| 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 |
2e-75 |
279.41 |
98.75 |
2,615,0,79,700,79,158 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 616 SDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVLRHACAHVGGWQQh 695
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 696 verkpGEPPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETMMLQGSDRVLRTLDLLSGFGVRLAMDDFG 775
cd01948 80 -----GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 776 TGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFAR 855
cd01948 155 TGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSR 234
|
...
gi 117929112 856 PVP 858
cd01948 235 PLP 237
|
|
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-52 |
202.43 |
100.00 |
3,441,0,89,531,89,38,569,128,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 442 HDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLRPSDQPARLGGD 521
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117929112 522 EFAVIIEDAlSTQAAERIAARITEQLRAPISVHGCELHIRASIGIATS-QGVQTADELLRNADLAMYMAKADGKGRYR 598
cd01949 81 EFAILLPGT-DLEEAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYpEDGEDLEELLRRADKALYQAKRSGRNRVV 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 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
1e-74 |
276.79 |
98.76 |
2,614,0,82,702,82,156 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 615 KSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVLRHACAHVGGWQQ 694
smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 695 HVerkpgePPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETMMLQGSDRVLRTLDLLSGFGVRLAMDDF 774
smart00052 81 QG------PPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 775 GTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFA 854
smart00052 155 GTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFS 234
|
....
gi 117929112 855 RPVP 858
smart00052 235 RPLP 238
|
|
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-74 |
274.12 |
98.83 |
2,610,0,85,702,85,168 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 611 RHQLKSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVLRHACAHVG 690
COG2200 1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 691 GWQQHverkpgePPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETMMLQGSDRVLRTLDLLSGFGVRLA 770
COG2200 81 TWPRA-------GPLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 771 MDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEGVETAQQARELERLGCRLGQG 850
COG2200 154 LDDFGTGYSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQG 233
|
250 260
....*....|....*....|
gi 117929112 851 YHFARPVPSAGIELLLQRYA 870
COG2200 234 YLFSRPLPADALDALLSSSQ 253
|
|
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 |
3e-59 |
225.76 |
100.00 |
5,614,0,89,706,89,19,726,108,24,751,132,58,810,190,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 615 KSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVLRHACAHVGGWQQ 694
pfam00563 1 EQALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 695 HVERKPGEPpfaVAVNLSPAQFAQPDLVAQIdEAVEAAGIDPNSLILEITETMMLQgSDRVLRTLDLLSGFGVRLAMDDF 774
pfam00563 81 NALLPPDLP---LSVNLSPASLLDPSFLEAL-LALKQGGLPPSRLVLEITESDLDE-DLRLLEALARLRSLGFRLALDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 775 GTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSpFVRAMIELGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFA 854
pfam00563 156 GTGYSSLSYLSRLPPDYIKIDRSFIKDLSDPESRA-LLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFS 234
|
..
gi 117929112 855 RP 856
pfam00563 235 KP 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 |
5e-47 |
184.76 |
100.00 |
3,437,0,93,531,93,36,567,130,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 438 QLAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLRPSDQPAR 517
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 518 LGGDEFAVIIEDAlSTQAAERIAARITEQLRAPISVHGCELHIRASIGIA-TSQGVQTADELLRNADLAMYMAKADGKGR 596
smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAaYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 117929112 597 YRWF 600
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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
1e-44 |
177.44 |
100.00 |
3,439,0,98,537,100,32,569,133,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 440 AFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLRPSDQPARLG 519
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 520 GDEFAVIIEDALSTQAAE--RIAARITEQLRAPISVHGCELHIRASIGIATS-QGVQTADELLRNADLAMYMAKADGKGR 596
pfam00990 81 GDEFAILLPDTSLEGAQElaERIRRLLAALKIPHTLSGLPLYVTISIGIAAYpNDGEDAEDLLKRADQALYQAKNQGRNR 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 |
| 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 |
4e-44 |
175.31 |
100.00 |
3,420,0,110,531,110,38,569,150,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 421 RLEQSLAQLRELEQKLTQLAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCA 500
COG2199 1 ALLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 501 VAERITGCLRPSDQPARLGGDEFAVIIEDAlSTQAAERIAARITEQLRAPISVHGCELHIRASIGIATS--QGVQTADEL 578
COG2199 81 VARRLRSNLREGDLVARLGGDEFAVLLPGT-SLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYpeDGSDDAELL 159
|
170 180
....*....|....*....|..
