| 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-81 |
299.05 |
99.58 |
4,660,0,83,746,83,12,758,96,88,849,184,55 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 661 TDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARWQRY 740
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 741 AQPggvFHVAVNVSGRQL-HPRLPDIVRTALTETGMPPGALVIEVTENILVKRSEEAIAVLRQLKSFGVRVAIDDFGTGY 819
cd01948 81 GPD---LRLSVNLSARQLrDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 820 SSLSYLARFPVDVLKIDKSFVEQITDRnsgTEGTELVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFSR 899
cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETD---PEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSR 234
|
....*
gi 117928688 900 PLPAE 904
cd01948 235 PLPAE 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 |
1e-49 |
193.96 |
99.36 |
2,486,1,92,579,93,64 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 487 DPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRRCVRPSDTVARLGGDE 566
cd01949 2 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGDE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117928688 567 FAILVVGPQAEAhGVDVAERVQRALAEPFLLSGREVTLAASIGIAVTDDGTETVDQLLRNADLAMYRAKSSRKGTYV 643
cd01949 82 FAILLPGTDLEE-AEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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 |
| 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 |
2e-06 |
50.66 |
100.00 |
3,367,0,63,431,63,28,459,92,11 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 368 SSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAPADVHRLEAILLDAVLRPRSThTIEFAMRHAAGHWRET 447
cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPV-TLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 117928688 448 ETVITSLVDDHD-IRGLVLNTRDV 470
cd00130 80 LVSLTPIRDEGGeVIGLLGVVRDI 103
|
|
cl02459 |
141436 |
PAS |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most... |
2 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
9e-88 |
320.31 |
99.59 |
4,659,0,84,746,84,13,759,98,87,849,185,55 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 660 ETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARWQR 739
smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 740 YAQPggvFHVAVNVSGRQLH-PRLPDIVRTALTETGMPPGALVIEVTENILVKRSEEAIAVLRQLKSFGVRVAIDDFGTG 818
smart00052 81 QGPP---LRISINLSARQLIsPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 819 YSSLSYLARFPVDVLKIDKSFVEQITDRnsgTEGTELVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFS 898
smart00052 158 YSSLSYLKRLPVDLLKIDKSFVRDLQTD---PEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFS 234
|
....*.
gi 117928688 899 RPLPAE 904
smart00052 235 RPLPLD 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 |
| 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 |
1e-75 |
279.90 |
97.27 |
4,655,0,85,744,85,15,759,101,80,842,181,68 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 656 RVQTETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGA 735
COG2200 1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 736 RWQRYaqpgGVFHVAVNVSGRQLH-PRLPDIVRTALTETGMPPGALVIEVTENILVKRSEEAIAVLRQLKSFGVRVAIDD 814
COG2200 81 TWPRA----GPLRLAVNLSPVQLRsPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 815 FGTGYSSLSYLARFPVDVLKIDKSFveqITDRNSGTEGTELVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQG 894
COG2200 157 FGTGYSSLSYLKRLPPDILKIDRSF---VRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQG 233
|
250
....*....|....*.
gi 117928688 895 YLFSRPLPAEGIDTLF 910
COG2200 234 YLFSRPLPADALDALL 249
|
|
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 |
5e-62 |
234.62 |
100.00 |
5,659,0,99,758,100,9,768,109,23,792,132,57,853,189,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 660 ETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARWQR 739
pfam00563 1 EQALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 740 YAQPGGVFHVAVNVSGRQL-HPRLPDIVRtALTETGMPPGALVIEVTENILVKrSEEAIAVLRQLKSFGVRVAIDDFGTG 818
pfam00563 81 NALLPPDLPLSVNLSPASLlDPSFLEALL-ALKQGGLPPSRLVLEITESDLDE-DLRLLEALARLRSLGFRLALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 819 YSSLSYLARFPVDVLKIDKSFVEQITDRNSGtegtELVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFS 898
pfam00563 159 YSSLSYLSRLPPDYIKIDRSFIKDLSDPESR----ALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFS 234
|
..
