....|..
gi 46198730 671 GYLWGRPAPLEE 682
COG5001 630 GYHYARPMPAEE 641
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
9e-44 |
173.76 |
61.84 |
11,293,239,24,317,268,61,378,330,31,410,361,29,439,391,41,481,432,18,499,451,34,533,492,23,556,516,7,563,528,16,579,546,103 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 294 DPLTGLPNRRRLEEDFRLLRGRWA-----LCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGGEFL 368
PRK10060 240 DSITGLPNRNAIQELIDHAIAQADnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 369 ALLPGGAKEA-EAFGQALGEALEAPLDLGEGRAFRVRVRAGVaLFPDDANTLSELLRRADQALREAKKAGKR-WTFYSLG 446
PRK10060 320 VLASHTSQAAlEAMASRILTRLRLPFRIGLIEVYTGCSIGIA-LSPEHGDDSESLIRSADTAMYTAKEGGRGqFCVFSPE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 447 LGEAVRERREVLAGLEKALAEGELRLYGQPIVDLaTGRPAGVEVLLRWARGEE-VVPASRFIPVAEEAGLIPELDLYVLR 525
PRK10060 399 MNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERgLIPPLEFISYAEESGLIVPLGRWVIL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 526 ALAQMTTA-------LPLHVNLSPQTLLDERLLLGLAP-LKGRNLR-----LELTEHALASPGAEAR--LKELSCMGFPV 590
PRK10060 478 DVVRQAAKwrdkginLRVAVNVSARQLADQTIFTALKQvLQELNFEycpidVELTESCLIENEELALsvIQQFSQLGAQV 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 591 VLDDFGQGYASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQ 670
PRK10060 558 HLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQ 637
|
410
....*....|..
gi 46198730 671 GYLWGRPAPLEE 682
PRK10060 638 GFLFAKPMPAVA 649
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
1e-41 |
166.55 |
51.19 |
11,293,378,22,315,403,59,374,463,45,422,508,15,437,524,62,499,587,26,525,614,6,531,626,4,535,631,15,550,652,27,577,681,106 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 294 DPLTGLPNRRRLEEDFRLLRGR---WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGGEFLAL 370
PRK11359 379 DPMTGLPNRNNLHNYLDDLVDKavsPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 371 LPGG-AKEAEAFGQALGEALEAPLDLGEGRAFRVRVRAGVALFPDDANTLselLRRADQALREAKKAG-KRWTFYSLGLG 448
PRK11359 459 SLENdVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDVGKNRDYL---LSTAHNAMDYIRKNGgNGWQFFSPAMN 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 449 EAVRERREVLAGLEKALAEGELRLYGQPIVDLATGRPAGVEVLLRWARGEE-VVPASRFIPVAEEAGLIPELDLYVLR-A 526
PRK11359 536 EMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHgHVPPSRFIPLAEEIGEIENIGRWVIAeA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 527 LAQMT------TALP-LHVNLSPQTLLDERL------LLGLAPLKGRNLRLELTEHALASPGAE--ARLKELSCMGFPVV 591
PRK11359 616 CRQLAewrsqnIHIPaLSVNLSALHFRSNQLpnqvsdAMHAWGIDGHQLTVEITESMMMEHDTEifKRIQILRDMGVGLS 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 592 LDDFGQGYASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQG 671
PRK11359 696 VDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQG 775
|
410
....*....|..