gi 117929112 579 LRNADLAMYMAKADGKGRYRWF 600
COG2199 160 LRRADLALYRAKRAGRNRVVVF 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 |
2e-37 |
152.88 |
100.00 |
5,438,0,98,537,98,12,549,111,8,557,120,14,571,135,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 439 LAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLRPSDQPARL 518
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 519 GGDEFAVIIEDALSTQAAeRIAARITEQLRA-PISVHGCE-LHIRASIGIATSQG-VQTADELLRNADLAMYMAKADGKG 595
TIGR00254 81 GGEEFVVILPGTPLEDAL-SKAERLRDAINSkPIEVAGSEtLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRN 159
|
....*.
gi 117929112 596 RYRWFR 601
TIGR00254 160 RVVVAD 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 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
2e-06 |
50.09 |
92.16 |
12,618,16,7,625,28,9,636,37,3,639,41,15,658,56,22,680,79,20,704,99,8,712,108,5,717,116,9,726,132,19,764,151,2,767,153,98 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 619 ERAAERG-----EFQVHYQPIvdLRT-GRPVAAEALVRWVHPerglLFPETFISEAENSGIINEIGRL-VLRHACAHVGG 691
PRK11596 17 ESLQERRfwlqcERAYTFQPI--YRTcGRLMAVELLTVVTHP----SNPSQRLSPDRYFAEITVSHRLdVVKEQLDLLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 692 WQQHVERKPgeppFAVAVNLS-PAQFA---QPDLVAQID-------EAVEAAGIDPNSLILEITEtmmlqgsdrvlrtld 760
PRK11596 91 KADFFVRHG----LLASVNIDgPTLIAlrqQPKILRLIErlpwlrfELVEHIRLPKDSTFASMCE--------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 761 llsgFGvRLAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEGVETAQQAREL 840
PRK11596 152 ----FG-PLWLDDFGTGMANFSALSEVRYDYIKVARELFVMLRQSPEGRTLFSQLLHLMNRYCRGVIVEGVETPEEWRDV 226
|
250 260
....*....|....*....|....*
gi 117929112 841 ERLGCRLGQGYHFARPVPSAGIELL 865
PRK11596 227 QRSPAFAAQGYFLSRPAPFDTLETL 251
|
|
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 |
| 128379 |
smart00065 |
GAF |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
true |
false |
false |
149 |
3e-06 |
49.30 |
86.58 |
4,288,19,28,319,47,20,344,67,44,389,111,37 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 289 DGGRLLRIRLDGHGEPRLMEAVTDPVVLawwERMTTANGPLVLQYAAKRPRkqrflARLFHDSADTSPSLEHEYLEHERV 368
smart00065 20 DRVLIYLVDEDDRGELVLVAADGLTLPL---LGLRYPLGEGLAGRVAETGR-----PLNIPDVEADPVFALDLLGRYQGV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 117929112 369 RNAIVAPLRGETRPIGMLMVgDRPGEGASFGGQDVRLFEALANHVSVALENGRLEQSL 426
smart00065 92 RSFLAVPLVADGELVGVLAL-HNKDSPRPFTEEDEELLQALANQLAIALANAQLYEEL 148
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 110584 |
pfam01590 |
GAF |
GAF domain |
GAF domain |
false |
false |
false |
153 |
7e-05 |
44.93 |
85.62 |
3,282,22,77,361,99,30,393,129,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 283 AIIAPPDGGRLLRIRLDGHGEPRLMEAVTDPVVLAWWERMTTANGPLVLQYAAKRPRKQRFLARLFHDSADTSPSLEheY 362
pfam01590 23 AILLADADGLLLYLVAGDGLSDIPLAARGLPLGGGVVGEVIAGGNPIVVPDVQDDPRFRDLTALAEELPAPVGCHEH--Y 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 117929112 363 LEHERVRNAIVAPLRGETRPIGMLMVGDRpgEGASFGGQDVRLFEALANHVSVAL 417
pfam01590 101 LRGLGIRSCLAVPLLGGGKLIGVLVLHST--SPRAFTEEELELLQALADQVAIAL 153
|
|
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 |
0.001 |
41.15 |
61.14 |
3,319,68,32,354,100,37,392,137,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 320 ERMTTANGPLVLQYAAKRPRKQRFLARLFHDSadtSPSLEHEYLEHERVRNAIVAPLRGETRPIGMLMVGDRpGEGASFG 399
COG2203 69 ELFGLVILPACLIGIALREGRPVVVEDILQDP---RFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDS-EPRRQWS 144
|
90 100 110
....*....|....*....|....*....|.
