| 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-82 |
302.13 |
99.58 |
2,383,0,77,463,77,162 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 384 EDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHRVAWtpr 463
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 464 LHCRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDEEAGTLAVLRALRDLGVRIALDDFGTGY 543
cd01948 78 QAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 544 SALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKPMP 623
cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
..
gi 117928627 624 AD 625
cd01948 238 AE 239
|
|
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 |
5e-42 |
167.76 |
100.00 |
2,208,0,88,297,88,69 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 209 HDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARIGGD 288
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117928627 289 EFGVLVTGlAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNTGKGRCV 366
cd01949 81 EFAILLPG-TDLEEAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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-85 |
312.61 |
100.00 |
2,382,0,82,467,82,159 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 383 EEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHRVAWTP 462
smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 463 RLhcrQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDEEAGTLAVLRALRDLGVRIALDDFGTG 542
smart00052 81 QG---PPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 543 YSALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKPM 622
smart00052 158 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 237
|
....
gi 117928627 623 PADT 626
smart00052 238 PLDD 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 |
3e-77 |
284.91 |
98.05 |
2,381,3,79,464,82,172 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 382 LEEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHRVAWt 461
COG2200 4 LERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRTW- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 462 prlHCRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDEEAGTLAVLRALRDLGVRIALDDFGT 541
COG2200 83 ---PRAGPLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 542 GYSALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKP 621
COG2200 160 GYSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRP 239
|
250
....*....|....*
gi 117928627 622 MPADTLPAHCPSSAS 636
COG2200 240 LPADALDALLSSSQS 254
|
|
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-64 |
241.17 |
100.00 |
4,382,0,108,491,108,22,514,130,55,570,185,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 383 EEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHRVAWTP 462
pfam00563 1 EQALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 463 RLHCRQDFCVSVNVSVRQLAEPGFVDVVtDALAASGVPPEVLVLEMTESVFiDEEAGTLAVLRALRDLGVRIALDDFGTG 542
pfam00563 81 NALLPPDLPLSVNLSPASLLDPSFLEAL-LALKQGGLPPSRLVLEITESDL-DEDLRLLEALARLRSLGFRLALDDFGTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117928627 543 YSALSYLRRFPVDILKLDRSFIAGLLGtAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKP 621
pfam00563 159 YSSLSYLSRLPPDYIKIDRSFIKDLSD-PESRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 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 |
3e-37 |
152.02 |
100.00 |
2,204,0,92,297,92,71 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 205 HLASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVAR 284
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 285 IGGDEFGVLVTGlAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNTGKGR 364
smart00267 81 LGGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 117928627 365 CVVF 368
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 |
| 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 |
7e-35 |
144.11 |
97.79 |
3,191,4,105,297,109,48,345,158,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 192 AVHARRRAETARYHLASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQR 271
COG2199 5 LLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVARR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 272 MTAIVRPTDTVARIGGDEFGVLVTGlAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAE-LLADA 350
COG2199 85 LRSNLREGDLVARLGGDEFAVLLPG-TSLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDDAElLLRRA 163
|
170
....*....|....*...
gi 117928627 351 DLAMTEAKNTGKGRCVVF 368
COG2199 164 DLALYRAKRAGRNRVVVF 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 |
9e-35 |
143.54 |
100.00 |
2,206,0,90,296,92,68 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 207 ASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARIG 286
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 287 GDEFGVLVTG--LAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNTGKGR 364
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 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
3e-29 |
125.53 |
99.39 |
4,205,0,91,297,91,19,316,111,4,320,116,48 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 206 LASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARI 285
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 286 GGDEFGVLVTGlAAPNEAEAIALRLRDAFRT-PFAV-DGRSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNTGKG 363
TIGR00254 81 GGEEFVVILPG-TPLEDALSKAERLRDAINSkPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 117928627 364 RCVVF 368
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 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
8e-05 |
44.31 |
37.25 |
3,532,153,10,542,166,8,553,174,74 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 533 RIALDDFGTG---YSALSYLRrfpVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLG 609
PRK11596 154 PLWLDDFGTGmanFSALSEVR---YDYIKVARELFVMLRQSPEGRTLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSP 230
|
90
....*....|....*...
gi 117928627 610 CRLGQGFLLQKPMPADTL 627
PRK11596 231 AFAAQGYFLSRPAPFDTL 248
|
|
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 |
| 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 |
8e-05 |
44.11 |
89.32 |
2,21,3,44,65,52,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 22 GMALLDVAGRFRAVNDAFAELVGVEADALIGSEETTFIRPDDRH-----WADWGIGGEPQRLQVRMCRADGTEIHVIRIL 96
cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREelrerLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83
|
90
....*....|..