gi 117928688 899 RP 900
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 |
2e-45 |
179.37 |
98.77 |
2,481,0,96,578,96,65 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 482 RQAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRRCVRPSDTVAR 561
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 562 LGGDEFAILVVGPQAEaHGVDVAERVQRALAEPFLLSGREVTLAASIGIAVTDDGTETVDQLLRNADLAMYRAKSSRKGT 641
smart00267 81 LGGDEFALLLPETSLE-EAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
..
gi 117928688 642 YV 643
smart00267 160 VA 161
|
|
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 |
4e-44 |
175.51 |
100.00 |
3,483,0,94,578,94,14,592,111,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 484 AFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRRCVRPSDTVARLG 563
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 564 GDEFAILVVGPQAEaHGVDVAERVQRALA---EPFLLSGREVTLAASIGIAVTDDGTETVDQLLRNADLAMYRAKSSRKG 640
pfam00990 81 GDEFAILLPDTSLE-GAQELAERIRRLLAalkIPHTLSGLPLYVTISIGIAAYPNDGEDAEDLLKRADQALYQAKNQGRN 159
|
.
gi 117928688 641 T 641
pfam00990 160 R 160
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 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-42 |
168.76 |
99.45 |
3,465,1,112,578,113,34,612,148,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 466 NTRDVSERKELERQLTRQAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLV 545
COG2199 2 LLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 546 ADRLRRCVRPSDTVARLGGDEFAILVVGPQAEaHGVDVAERVQRALAEPFLLSGREVTLAASIGIAV-TDDGTETVDQLL 624
COG2199 82 ARRLRSNLREGDLVARLGGDEFAVLLPGTSLE-EAARLAERIRAALEEPFFLGGEELRVTVSIGVALyPEDGSDDAELLL 160
|
170 180
....*....|....*....|.
gi 117928688 625 RNADLAMYRAKSSRKGTYVRF 645
COG2199 161 RRADLALYRAKRAGRNRVVVF 181
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
4e-32 |
135.54 |
98.18 |
5,482,0,89,573,89,7,580,97,11,591,109,10,601,120,42 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 483 QAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRRCVRPSDTVARL 562
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 563 GGDEFAILVvgPQAEAHG-VDVAERVQRAL-AEPFLLSGRE-VTLAASIGIAVTDDGTETVDQLLRNADLAMYRAKSSRK 639
TIGR00254 81 GGEEFVVIL--PGTPLEDaLSKAERLRDAInSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGR 158
|
....
gi 117928688 640 GTYV 643
TIGR00254 159 NRVV 162
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
4e-08 |
55.49 |
63.92 |
10,734,88,13,748,101,10,758,116,4,767,120,5,773,125,3,778,128,16,798,144,9,808,153,32,842,185,6,849,191,60 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 735 ARWQRYAQPGGVFhVAVNVSGRQL-----HPRLpdivrTALTEtGMPpgALVIEVTENILVKRSEeaiaVLRQLKSFGvR 809
PRK11596 89 AQKADFFVRHGLL-ASVNIDGPTLialrqQPKI-----LRLIE-RLP--WLRFELVEHIRLPKDS----TFASMCEFG-P 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 810 VAIDDFGTGYSSLSYLARFPVDVLKIDKSFVeqITDRNSgTEGTELVRTILHLGRALRLGTVAEGIETREQYAALLAMSC 889
PRK11596 155 LWLDDFGTGMANFSALSEVRYDYIKVARELF--VMLRQS-PEGRTLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPA 231
|
170 180
....*....|....*....|
gi 117928688 890 DYGQGYLFSRPLPAEGIDTL 909
PRK11596 232 FAAQGYFLSRPAPFDTLETL 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 |
| 128402 |
smart00091 |
PAS |
PAS domain |
PAS domain |
false |
false |
false |
67 |
9e-06 |
48.16 |
97.01 |
1,359,1,65 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117928688 360 WFRSLVQNSSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAPADVHRLEAILLDAV 424
smart00091 2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDREEVQEALQRLL 66
|
|
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... |
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
4e-98 |
354.81 |
64.40 |
9,468,221,39,509,260,58,569,318,13,582,332,100,683,432,56,742,488,19,761,508,82,844,590,8,854,598,50 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 469 DVSERKELERQLTRQAFSDPLTGLANRALFANRVEHALSerSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADR 548
PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAIA--QADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 549 LRRCVRPSDTVARLGGDEFaiLVVGPQAEAHGVD-VAERVQRALAEPFLLSGREVTLAASIGIAVTDDGTETVDQLLRNA 627
PRK10060 300 ILSCLEEDQTLARLGGDEF--LVLASHTSQAALEaMASRILTRLRLPFRIGLIEVYTGCSIGIALSPEHGDDSESLIRSA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 628 DLAMYRAKSSRKGTYVRFRTEMHDALLARVQTETDLRHALSRRELVLHYQPTVNLrTGQVVGVEALIRWYHPTRGLIQPM 707
PRK10060 378 DTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 708 DFIGMAEETGLVESIGAWAIRECCRQGARWQRyaqPGGVFHVAVNVSGRQLHPR-LPDIVRTALTETGMPPGALVIEVTE 786
PRK10060 457 EFISYAEESGLIVPLGRWVILDVVRQAAKWRD---KGINLRVAVNVSARQLADQtIFTALKQVLQELNFEYCPIDVELTE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 787 NILVKRSEEAIAVLRQLKSFGVRVAIDDFGTGYSSLSYLARFPVDVLKIDKSFVEQItDRNSGTEGteLVRTILHLGRAL 866
PRK10060 534 SCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDI-HKQPVSQS--LVRAIVAVAQAL 610
|
410 420 430
....*....|....*....|....*....|....*...
gi 117928688 867 RLGTVAEGIETREQYAALLAMSCDYGQGYLFSRPLPAE 904
PRK10060 611 NLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAV 648
|
|
|
|
|
|
|
-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 |
7e-84 |
307.34 |
64.86 |
4,466,210,276,748,486,12,760,499,86,849,585,55 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 467 TRDVSERKELERQLTRQAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVA 546
COG5001 211 TQRAEETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 547 DRLRRCVRPSDTVARLGGDEFAILVVGPQAEAHGVDVAERVQRALAEPFLLSGREVTLAASIGIAVTDDGTETVDQLLRN 626
COG5001 291 RRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQLFER 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 627 ADLAMYRAKSSRKGTYVRFRTEMHDALLARVQTETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQP 706
COG5001 371 ADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIGPVPP 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 707 MDFIGMAEETGLVESIGAWAIRECCRQGARWQRYAQpggvfhVAVNVSGRQLHP-RLPDIVRTALTETGMPPGALVIEVT 785
COG5001 451 DVFIGIAERSGQIVELTRLLLAKALREARAWPMDVR------VSINLSARDLASmENVRRLLAIVSESCIAPHRLDFEIT 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 786 ENILVKRSEEAIAVLRQLKSFGVRVAIDDFGTGYSSLSYLARFPVDVLKIDKSFVEQITDRnsgTEGTELVRTILHLGRA 865
COG5001 525 ETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEEN---PTSEDIVRTVLQLGRN 601
|
410 420 430
....*....|....*....|....*....|....*....
gi 117928688 866 LRLGTVAEGIETREQYAALLAMSCDYGQGYLFSRPLPAE 904
COG5001 602 LRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMPAE 640
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
2e-82 |
302.91 |
53.07 |
9,471,363,41,516,404,51,569,455,13,582,469,28,612,497,127,741,624,18,759,643,83,842,727,8,854,735,52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 472 ERKELERQLTRQAFSDPLTGLANRALFANRVEHALSERSRQpgevAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRR 551
PRK11359 364 EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 552 CVRPSDTVARLGGDEFaiLVVGPQAEAHGVD-VAERVQRALAEPFLLSGREVTLAASIGIavTDDGTETVDQLLRNADLA 630
PRK11359 440 KLKPDQYLCRIEGTQF--VLVSLENDVSNITqIADELRNVVSKPIMIDDKPFPLTLSIGI--SYDVGKNRDYLLSTAHNA 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 631 MYRAKSSRKGTYVRFRTEMHDALLARVQTETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFI 710
PRK11359 516 MDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFI 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 711 GMAEETGLVESIGAWAIRECCRQGARWQRyaQPGGVFHVAVNVSGRQLH-PRLPDIVRTALTETGMPPGALVIEVTENIL 789
PRK11359 596 PLAEEIGEIENIGRWVIAEACRQLAEWRS--QNIHIPALSVNLSALHFRsNQLPNQVSDAMHAWGIDGHQLTVEITESMM 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 790 VKRSEEAIAVLRQLKSFGVRVAIDDFGTGYSSLSYLARFPVDVLKIDKSFVEQ-ITDRNSGTegteLVRTILHLGRALRL 868
PRK11359 674 MEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRcLTEKRILA----LLEAITSIGQSLNL 749
|
410 420 430
....*....|....*....|....*....|....*...