gi 117929112 400 GQDVRLFEALANHVSVALENGRLEQSLAQLR 430
COG2203 145 EEELELLEELAEQVAIAIERARLYEELQEAE 175
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
1e-94 |
342.86 |
65.01 |
8,429,226,37,468,263,62,532,325,4,536,330,33,569,364,68,638,432,54,697,486,4,702,490,167 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 430 RELEQKLTQLAFHDPLTGLANRALFSERLSQVLAKAKaeGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCL 509
PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDHAIAQAD--NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 510 RPSDQPARLGGDEFAVIIEDAlsTQAA-ERIAARITEQLRAPISVHGCELHIRASIGIATS-QGVQTADELLRNADLAMY 587
PRK10060 305 EEDQTLARLGGDEFLVLASHT--SQAAlEAMASRILTRLRLPFRIGLIEVYTGCSIGIALSpEHGDDSESLIRSADTAMY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 588 MAKADGKGRYRWFRPSMRTAVVSRHQLKSDLERAAERGEFQVHYQPIVDLrTGRPVAAEALVRWVHPERGLLFPETFISE 667
PRK10060 383 TAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 668 AENSGIINEIGRLVLRHACAHVGGWqqhveRKPGePPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETM 747
PRK10060 462 AEESGLIVPLGRWVILDVVRQAAKW-----RDKG-INLRVAVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESC 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 748 MLQGSDRVLRTLDLLSGFGVRLAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTL 827
PRK10060 536 LIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVI 615
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 117929112 828 AEGVETAQQARELERLGCRLGQGYHFARPVPSAGIELLLQRY 869
PRK10060 616 AEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRY 657
|
|
|
|
|
|
|
-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-91 |
332.76 |
64.86 |
5,421,209,106,528,315,14,542,330,27,569,358,123,701,481,158 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 422 LEQSLAQLRELEQKLTQLAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAV 501
COG5001 210 LTQRAEETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 502 AERITGCLRPSDQPARLGGDEFAVIIeDALSTQAAERIAAR-ITEQLRAPISVHGCELHIRASIGIATS-QGVQTADELL 579
COG5001 290 GRRLKAFDGAPILAARLGGDEFALII-PALEDDALRVAGARaLCESLQAPYDLRGVRVQVGASIGIAPFpSGADTSEQLF 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 580 RNADLAMYMAKADGKGRYRWFRPSMRTAVVSRHQLKSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLL 659
COG5001 369 ERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIGPV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 660 FPETFISEAENSGIINEIGRLVLRHACAHVGGWqqhverkpgEPPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSL 739
COG5001 449 PPDVFIGIAERSGQIVELTRLLLAKALREARAW---------PMDVRVSINLSARDLASMENVRRLLAIVSESCIAPHRL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 740 ILEITETMMLQGSDRVLRTLDLLSGFGVRLAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELG 819
COG5001 520 DFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLG 599
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 117929112 820 EALGLVTLAEGVETAQQARELERLGCRLGQGYHFARPVPS 859
COG5001 600 RNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMPA 639
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
1e-78 |
289.82 |
52.69 |
5,430,366,38,472,404,65,538,469,33,572,502,120,697,622,165 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 431 ELEQKLTQLAFHDPLTGLANRALFSERLSQVLAKAKAEgrtcAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLR 510