gi 46198730 672 YLWGRPAPLEEV 683
PRK11359 776 YFFSRPLPAEEI 787
|
|
|
|
|
|
|
-1 |
| 34551 |
COG4943 |
COG4943 |
Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms] |
Predicted signal transduction protein containing sensor and EAL domains [Signal... |
false |
true |
false |
524 |
8e-37 |
150.49 |
47.33 |
7,451,263,47,498,311,26,524,338,13,537,357,14,551,377,27,578,408,5,586,413,98 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 452 RERREVLAGLEKALAEGELRLYGQPIVDLATGRPAGVEVLLRWARGE-EVVPASRFIPVAEEAGLIPELDLYVL-RALAQ 529
COG4943 264 RRYLSPRRRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDgTVVSPDVFIPLAEESGMIEQITDYVIrNVFRD 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 530 MTTALPLH------VNLSPQTLLDERLL------LGLAPLKGRNLRLELTEHALASPGAEA----RLKELscmGFPVVLD 593
COG4943 344 LGDLLRQHrdlhvsINLSASDLASPRLIdrlnrkLAQYQVRPQQIALELTERTFADPKKMTpiilRLREA---GHEIYID 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 594 DFGQGYASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYL 673
COG4943 421 DFGTGYSNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWL 500
|
250
....*....|.
gi 46198730 674 WGRPAPLEEVL 684
COG4943 501 FSKALPAQAFL 511
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
6e-35 |
144.08 |
37.54 |
11,292,689,23,315,719,58,373,778,65,438,844,20,458,866,33,491,900,2,493,903,36,529,949,10,539,960,11,550,972,29,579,1003,105 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 293 HDPLTGLPNRRRLEEDFRLLRGR-------WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGG 365
PRK09776 690 HDALTGLANRASFEKQLREALQTvnsthqrHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGD 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 366 EFLALLPG-GAKEAEAFGQALGEALEAPLDLGEGRAFRVRVRAGVALFPDDANTLSELLRRADQALREAKKAGK-RWTFY 443
PRK09776 770 EFGLLLPDcNVESARFIATRIISAINDYRFPWEGRVYRVGASAGITAIDDNNHQASEVMSQADIACYAAKNAGRgRVTVY 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 444 SLGLGEAVRERREVL--AGLEKALAEGELRLYGQPIVDLATGRPAGVEVL-LR-WARGEEVVPASRFIPVAEEAGLIPEL 519
PRK09776 850 EPQQAAAHSERRELSlaEQWRSMLEENQLMLQAQEIASPRIPEARNLWLIsLRlWDCEGEIIDEGAFRPAAEDPALMHAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 520 DLYVLRALAQ----------MTTALPLHVN-LSPQTLLDERL-LLGLAPLKGRNLRLELTEHALASPGAEAR--LKELSC 585
PRK09776 930 DRWVIHELFQqgaravaskgLSIAIPLSVAsLSSATLLPFLLeQLENSPLPPRLLHLEITETALLNHAEAASrlVQKLRL 1009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 586 MGFPVVLDDFGQGYASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVG 665
PRK09776 1010 AGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEMLVSIINGIAQRLGMKTIAGPVELPLTLDTLSGIG 1089
|
410
....*....|....*....
gi 46198730 666 YSLGQGYLWGRPAPLEEVL 684
PRK09776 1090 VDLAQGYVIGRPQPLDLLL 1108
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
2e-33 |
139.13 |
55.45 |
14,338,281,29,368,310,9,377,322,38,417,360,21,438,382,58,496,442,8,505,450,19,524,473,4,528,480,32,560,518,10,570,529,4,574,534,31,605,568,18,626,586,56 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 339 DALLARTSRRLQALLPREGRLYRLEGGEFlALLPGGAKE---AEAFGQALGEALEAPLDLGEGRAFRVRVRAGVALFPDD 415
PRK13561 282 EILLLTLVEKLKSVLSPRMVLAQISGYDF-AIIANGVKEpwhAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 416 anTLSELLRRADQALREAKKAGK-RWTFYSLGLGEAVRERREVLAGLEKALAEGELRLYGQPIVDLATGRPAGVEVLLRW 494