gi 117928627 97 TAAADEEPFVLG 108
cd00130 84 TPIRDEGGEVIG 95
|
|
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 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
3e-92 |
334.77 |
63.95 |
6,196,226,33,231,259,69,301,328,104,406,432,57,463,490,4,471,494,156 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 197 RRAETARYHLASHDALTGLVNRTTFAARVADAVgqAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIV 276
PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDHAI--AQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 277 RPTDTVARIGGDEFGVLVTGLAAPnEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTE 356
PRK10060 305 EEDQTLARLGGDEFLVLASHTSQA-ALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALSPEHGDDSESLIRSADTAMYT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 357 AKNTGKGRCVVFRPALRRAAAQRIALEEDLRAAVEAGAFRLDFQPIVELaTGMWVGAEALLRWPHPTRGLVPPLDFIPLA 436
PRK10060 384 AKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 437 EDSGLVVPLGEWVLRTALQHRVAWTPR-LHCRqdfcVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFID 515
PRK10060 463 EESGLIVPLGRWVILDVVRQAAKWRDKgINLR----VAVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESCLIE 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 516 EEAGTLAVLRALRDLGVRIALDDFGTGYSALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEG 595
PRK10060 539 NEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEG 618
|
410 420 430
....*....|....*....|....*....|..
gi 117928627 596 IETYDQLEILRQLGCRLGQGFLLQKPMPADTL 627
PRK10060 619 VETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
|
|
|
|
|
-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-78 |
288.08 |
63.80 |
2,196,217,269,471,486,154 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 197 RRAETARYHLASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIV 276
COG5001 218 RRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 277 RPTDTVARIGGDEFGVLVTGLAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTE 356
COG5001 298 GAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQLFERADYALYH 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 357 AKNTGKGRCVVFRPALRRAAAQRIALEEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLA 436
COG5001 378 AKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIGPVPPDVFIGIA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 437 EDSGLVVPLGEWVLRTALQHRVAWTPRLHcrqdfcVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDE 516
COG5001 458 ERSGQIVELTRLLLAKALREARAWPMDVR------VSINLSARDLASMENVRRLLAIVSESCIAPHRLDFEITETAIVCD 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 517 EAGTLAVLRALRDLGVRIALDDFGTGYSALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGI 596
COG5001 532 FDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLRMECVVEGV 611
|
410 420
....*....|....*....|....*....
gi 117928627 597 ETYDQLEILRQLGCRLGQGFLLQKPMPAD 625
COG5001 612 ETEAQRDRVAALGATVMQGYHYARPMPAE 640
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
1e-69 |
259.39 |
54.82 |
7,182,350,15,199,365,6,205,374,30,239,404,51,291,455,51,344,506,116,462,622,166 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 183 VRSISSVVCAVHARRraETARYH---LASHDALTGLVNRTTFAARVADAVGQAERGrghlCVLMVDIDGFKRVNDSLGHL 259
PRK11359 351 VADISQHMAALALEQ--EKSRQHieqLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 260 HGDRLLRDIAQRMTAIVRPTDTVARIGGDEFgVLVTGLAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASR 339
PRK11359 425 WADQALLEVVNRFREKLKPDQYLCRIEGTQF-VLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDVGK 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 340 GIEpaELLADADLAMTEAKNTGKGRCVVFRPALRRAAAQRIALEEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRW 419
PRK11359 504 NRD--YLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARW 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 420 PHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHRVAWtpRLHCRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGV 499
PRK11359 582 HDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEW--RSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGI 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 500 PPEVLVLEMTESVFIDEEAGTLAVLRALRDLGVRIALDDFGTGYSALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRA 579
PRK11359 660 DGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEA 739
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 117928627 580 VIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKPMPADTLP 628
PRK11359 740 ITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIP 788
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
2e-63 |
238.90 |
64.67 |
7,194,220,10,206,230,28,238,258,100,339,358,124,466,482,86,552,571,15,570,586,55 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 195 ARRRAETARYhlASHDALTGLVNRTTFAARVADAVGQAERgrghLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTA 274
PRK13561 221 QRHYEEQNEN--AMRFPVSDLPNKALLMALLEQVVARKQT----TALMIITCETLRDTAGVLKEAQREILLLTLVEKLKS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 275 IVRPTDTVARIGGDEFGVLVTGLAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASrGIEPAELLADADLAM 354
PRK13561 295 VLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYG-DLTAEQLYSRAVSAA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 355 TEAKNTGKGRCVVFRPALRRAAAQRIALEEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIP 434
PRK13561 374 FTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPDGLID 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 435 LAEDSGLVVPLGEWVLRTALQHRVAWTPRlhcRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFI 514
PRK13561 454 RIESCGLMVTVGHWVLEESCRLLAAWQER---GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 515 DEEAGTLAVLRALRDLGVRIALDDFGTGYSALSYLRRF---PVDILKLDRSFIAGLlgtAQDQAVTRAVIGLAQQLDLDL 591
PRK13561 531 DDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGL---PEDSSMVAAIIMLAQSLNLQM 607
|
410 420 430
....*....|....*....|....*....|....