PRK11359 367 KSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 511 PSDQPARLGGDEFAVIIEDALSTQAAErIAARITEQLRAPISVHGCELHIRASIGIATSQGvQTADELLRNADLAMYMAK 590
PRK11359 443 PDQYLCRIEGTQFVLVSLENDVSNITQ-IADELRNVVSKPIMIDDKPFPLTLSIGISYDVG-KNRDYLLSTAHNAMDYIR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 591 ADGKGRYRWFRPSMRTAVVSRHQLKSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAEN 670
PRK11359 521 KNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEE 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 671 SGIINEIGRLVLRHACAHVGGWqqhveRKPGEPPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETMMLQ 750
PRK11359 601 IGEIENIGRWVIAEACRQLAEW-----RSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMME 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 751 GSDRVLRTLDLLSGFGVRLAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEG 830
PRK11359 676 HDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEG 755
|
410 420 430
....*....|....*....|....*....|..
gi 117929112 831 VETAQQARELERLGCRLGQGYHFARPVPSAGI 862
PRK11359 756 VETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
4e-67 |
251.61 |
66.05 |
6,420,214,11,434,225,32,470,257,230,706,487,80,786,570,14,803,584,60 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 421 RLEQSLAQLREleqKLTQLAFHDPLTGLANRALFSERLSQVLAKAKaegrTCAVLFIDLDDFKTVNDTLGHDAGDELLCA 500
PRK13561 215 LNQQLLQRHYE---EQNENAMRFPVSDLPNKALLMALLEQVVARKQ----TTALMIITCETLRDTAGVLKEAQREILLLT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 501 VAERITGCLRPSDQPARLGGDEFAVIIEDALSTQAAERIAARITEQLRAPISVHGCELHIRASIGIATSQGVQTADELLR 580
PRK13561 288 LVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 581 NADLAMYMAKADGKGRYRWFRPSMRTAVVSRHQLKSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLF 660
PRK13561 368 RAVSAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 661 PETFISEAENSGIINEIGRLVLRHACAHVGGWQQHVERKPgeppfaVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLI 740
PRK13561 448 PDGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLP------LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 741 LEITETMMLQGSDRVLRTLDLLSGFGVRLAMDDFGTGYASLASLRK---LPIDIIKIAKTFTDditGNEEKSPFVRAMIE 817
PRK13561 522 LEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVD---GLPEDSSMVAAIIM 598
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 117929112 818 LGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFARPVPSAGIE 863
PRK13561 599 LAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPLPIEIFE 644
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
2e-59 |
226.51 |
38.71 |
7,423,671,107,531,778,18,549,797,17,566,815,51,617,868,31,648,900,36,691,936,167 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 424 QSLAQLRELEQKLTQLAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAE 503
PRK09776 672 QDVTESRAMLRQLSYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELAS 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 504 RITGCLRPSDQPARLGGDEFAVIIEDAlSTQAAERIAARITEQLRA-PISVHGCELHIRASIGI-ATSQGVQTADELLRN 581