gi 117928688 869 GTVAEGIETREQYAALLAMSCDYGQGYLFSRPLPAEGI 906
PRK11359 750 TVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
8e-72 |
267.40 |
63.90 |
10,478,225,29,511,254,11,522,269,15,540,284,5,546,289,68,615,357,123,741,480,17,758,498,70,828,571,20,854,591,50 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 479 QLTRQAFSDPLTGLANRALFANRVEHALSersrQPGEVAVLFLD----LDGFKGVNDAQGHAVgdhLLTLVaDRLRRCVR 554
PRK13561 226 EQNENAMRFPVSDLPNKALLMALLEQVVA----RKQTTALMIITcetlRDTAGVLKEAQREIL---LLTLV-EKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 555 PSDTVARLGGDEFAILVVGPQAEAHGVDVAERVQRALAEPFLLSGREVTLAASIGIAVTDdGTETVDQLLRNADLAMYRA 634
PRK13561 298 PRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFY-GDLTAEQLYSRAVSAAFTA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 635 KSSRKGTYVRFRTEMHDALLARVQTETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAE 714
PRK13561 377 RRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPDGLIDRIE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 715 ETGLVESIGAWAIRECCRQGARWQryaQPGGVFHVAVNVSGRQL-HPRLPDIVRTALTETGMPPGALVIEVTENILVKRS 793
PRK13561 457 SCGLMVTVGHWVLEESCRLLAAWQ---ERGIMLPLSVNLSALQLmHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 794 EEAIAVLRQLKSFGVRVAIDDFGTGYSSLSYLARF---PVDVLKIDKSFVEQITDRNSgtegteLVRTILHLGRALRLGT 870
PRK13561 534 HAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPEDSS------MVAAIIMLAQSLNLQM 607
|
410 420 430
....*....|....*....|....*....|....
gi 117928688 871 VAEGIETREQYAALLAMSCDYGQGYLFSRPLPAE 904
PRK13561 608 IAEGVETEAQRDWLAKAGVGVAQGFLFARPLPIE 641
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
2e-63 |
239.61 |
39.70 |
11,456,660,117,573,780,5,582,785,11,593,797,69,662,868,31,693,900,43,738,943,6,746,949,12,758,962,87,846,1049,5,853,1054,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 457 DHDIRGLVLNTRDVSERKELERQLTRQAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHA 536
PRK09776 661 DGENIGSVLVFQDVTESRAMLRQLSYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 537 VGDHLLTLVADRLRRCVRPSDTVARLGGDEFAILVVG---PQAEAhgvdVAERVQRALAE-PFLLSGREVTLAASIGIAV 612
PRK09776 741 AGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDcnvESARF----IATRIISAINDyRFPWEGRVYRVGASAGITA 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 613 TDDGTETVDQLLRNADLAMYRAKSSRKGTYVRFRTEMHDALLARVQTETD--LRHALSRRELVLHYQPTVNLRTGQVVGV 690
PRK09776 817 IDDNNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSERRELSLAeqWRSMLEENQLMLQAQEIASPRIPEARNL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 691 EAL-IRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARwqRYAQPGgvFHVAVNVSGRQL-HPRLPDIVRT 768
PRK09776 897 WLIsLRLWDCEGEIIDEGAFRPAAEDPALMHALDRWVIHELFQQGAR--AVASKG--LSIAIPLSVASLsSATLLPFLLE 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 769 ALTETGMPPGALVIEVTENILVKRSEEAIAVLRQLKSFGVRVAIDDFGTGYSSLSYLARFPVDVLKIDKSFVEQITDrNS 848
PRK09776 973 QLENSPLPPRLLHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQG-NL 1051
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 117928688 849 GTEgtELVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFSRPLP 902