gi 117928627 592 VAEGIETYDQLEILRQLGCRLGQGFLLQKPMPAD 625
PRK13561 608 IAEGVETEAQRDWLAKAGVGVAQGFLFARPLPIE 641
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
9e-63 |
236.53 |
38.17 |
7,204,685,97,302,782,14,316,797,67,383,866,20,403,890,7,413,897,43,460,940,171 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 205 HLASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVAR 284
PRK09776 686 YSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLAR 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 285 IGGDEFGVLVTGLAAPNeAEAIALRLRDAFRT-PFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNTGKG 363
PRK09776 766 LGGDEFGLLLPDCNVES-ARFIATRIISAINDyRFPWEGRVYRVGASAGITAIDDNNHQASEVMSQADIACYAAKNAGRG 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 364 RCVVFRPALRRAAAQRIALE--EDLRAAVEAGAFRLDFQPIV----ELATGMWvgaEALLRWPHPTRGLVPPLDFIPLAE 437
PRK09776 845 RVTVYEPQQAAAHSERRELSlaEQWRSMLEENQLMLQAQEIAspriPEARNLW---LISLRLWDCEGEIIDEGAFRPAAE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 438 DSGLVVPLGEWVLRTALQHrvawTPRLHCRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDEE 517
PRK09776 922 DPALMHALDRWVIHELFQQ----GARAVASKGLSIAIPLSVASLSSATLLPFLLEQLENSPLPPRLLHLEITETALLNHA 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 518 AGTLAVLRALRDLGVRIALDDFGTGYSALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIE 597
PRK09776 998 EAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEMLVSIINGIAQRLGMKTIAGPVE 1077
|
410 420 430
....*....|....*....|....*....|....
gi 117928627 598 TYDQLEILRQLGCRLGQGFLLQKPMPADTLPAHC 631
PRK09776 1078 LPLTLDTLSGIGVDLAQGYVIGRPQPLDLLLNSS 1111
|
|
|
|
|
|
|
-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 |
7e-56 |
213.67 |
44.85 |
3,385,272,75,463,347,55,519,402,105 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 386 LRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHRVAWtprLH 465
COG4943 273 LQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDL---LR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 466 CRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDEEAgTLAVLRALRDLGVRIALDDFGTGYSA 545
COG4943 350 QHRDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFADPKK-MTPIILRLREAGHEIYIDDFGTGYSN 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117928627 546 LSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKPMPA 624
COG4943 429 LHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKALPA 507
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
6e-52 |
200.70 |
57.69 |
5,211,304,23,235,327,228,466,555,82,548,640,19,570,659,65 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 212 LTGLVNRTTFAARVADAVGQAERgRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARIGGDEFG 291
PRK11829 305 VTELPNRSLFISLLEKEIASSTR-TDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 292 VLVTGLAAPNEAEAIALRLRDAFRTPFAVDGRSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNTGKGRCVVFRPA 371
PRK11829 384 VLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPH 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 372 LRRAAAQRIALEEDLRAAVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLR 451
PRK11829 464 LIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLE 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 452 TALQHRVAWTPRlhcRQDFCVSVNVSVRQLAEPGFVDVVTDALAASGVPPEVLVLEMTESVFIDEEAGTLAVLRALRDLG 531
PRK11829 544 EACRILADWKAR---GVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLG 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 532 VRIALDDFGTGYSALSY---LRRFPVDILKLDRSFIAGLlgtAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQL 608
PRK11829 621 LLIALDDFGIGYSSLRYlnhLKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEH 697
|
410 420
....*....|....*....|....*..