PRK09776 752 LMLSMLRSSDVLARLGGDEFGLLLPDC-NVESARFIATRIISAINDyRFPWEGRVYRVGASAGItAIDDNNHQASEVMSQ 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 582 ADLAMYMAKADGKGRYRWFRPSMRTAVVSRHQLKSD--LERAAERGEFQVHYQPIVDLRTGRPVAAEAL-VRWVHPERGL 658
PRK09776 831 ADIACYAAKNAGRGRVTVYEPQQAAAHSERRELSLAeqWRSMLEENQLMLQAQEIASPRIPEARNLWLIsLRLWDCEGEI 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 659 LFPETFISEAENSGIINEIGRLVLRHacahvggWQQHVERKPGEPPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNS 738
PRK09776 911 IDEGAFRPAAEDPALMHALDRWVIHE-------LFQQGARAVASKGLSIAIPLSVASLSSATLLPFLLEQLENSPLPPRL 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 739 LILEITETMMLQGSDRVLRTLDLLSGFGVRLAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIEL 818
PRK09776 984 LHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEMLVSIINGI 1063
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 117929112 819 GEALGLVTLAEGVETAQQARELERLGCRLGQGYHFARPVP 858
PRK09776 1064 AQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRPQP 1103
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
6e-54 |
208.01 |
56.87 |
6,443,303,28,472,331,101,573,433,127,706,560,76,782,639,21,806,660,57 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 444 PLTGLANRALFSERLSQVLAKAKAEGRTcAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLRPSDQPARLGGDEF 523
PRK11829 304 PVTELPNRSLFISLLEKEIASSTRTDHF-HLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 524 AVIIEDALSTQAAERIAARITEQLRAPISVHGCELHIRASIGIATSQGVQ-TADELLRNADLAMYMAKADGKGRYRWFRP 602
PRK11829 383 AVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQdTAESMMRNASTAMMAAHHEGRNQIMVFEP 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 603 SMRTAVVSRHQLKSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVL 682
PRK11829 463 HLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 683 RHACAHVGGWQQHVERKPgeppfaVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETMMLQGSDRVLRTLDLL 762
PRK11829 543 EEACRILADWKARGVSLP------LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLREL 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 763 SGFGVRLAMDDFGTGYASLA---SLRKLPIDIIKIAKTFTDDITgneEKSPFVRAMIELGEALGLVTLAEGVETAQQARE 839
PRK11829 617 QGLGLLIALDDFGIGYSSLRylnHLKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQW 693
|
410 420
....*....|....*....|....
gi 117929112 840 LERLGCRLGQGYHFARPVPSAGIE 863
PRK11829 694 LLEHGIQCGQGFLFSPPLPRAEFE 717
|
|
|
|
|
|
|
-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 |
6e-50 |
194.41 |
48.85 |
6,610,265,82,692,348,3,702,351,43,745,395,11,758,406,100,861,506,15 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 611 RHQLKSDLERAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVLRHACAHVG 690
COG4943 266 YLSPRRRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLG 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 691 GW-QQHverkpgePPFAVAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITE-TMMLQGSDRVLrtLDLLSGFGVR 768
COG4943 346 DLlRQH-------RDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTErTFADPKKMTPI--ILRLREAGHE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 769 LAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEGVETAQQARELERLGCRLG 848
COG4943 417 IYIDDFGTGYSNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYG 496
|
250 260
....*....|....*....|....*...