PRK09776 1052 MDE--MLVSIINGIAQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRPQP 1103
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
3e-59 |
225.73 |
71.57 |
12,401,191,50,457,241,24,481,285,6,487,303,25,513,328,85,600,413,4,604,419,134,741,553,20,761,575,4,766,579,58,824,640,24,854,664,48 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 402 QRFVSLVAPADVHRLEAILLDAVLRPRSTHTIEFAMRHAAGHWRETETVItslvddHDIRGLVLNTRDVSERKELERQLT 481
PRK11829 192 QPLAHLVLRADSFRMYQFILSALSAMLSTYLLLALVLSVSIAWCINRLII------HPLRAMAKELEDIGDHGVLHHQLT 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 482 --------------------RQAFSD------------PLTGLANRALFANRVEHALSERSRQpGEVAVLFLDLDGFKGV 529
PRK11829 266 lpahhqddelgvlvrnynrnQQLLADayadmgrishrfPVTELPNRSLFISLLEKEIASSTRT-DHFHLLVIGIETLQEV 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 530 NDAQGHAVGDHLLTLVADRLRRCVRPSDTVARLGGDEFAILVVGPQAEAHGVDVAERVQRALAEPFLLSgrEVTL--AAS 607
PRK11829 345 SGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFD--EITLrpSAS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 608 IGIAVTDDGTETVDQLLRNADLAMYRAKSSRKGTYVRFRTEMHDALLARVQTETDLRHALSRRELVLHYQPTVNLRTGQV 687
PRK11829 423 IGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQV 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 688 VGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARWQryaQPGGVFHVAVNVSGRQLHPR--LPDI 765
PRK11829 503 IGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWK---ARGVSLPLSVNISGLQVQNKqfLPHL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 766 vRTALTETGMPPGALVIEVTENILVKRSEEAIAVLRQLKSFGVRVAIDDFGTGYSSLSY---LARFPVDVLKIDKSFVEQ 842
PRK11829 580 -KTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYlnhLKSLPIHMIKLDKSFVKN 658
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 843 ITDRNSgtegteLVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFSRPLP 902
PRK11829 659 LPEDDA------IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 712
|
|
|
|
|
|
|
-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 |
5e-52 |
201.34 |
45.04 |
7,662,272,77,740,349,4,746,353,13,759,367,28,787,397,16,806,413,48,857,461,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 663 LRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARWQRyAQ 742
COG4943 273 LQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDLLR-QH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 743 PGgvFHVAVNVSGRQLH-PRLPDIVRTALTETGMPPGALVIEVTEN--ILVKRSEEAIAVLRQLksfGVRVAIDDFGTGY 819
COG4943 352 RD--LHVSINLSASDLAsPRLIDRLNRKLAQYQVRPQQIALELTERtfADPKKMTPIILRLREA---GHEIYIDDFGTGY 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 820 SSLSYLARFPVDVLKIDKSFVEQITDRNSGTEGTElvrTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFSR 899
COG4943 427 SNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAP---HIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSK 503
|
....*
gi 117928688 900 PLPAE 904
COG4943 504 ALPAQ 508
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
4e-41 |
165.61 |
47.68 |