gi 117928627 609 GCRLGQGFLLQKPMPADTLPAHCPSSA 635
PRK11829 698 GIQCGQGFLFSPPLPRAEFEAQYFSSA 724
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
3e-40 |
161.76 |
47.30 |
6,388,270,68,460,338,4,464,344,32,498,376,5,503,383,16,520,399,116 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 389 AVEAGAFRLDFQPIVELATGMWVGAEALLRWPHPTRGLVPPLDFIPLAEDSGLVVPLGEWVLRTALQHrvawTPRL--HC 466
PRK10551 271 AIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARD----AAELqkVL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 467 RQDFCVSVNVSVRQLAEPGFVDVVTDALAAsgVPPEV--LVLEMTESVFIDEEAGtLAVLRALRDLGVRIALDDFGTGYS 544
PRK10551 347 PVGAKLGINIAPAHLHSDSFKADVQRLLAS--LPADHfqIVLEITERDMLQEEEA-LKLFAWLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 545 ALSYLRRFPVDILKLDRSFIAGLLGTAQDQAVTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKPMPA 624
PRK10551 424 ALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISRPLPL 503
|
250
....*....|..
gi 117928627 625 DTLPAHCPSSAS 636
PRK10551 504 DDFVKWLKKPYS 515
|
|
|
|
|
|
|
-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-28 |
121.56 |
38.16 |
4,204,267,93,298,360,17,315,378,9,324,389,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 205 HLASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVAR 284
COG3706 268 ELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVAR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 285 IGGDEFGVLVTGLaAPNEAEAIALRLRDAFR-TPFAVDGRS--VHLSASIGVATSASRGIEPAELLADADLAMTEAKNTG 361
COG3706 348 YGGEEFAVVLPDT-DLEAAIAIAERIRQKINeLPFVHELSRepLEVTISIGVAEGKPGEDSIEELLKRADKALYKAKASG 426
|
....*..
gi 117928627 362 KGRCVVF 368
COG3706 427 RNRVVVK 433
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
3e-25 |
111.94 |
35.67 |
5,205,290,89,294,381,5,302,386,12,314,399,8,322,409,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 206 LASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARI 285
PRK09581 291 MAVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 286 GGDEFGVLV--TGLAApneAEAIALRLRDAF-RTPFAVDG--RSVHLSASIGVATSASRGIEPAELLADADLAMTEAKNT 360
PRK09581 371 GGEEFVVVMpdTDIEV---AIAVAERIRRKIaEEPFAISDgkERLNVTVSIGVAELRPSGESIEALIKRADKALYEAKNT 447
|
....*.
gi 117928627 361 GKGRCV 366
PRK09581 448 GRNRVV 453
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
2e-23 |
106.33 |
54.27 |
5,205,128,24,231,152,65,297,217,19,316,237,17,334,254,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 206 LASHDALTGLVNRTTFAARVADAVgqAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARI 285
PRK09894 129 RSNMDVLTGLPGRRVLDESFDHQL--RNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 286 GGDEFGVLVTGlAAPNEAEAIALRLRDAFRT-PFAVDGRSVHLSASIGVaTSASRGIEPAELLADADLAMTEAKNTGKGR 364
PRK09894 207 GGEEFIIILKA-ATDEEACRAGERIRQLIANqAITHSEGRINITATFGV-TRAFPEEPLDEVIGRADRAMYEGKQAGRNR 284
|
...
gi 117928627 365 CVV 367
PRK09894 285 VMF 287
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
7e-15 |
77.75 |
31.45 |
3,206,247,19,226,266,94,320,361,14 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 207 ASHDALTGLVNRTTFAARVaDAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAIVRPTDTVARIG 286
PRK09966 248 ALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 117928627 287 GDEFGVLVTGLAAPNEAEAIALRLRDAFRTPFAV-DGRSVHLSASIGVA 334
PRK09966 327 GDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYA 375
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
1e-14 |
76.85 |
64.64 |
16,206,227,61,267,289,15,282,305,17,300,322,7,307,332,17,324,350,2,330,352,5,335,362,13,363,375,22,385,407,18,403,434,15,421,449,3,431,452,25,457,477,9,470,486,30,500,517,125 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 207 ASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRD-IAQRMTAIVRPTDTV-AR 284