PRK13561 361 --TAEQLYSRAVSAAFTARRKGKnQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 495 AR--GEEVVPASrFIPVAEEAGLIPELDLYVL----RALA---QMTTALPLHVNLSPQTLLDERLLLGLAPLKGR----- 560
PRK13561 439 QQpdGSWDLPDG-LIDRIESCGLMVTVGHWVLeescRLLAawqERGIMLPLSVNLSALQLMHPNMVADMLELLTRyriqp 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 561 -NLRLELTEHA-LASP-GAEARLKELSCMGFPVVLDDFGQGYASLRLL---VGLPFSMAKVDRGFVGGIgldPKAEAALK 634
PRK13561 518 gTLILEVTESRrIDDPhAAVAILRPLRNAGVRIALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGL---PEDSSMVA 594
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 46198730 635 AVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRPAPLEE 682
PRK13561 595 AIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPLPIEI 642
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
5e-30 |
128.25 |
46.91 |
8,451,262,12,467,274,27,494,304,4,500,308,28,528,340,7,535,351,13,548,370,34,582,405,100 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 452 RERREVLAGLEKalaeGELRLYGQPIVDLATGRPAGVEVLLRW---ARGEevVPASRFIPVAEEAGLIPELDLYVLRALA 528
PRK10551 263 RPGREILTAIKR----EQFYVVYQPVVDTQTLRVTGLEVLLRWrhpTAGE--IPPDAFINYAEAQKLIVPLTQHLFELIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 529 ----QMTTALP----LHVNLSPQTLLDE------RLLLGLAPLKGRNLRLELTEHALASPGAEARLKE-LSCMGFPVVLD 593
PRK10551 337 rdaaELQKVLPvgakLGINIAPAHLHSDsfkadvQRLLASLPADHFQIVLEITERDMLQEEEALKLFAwLHSQGIEIAID 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 594 DFGQGYASLRLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYL 673
PRK10551 417 DFGTGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYW 496
|
....*....
gi 46198730 674 WGRPAPLEE 682
PRK10551 497 ISRPLPLDD 505
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
4e-24 |
108.25 |
38.87 |
10,416,432,26,442,459,54,496,515,6,503,521,21,524,546,8,532,557,25,557,588,22,579,612,26,605,641,18,626,659,56 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 417 NTLSELLRRADQALREAKKAGKRWTF-YSLGLGEAVRERREVLAGLEKALAEGELRLYGQPIVDLATGRPAGVEVLLRWA 495
PRK11829 433 DTAESMMRNASTAMMAAHHEGRNQIMvFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWC 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 496 R--GEEVVPaSRFIPVAEEAGLIPELDLYVL----RALAQMTT---ALPLHVNLSPQTLLDERLLLGLAPL------KGR 560
PRK11829 513 QpdGSYVLP-SGFVHFAEEEGMMVPLGNWVLeeacRILADWKArgvSLPLSVNISGLQVQNKQFLPHLKTLishyhiDPQ 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 561 NLRLELTEHALASPGAEAR--LKELSCMGFPVVLDDFGQGYASLRLL---VGLPFSMAKVDRGFVGGIgldPKAEAALKA 635
PRK11829 592 QLLLEITETAQIQDLDEALrlLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARI 668
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 46198730 636 VLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRPAPLEE 682
PRK11829 669 ISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE 715
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
2e-13 |
72.61 |
58.72 |
15,320,264,35,355,301,18,373,320,18,391,343,19,417,362,20,437,389,11,449,400,5,458,405,21,480,426,20,500,447,20,520,471,11,531,483,20,559,503,11,570,520,8,578,539,102 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 321 LDLVDLYEVNEAYGREAGDALLARTSRRLQALLPR--EGRLYRLEGGEFLALLPG-GAKEAEAFGQALGEALEA-----P 392