8,652,257,95,749,352,10,759,363,13,774,376,4,778,382,14,793,396,50,851,446,6,857,457,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 653 LLARVQTETDLRHALSRRELVLHYQPTVNLRTGQVVGVEALIRWYHPTRGLIQPMDFIGMAEETGLVESIGAWAIRECCR 732
PRK10551 258 LSLRMRPGREILTAIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIAR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 733 QGARWQRYAQPGGVFhvAVNVSGRQLH-PRLPDIVRTALTEtgMPPG--ALVIEVTENILVKRsEEAIAVLRQLKSFGVR 809
PRK10551 338 DAAELQKVLPVGAKL--GINIAPAHLHsDSFKADVQRLLAS--LPADhfQIVLEITERDMLQE-EEALKLFAWLHSQGIE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 810 VAIDDFGTGYSSLSYLARFPVDVLKIDKSFVEQItdrnsgteGTELVR-----TILHLGRALRLGTVAEGIETREQYAAL 884
PRK10551 413 IAIDDFGTGHSALIYLERFTLDYLKIDRGFINAI--------GTETVTspvldAVLTLAKRLNMLTVAEGVETPEQARWL 484
|
250 260
....*....|....*....|
gi 117928688 885 LAMSCDYGQGYLFSRPLPAE 904
PRK10551 485 REHGVNFLQGYWISRPLPLD 504
|
|
|
|
|
|
|
-1 |
| 33501 |
COG3706 |
PleD |
Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal transduction mechanisms] |
Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal... |
false |
true |
false |
435 |
2e-32 |
136.20 |
44.37 |
5,462,241,19,481,267,98,580,365,13,593,379,12,605,393,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 463 LVLNTRDVSERKELERQLT-------RQAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGH 535
COG3706 242 LRARLRRQLRRKRYERQLReslerlqELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGH 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 536 AVGDHLLTLVADRLRRCVRPSDTVARLGGDEFAILVVGPQAEAHgVDVAERVQRALAE-PFLLSGREVTLA--ASIGIAV 612
COG3706 322 DVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLPDTDLEAA-IAIAERIRQKINElPFVHELSREPLEvtISIGVAE 400
|
170 180 190
....*....|....*....|....*....|....
gi 117928688 613 TDDGTETVDQLLRNADLAMYRAKSSRKGTYVRFR 646
COG3706 401 GKPGEDSIEELLKRADKALYKAKASGRNRVVVKR 434
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
5e-30 |
128.50 |
36.32 |
8,472,281,9,482,290,20,503,310,12,515,323,52,569,375,10,579,386,13,592,400,7,599,409,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 473 RKELERQLTrQAFSDPLTGLANRALFANRVeHALSERSRQPGE-VAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRR 551
PRK09581 282 RQNLEQSIE-MAVTDGLTGLHNRRYFDMHL-KQLIERANERGKpLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 552 CVRPSDTVARLGGDEFaiLVVGPQAEAH-GVDVAERVQRALA-EPFLLSG--REVTLAASIGIAVTDDGTETVDQLLRNA 627
PRK09581 360 NIRGTDLIARYGGEEF--VVVMPDTDIEvAIAVAERIRRKIAeEPFAISDgkERLNVTVSIGVAELRPSGESIEALIKRA 437
|
170
....*....|
gi 117928688 628 DLAMYRAKSS 637
PRK09581 438 DKALYEAKNT 447
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
2e-26 |
116.91 |
66.51 |
20,472,213,6,478,221,4,482,226,72,554,300,17,573,317,2,575,322,3,580,325,10,590,338,8,599,346,5,606,351,10,617,361,36,654,397,2,656,401,25,682,426,55,742,481,16,758,498,21,779,520,67,849,587,10,861,597,9,870,608,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 473 RKELER--QLTR-QAFSDPLTGLANRALFANRVEHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRL 549