gi 117929112 849 QGYHFARPVPsagIELLLQRYAEQQAGL 876
COG4943 497 QGWLFSKALP---AQAFLDWAEQQPARE 521
|
|
|
|
|
|
|
-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 |
1e-36 |
150.07 |
53.56 |
7,378,202,19,402,221,9,411,231,15,426,256,103,530,359,25,555,387,15,570,403,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 379 ETRPIGMLMVGDRPGEGASfggqdVRLFEALAN-HVSVALENGRLEQSL----------AQLRELEQKLTQLAFHDPLTG 447
COG3706 203 RTRDIPIILLSSKDDDELV-----VRAFELGVNdYITKPIEEGELRARLrrqlrrkryeRQLRESLERLQELALVDGLTG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 448 LANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLRPSDQPARLGGDEFAVII 527
COG3706 278 LFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVL 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117929112 528 EDaLSTQAAERIAARITEQLRAPISVHG---CELHIRASIGIATSQ-GVQTADELLRNADLAMYMAKADGKGRYRWFRP 602
COG3706 358 PD-TDLEAAIAIAERIRQKINELPFVHElsrEPLEVTISIGVAEGKpGEDSIEELLKRADKALYKAKASGRNRVVVKRA 435
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
3e-34 |
142.37 |
37.64 |
8,427,279,4,431,284,6,438,290,88,526,383,7,535,390,10,548,400,9,557,411,14,571,426,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 428 QLRE-LEQKLTqLAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERIT 506
PRK09581 280 ALRQnLEQSIE-MAVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 507 GCLRPSDQPARLGGDEFAVI-----IEDALSTqaAERIAARITEqlrAPISVHGCE--LHIRASIGIATSQG-VQTADEL 578
PRK09581 359 KNIRGTDLIARYGGEEFVVVmpdtdIEVAIAV--AERIRRKIAE---EPFAISDGKerLNVTVSIGVAELRPsGESIEAL 433
|
170
....*....|....*...
gi 117929112 579 LRNADLAMYMAKADGKGR 596
PRK09581 434 IKRADKALYEAKNTGRNR 451
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
7e-34 |
141.34 |
44.98 |
4,619,269,77,702,346,4,706,351,47,754,398,104 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 620 RAAERGEFQVHYQPIVDLRTGRPVAAEALVRWVHPERGLLFPETFISEAENSGIINEIGRLVLRHACAHVGGWQQHVerk 699
PRK10551 270 TAIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVL--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 700 pgePPFA-VAVNLSPAQFAQPDLVAQIDEAVEAAGIDPNSLILEITETMMLQGSDrVLRTLDLLSGFGVRLAMDDFGTGY 778
PRK10551 347 ---PVGAkLGINIAPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMLQEEE-ALKLFAWLHSQGIEIAIDDFGTGH 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 779 ASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVRAMIELGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFARPVP 858
PRK10551 423 SALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISRPLP 502
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
7e-30 |
127.69 |
64.33 |
13,439,227,71,510,300,19,530,319,13,546,332,11,557,350,2,563,352,22,585,387,7,592,397,7,604,404,3,617,407,19,637,426,61,706,487,19,725,507,133 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 440 AFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAERITGCLR--PSDQPAR 517
PRK11059 228 AFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFELINLLSTFVQryPGALLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 518 LGGDEFAVIIEDaLSTQAAERIAARIteqLRAPISVHGCE-------LHirasIGIATSQGVQTADELLRNADLA----- 585
PRK11059 308 YSRSDFAVLLPH-RSLKEADSLASQL---LKAVDSLPPPKmldrddfLH----IGIAAYRSGQSTEQVMEEAEMAlrsaq 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 586 --------MYMAKAD---GKGRYRWfrpsmRTAvvsrhqlksdLERAAERGEFQVHYQPIVDlRTGRPVAAEALVRWVHP 654
PRK11059 380 lqggnswfMYDKAQDpekGRGSVRW-----RTL----------LEQALVRGGPRLYQQPVVT-RDGQVHHRELMCRIRDG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 655 ERGLLFPETFISEAENSGIINEIGRLVLRHACAHVGGWQQHVERkpgeppfaVAVNLSPAQFAQPDLVAQI-DEAVEAAG 733