PRK11059 228 AFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFElINLLSTFVQRYPGALlAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 285 IGGDEFGVLVTGLAApNEAEAIA---LRLRDAFRTPFAVDGRS-VHlsasIGVAT-----SASRGIEPAELLAdadlamt 355
PRK11059 308 YSRSDFAVLLPHRSL-KEADSLAsqlLKAVDSLPPPKMLDRDDfLH----IGIAAyrsgqSTEQVMEEAEMAL------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 356 eakntgkgRCVVFRPALRRAAAQRIALEED----------LRAAVEAGAFRLDFQPIV---------ELATGMWVGAEAL 416
PRK11059 376 --------RSAQLQGGNSWFMYDKAQDPEKgrgsvrwrtlLEQALVRGGPRLYQQPVVtrdgqvhhrELMCRIRDGQGNE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 417 LRwphPTRglvppldFIPLAEDSGLVVPLGEWVLRTALQHrVAWTPRLHCrqdfCVSVNVSVRQLAEPGFVDVVTDALAA 496
PRK11059 448 VR---AAE-------FMPMVLQCGLSEQYDRQVIERVLPL-LSYWPEESQ----NLSINLSVDSLLSRAFQRWLRDTLLQ 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 497 SGVP-PEVLVLEMTESVFIDEEAGTLAVLRALRDLGVRIALDDFGTGYSALSYLRRFPVDILKLDRSFIAGLLGTAQDQA 575
PRK11059 513 CERSqRKRLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHQRTENQL 592
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 117928627 576 VTRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKPMPAD 625
PRK11059 593 FVRSLVGACAGTETQVFAEGVESREEWQTLQILGVSGGQGDFFASPQPLD 642
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
8e-13 |
70.70 |
45.01 |
5,195,202,6,205,208,96,304,304,7,311,316,8,322,324,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 196 RRRAETaryhLASHDALTGLVNRTTFAARVADAVGQAERGRGHLCVLMVDIDGFKRVNDSLGHLHGDRLLRDIAQRMTAI 275
PRK10245 203 KRRLQV----MSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQIT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 276 VRPTDTVARIGGDEFGVLVTGLAAPNeaeAIALRLR-----DAFRTPFAvdgRSVHLSASIGVATSASRGIEPAELLADA 350
PRK10245 279 LRGSDVIGRFGGDEFAVIMSGTPAES---AITAMLRvheglNTLRLPNA---PQVTLRISVGVAPLNPQMSHYREWLKSA 352
|
170
....*....|....*..
gi 117928627 351 DLAMTEAKNTGKGRCVV 367
PRK10245 353 DLALYKAKKAGRNRTEV 369
|
|
|
|
|
|
|
-1 |
| 129332 |
TIGR00229 |
sensory_box |
PAS domain S-box |
PAS domain S-box |
true |
true |
false |
124 |
8e-10 |
60.76 |
93.55 |
3,8,1,63,71,70,27,98,99,18 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 9 EARFGETYRRVAIGMALLDVAGRFRAVNDAFAELVGVEADALIGSEETTFIRPDDRHWADWGI------GGEPQRLQVRM 82
TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIerllegEREPYSEERRV 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 117928627 83 CRADGTEIHVIRILTA--AADEEPFVLGHYIDVTEH 116
TIGR00229 82 RRKDGSEIWVEVSVSPirTNGGELGVVGIVRDITER 117
|
|
|
|
|
|
|
-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 |
3e-08 |
55.67 |
31.94 |
7,484,63,10,494,76,23,519,99,20,540,119,13,553,133,7,566,140,9,577,149,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928627 485 GFVDVVTDAL---AASGVPPEVLVLEMTESVFIDEEagTLAVLRALRDLGVRIALDDFgTGYSALSYLRRFP-VDILKLD 560
COG3434 64 CFINFPEELLisdLPELLPPDKVVIEILEDCPPTEK--LLSAIKELKQKGYLLALDDF-IFSNVSEWKPLLPlSDIVKID 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117928627 561 rsfiagLLGTAQDQAvtRAVIGLAQQLDLDLVAEGIETYDQLEILRQLGCRLGQGFLLQKP 621
COG3434 141 ------FKRVTFDKA--RLFDRDLGYINKKFLAEKVETEEEFEQAKKAGFDLFQGYFFSKP 193
|
|
|
|
|
|
|
-1 |
| 117024 |
pfam08447 |
PAS_3 |
PAS fold |
PAS fold |
false |
true |
false |
90 |
0.004 |
38.52 |
85.56 |
3,34,3,22,56,27,8,64,41,39 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117928627 35 VNDAFAELVGVEADALIGSEET--TFIRPDDR------HWADWGIGGEPQRLQVRMCRADGTEIHVIRILTAAADEE 103
pfam08447 4 WSPRFEEILGYTPEELKSSYEDwlDLVHPEDRervrraLQEFSLKKGEPYSGEYRIRRKDGEYRWVEARGRPIRDEN 80
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
0.008 |
37.38 |
5.65 |
1,2,296,63 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117928627 3 ADLHAIEARFGETYRRVAIGMALLDVAGRFRAVNDAFAELVGVEADALIGSEETTFIRPDDRH 65
PRK09776 297 KHISESETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLN 359
|
|
|
|
|
|
|
-1 |
|