PRK11059 214 RKERSRfdTFIRsNAFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFELINLL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 550 RRCVR--PSDTVARLGGDEFAILVvgPQ---AEAhgVDVAERVQRA---LAEPFLLSgREVTLaaSIGIAVTDDGtETVD 621
PRK11059 294 STFVQryPGALLARYSRSDFAVLL--PHrslKEA--DSLASQLLKAvdsLPPPKMLD-RDDFL--HIGIAAYRSG-QSTE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 622 QLLRNADLAMYRAKSSRKGTYVRFRTEMHDALlAR--VQTETDLRHALSRRELVLHYQPTVNlRTGQVVGVEALIRWYHP 699
PRK11059 366 QVMEEAEMALRSAQLQGGNSWFMYDKAQDPEK-GRgsVRWRTLLEQALVRGGPRLYQQPVVT-RDGQVHHRELMCRIRDG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 700 TRGLIQPMDFIGMAEETGLVESIGAWAIRECCRQGARWqryaqPGGVFHVAVNVSGRQL-HPRLPDIVRTALTETGMPPG 778
PRK11059 444 QGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLSYW-----PEESQNLSINLSVDSLlSRAFQRWLRDTLLQCERSQR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 779 A-LVIEVTENILVKRSEEAIAVLRQLKSFGVRVAIDDFGTGYSSLSYLARFPVDVLKIDKSFVEQITDRnsgTEGTELVR 857
PRK11059 519 KrLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHQR---TENQLFVR 595
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 117928688 858 TIlhLGRALRLGT--VAEGIETREQYAALLAMSCDYGQGYLFSRPLP 902
PRK11059 596 SL--VGACAGTETqvFAEGVESREEWQTLQILGVSGGQGDFFASPQP 640
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
1e-24 |
110.57 |
54.61 |
8,475,120,11,486,132,27,515,159,56,573,215,3,576,221,4,582,225,11,593,237,23,617,260,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 476 LERQLTRQAFS-DPLTGLANRALFANRVEHALSERSRQPgeVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRRCVR 554
PRK09894 121 YKIYLLTIRSNmDVLTGLPGRRVLDESFDHQLRNREPLN--LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 555 PSDTVARLGGDEFAILVvgPQA---EAHGvdVAERVQRALAE-PFLLSGREVTLAASIGIAVTDDGtETVDQLLRNADLA 630
PRK09894 199 PYETVYRYGGEEFIIIL--KAAtdeEACR--AGERIRQLIANqAITHSEGRINITATFGVTRAFPE-EPLDEVIGRADRA 273
|
....*..
gi 117928688 631 MYRAKSS 637
PRK09894 274 MYEGKQA 280
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
1e-22 |
103.95 |
39.07 |
4,478,242,24,503,266,92,595,359,22,618,381,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 479 QLTRQAFSDPLTGLANRALFANRVeHALSERSRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLRRCVRPSDT 558
PRK09966 243 QLLRTALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 559 VARLGGDEFAILVVGPQAEAHGVDVAERVQRALAEPF-LLSGREVTLAASIGIAVTDDGTeTVDQLLRNADLAMYRAKSS 637
PRK09966 322 AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFdLHNGHQTTMTLSIGYAMTIEHA-SAEKLQELADHNMYQAKHQ 400
|
.
gi 117928688 638 R 638
PRK09966 401 R 401
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
2e-17 |
86.87 |
45.55 |
5,474,200,21,495,225,11,510,236,68,579,304,59,643,363,6 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 475 ELERQLTRQAFSDPLTGLANR----ALFANRVEHALsersRQPGEVAVLFLDLDGFKGVNDAQGHAVGDHLLTLVADRLR 550
PRK10245 201 EHKRRLQVMSTRDGMTGVYNRrhweTMLRNEFDNCR----RHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 551 RCVRPSDTVARLGGDEFAILVVGPQAEAhGVDVAERVQRALAEPFLLSGREVTLAASIGIAVTDDGTETVDQLLRNADLA 630
PRK10245 277 ITLRGSDVIGRFGGDEFAVIMSGTPAES-AITAMLRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLA 355
|
170
....*....|....*....