PRK11059 265 IRLPDFDLLQEELGESQVDELLFELINLLSTFVQRypGALLARYSRSDFAVLLPHrSLKEADSLASQLLKAVDSlpppkM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 393 LDLGEGRAFRVRVRAGVAlfpddanTLSELLRRADQALREAKKAG-------KRWTFYSLGLGeAVRERrevlAGLEKAL 465
PRK11059 345 LDRDDFLHIGIAAYRSGQ-------STEQVMEEAEMALRSAQLQGgnswfmyDKAQDPEKGRG-SVRWR----TLLEQAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 466 AEGELRLYGQPIVDlATGRPAGVEVLLRWARGEEV-VPASRFIPVAEEAGLIPELD----LYVLRALAQMT-TALPLHVN 539
PRK11059 413 VRGGPRLYQQPVVT-RDGQVHHRELMCRIRDGQGNeVRAAEFMPMVLQCGLSEQYDrqviERVLPLLSYWPeESQNLSIN 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 540 LSPQTLLDERLLlglaplkgRNLRLELTEHA------LASPGAEA-----------RLKELSCMGFPVVLDDFGQGYASL 602
PRK11059 492 LSVDSLLSRAFQ--------RWLRDTLLQCErsqrkrLIFELAEAdvvqhidrlrpVLRMLRGLGCRLAVDQAGLTVVST 563
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46198730 603 RLLVGLPFSMAKVDRGFVGGIGLDPKAEAALKAVLALSRELEIALVAEGVEREDQWAWLRSVGYSLGQGYLWGRPAPL 680
PRK11059 564 SYIKELNVELIKLHPSLVRNIHQRTENQLFVRSLVGACAGTETQVFAEGVESREEWQTLQILGVSGGQGDFFASPQPL 641
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
2e-08 |
56.64 |
51.19 |
5,293,132,22,315,159,60,375,220,16,391,237,24,417,261,21 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 294 DPLTGLPNRRRLEEDFRLLRGR-----WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGGEFL 368
PRK09894 133 DVLTGLPGRRVLDESFDHQLRNreplnLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEEFI 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46198730 369 ALLPGGA-KEAEAFGQALGEALEA-PLDLGEGRAFRVRVRAGVALFPDDanTLSELLRRADQALREAKKAGK 438
PRK09894 213 IILKAATdEEACRAGERIRQLIANqAITHSEGRINITATFGVTRAFPEE--PLDEVIGRADRAMYEGKQAGR 282
|
|
|
|
|
|
|
-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 |
4e-07 |
51.84 |
35.86 |
5,292,271,23,315,301,62,377,368,10,388,378,27,416,405,22 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 293 HDPLTGLPNRRRLEEDFRLLRGR-------WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGG 365
COG3706 272 VDGLTGLFNRRYFDEHLADLWKRalregrpLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGE 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46198730 366 EFLALLPGGAKE-----AEAFGQALGEaLEAPLDLGEGRAFRVRVRAGVALFPDDaNTLSELLRRADQALREAKKAGK 438
COG3706 352 EFAVVLPDTDLEaaiaiAERIRQKINE-LPFVHELSREPLEVTISIGVAEGKPGE-DSIEELLKRADKALYKAKASGR 427
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
5e-05 |
45.01 |
27.27 |
3,292,249,23,315,278,65,380,345,15 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 293 HDPLTGLPNRRRLEEDFRLLRGR------WALCRLDLVDLYEVNEAYGREAGDALLARTSRRLQALLPREGRLYRLEGGE 366
PRK09966 250 HDPLTGLANRAAFRSGINTLMNNsdarktSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDE 329
|
90 100 110
....*....|....*....|....*....|.
gi 46198730 367 FLALLPGGAKEAEA--FGQALGEALEAPLDL 395
PRK09966 330 FAMVLYDVQSESEVqqICSALTQIFNLPFDL 360
|
|
|
|
|
|
|
-1 |
| 130876 |
TIGR01817 |
nifA |
Nif-specific regulatory protein |
Nif-specific regulatory protein |
false |
true |
false |
534 |
5e-04 |
41.62 |
15.36 |
3,193,71,28,222,99,30,252,130,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46198730 194 GQGPTGRALRSGRPQVLRSVEEDPRYAPwRERAQVFGFASSAAFPLRVEGRVWGSLNVY-APEEDAFDEEEVRLLEDLAR 272
TIGR01817 72 GEGAIGQIVATGNSLVVPDVAAEPLFLD-RLSLYDPGPVPFIGVPIKADSETIGVLAADrDFRSRERLEEEVRFLEMVAN 150
|
...
gi 46198730 273 LIG 275
TIGR01817 151 LIG 153
|
|
|
|
|
|
|
-1 |
|