PRK11059 444 QGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLSYWPEESQN--------LSINLSVDSLLSRAFQRWLrDTLLQCER 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 734 IDPNSLILEITETMMLQGSDRVLRTLDLLSGFGVRLAMDDFGTGYASLASLRKLPIDIIKIAKTFTDDITGNEEKSPFVR 813
PRK11059 516 SQRKRLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHQRTENQLFVR 595
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 117929112 814 AMIELGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFARPVP 858
PRK11059 596 SLVGACAGTETQVFAEGVESREEWQTLQILGVSGGQGDFFASPQP 640
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
1e-27 |
120.97 |
61.09 |
6,415,105,10,426,115,12,438,128,27,467,155,68,535,226,11,549,237,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 416 ALENGRLEQSlAQLRELEQKLTQ-LAFHDPLTGLANRALFSERLSQVLAKAkaEGRTCAVLFIDLDDFKTVNDTLGHDAG 494
PRK09894 106 AFQEGLLSFT-AALTDYKIYLLTiRSNMDVLTGLPGRRVLDESFDHQLRNR--EPLNLYLALLDIDRFKLVNDTYGHLIG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 495 DELLCAVAERITGCLRPSDQPARLGGDEFAVIIEDALSTQA---AERIAARITEQlraPISVHGCELHIRASIGIATSQG 571
PRK09894 183 DVVLRTLATYLASWTRPYETVYRYGGEEFIIILKAATDEEAcraGERIRQLIANQ---AITHSEGRINITATFGVTRAFP 259
|
170 180
....*....|....*....|....*
gi 117929112 572 VQTADELLRNADLAMYMAKADGKGR 596
PRK09894 260 EEPLDEVIGRADRAMYEGKQAGRNR 284
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
4e-25 |
112.03 |
40.54 |
5,427,233,3,431,236,8,439,247,29,469,276,85,554,362,36 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 428 QLReLEQKLTQL---AFHDPLTGLANRALFSERLSQVLAKAKAEgRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAER 504
PRK09966 234 QLR-LQAKNAQLlrtALHDPLTGLANRAAFRSGINTLMNNSDAR-KTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 505 ITGCLRPSDQPARLGGDEFAVIIEDALSTQAAERIAARITEQLRAPISVH-GCELHIRASIGIATSQGVQTADELLRNAD 583
PRK09966 312 LAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHASAEKLQELAD 391
|
....*..
gi 117929112 584 LAMYMAK 590
PRK09966 392 HNMYQAK 398
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
1e-20 |
96.89 |
46.63 |
5,423,193,105,531,298,10,541,310,26,567,338,3,571,341,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 424 QSLAQLRELEQKLTQLAFHDPLTGLANRALFSERLSQVLAKAKAEGRTCAVLFIDLDDFKTVNDTLGHDAGDELLCAVAE 503
PRK10245 194 QTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 504 RITGCLRPSDQPARLGGDEFAVIIEdalSTQAAERIAA--RITEQLRAPISVHGCELHIRASIGIA--TSQgVQTADELL 579
PRK10245 274 QLQITLRGSDVIGRFGGDEFAVIMS---GTPAESAITAmlRVHEGLNTLRLPNAPQVTLRISVGVAplNPQ-MSHYREWL 349
|
170
....*....|....*..
gi 117929112 580 RNADLAMYMAKADGKGR 596
PRK10245 350 KSADLALYKAKKAGRNR 366
|
|
|
|
|
|
|
-1 |
| 33240 |
COG3434 |
COG3434 |
Predicted signal transduction protein containing EAL and modified HD-GYP domains [Signal transduction mechanisms] |
Predicted signal transduction protein containing EAL and modified HD-GYP domains [... |
false |
true |
false |
407 |
7e-06 |
48.35 |
27.27 |
6,735,82,12,749,94,25,777,119,9,786,130,2,788,133,13,809,146,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117929112 736 PNSLILEITETMmlQGSDRVLRTLDLLSGFGVRLAMDDFgtgYASLASLRK--LP-IDIIKIAKTFTDDitgneeksPFV 812
COG3434 83 PDKVVIEILEDC--PPTEKLLSAIKELKQKGYLLALDDF---IFSNVSEWKplLPlSDIVKIDFKRVTF--------DKA 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 117929112 813 RAMIELGEALGLVTLAEGVETAQQARELERLGCRLGQGYHFARP 856
COG3434 150 RLFDRDLGYINKKFLAEKVETEEEFEQAKKAGFDLFQGYFFSKP 193
|
|
|
|
|
|
|
-1 |
|