gi 117928688 631 MYRAKSSRkgtyvRFRTEM 649
PRK10245 356 LYKAKKAG-----RNRTEV 369
|
|
|
|
|
|
|
-1 |
| 129332 |
TIGR00229 |
sensory_box |
PAS domain S-box |
PAS domain S-box |
true |
true |
false |
124 |
3e-13 |
72.70 |
98.39 |
3,358,2,52,410,56,17,429,73,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 359 KWFRSLVQNSSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAP--ADVHRLEAILLDAVLRPrsTHTIEFA 436
TIGR00229 3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEedREEVRERIERLLEGERE--PYSEERR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 117928688 437 MRHAAGHWRETETVITSLVDDHDIRGLVLNTRDVSERKELERQL 480
TIGR00229 81 VRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKQAEEAL 124
|
|
|
|
|
|
|
-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 |
4e-09 |
59.14 |
31.45 |
7,750,65,15,774,80,16,792,96,24,818,120,11,829,133,7,839,140,6,853,146,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 751 VNVSGRQLHPRLPDIvrtaltetgMPPGALVIEVTENILVkrSEEAIAVLRQLKSFGVRVAIDDFGtgYSSLSYLARFP- 829
COG3434 66 INFPEELLISDLPEL---------LPPDKVVIEILEDCPP--TEKLLSAIKELKQKGYLLALDDFI--FSNVSEWKPLLp 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117928688 830 -VDVLKIDksfVEQITDrnsgtegtELVRTILHLGRALRLGTVAEGIETREQYAALLAMSCDYGQGYLFSRP 900
COG3434 133 lSDIVKID---FKRVTF--------DKARLFDRDLGYINKKFLAEKVETEEEFEQAKKAGFDLFQGYFFSKP 193
|
|
|
|
|
|
|
-1 |
| 138539 |
PRK11360 |
PRK11360 |
sensory histidine kinase AtoS; Provisional |
sensory histidine kinase AtoS; Provisional |
false |
true |
false |
607 |
8e-07 |
51.62 |
19.28 |
6,363,265,51,417,316,6,424,322,7,431,332,10,444,342,14,458,357,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 364 LVQNSSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAPADVHrleAILLDAvLRPRSTH---TIEFAMRHA 440
PRK11360 266 IIENAADGIIAIDRQGDITTMNPAAEVITGYQRHELVGQPYSMLFDNTQFY---SPVLDT-LEHGTEHvalEISFPGRDR 341
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 117928688 441 AghwRETETVITSLVDDH-DIRGLVLNTRDVSERKELERQLTRQ 483
PRK11360 342 T---IELSVTTSRLHDTHgEMIGAVVIFSDLTARKRLQRRMARA 382
|
|
|
|
|
|
|
-1 |
| 117025 |
pfam08448 |
PAS_4 |
PAS fold |
PAS fold |
false |
true |
false |
110 |
3e-06 |
49.72 |
98.18 |
4,366,2,52,419,54,18,438,72,20,458,93,17 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 367 NSSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAPADVHRLEAiLLDAVLRPRSTHTIEFAMrHAAGHWRE 446
pfam08448 3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLER-ALRRALEGEEPIDFLEEL-LLNGEERH 80
|
90 100 110
....*....|....*....|....*....|
gi 117928688 447 TETVITSLVDDH-DIRGLVLNTRDVSERKE 475
pfam08448 81 YELRLTPLRDPDgEVIGVLVISRDITERRR 110
|
|
|
|
|
|
|
-1 |
| 32384 |
COG2202 |
AtoS |
FOG: PAS/PAC domain [Signal transduction mechanisms] |
FOG: PAS/PAC domain [Signal transduction mechanisms] |
false |
true |
false |
232 |
3e-05 |
46.12 |
54.74 |
3,352,105,79,431,185,11,442,197,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 353 ALRTHAKWFRSLVQNSSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAPADVHRLEAILLDAVLRPRSTH- 431
COG2202 106 ALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEGRGGPl 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 117928688 432 TIEFAMRHAAG-HWRETETVITSLVDDHDIRGLVLNTRDVSERKELE 477
COG2202 186 EIEYRVRRKDGeRVRWILSRISPVRDDGEIVGVVGIARDITERKQAE 232
|
|
|
|
|
|
|
-1 |
| 110021 |
pfam00989 |
PAS |
PAS fold |
PAS fold |
false |
true |
false |
112 |
5e-04 |
42.39 |
98.21 |
4,360,2,63,423,66,19,444,85,12,456,98,14 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 361 FRSLVQNSSDIITIVDPSGVIRYQTPSATRVLGYDPNAMVGQRFVSLVAPADVHRLEAILLDA-VLRPRSTHTIEFAMRH 439
pfam00989 3 LRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEDDDAVAELLRQALlQGEESRGFEVSFRVSD 82
|
90 100 110
....*....|....*....|....*....|..
gi 117928688 440 AAGhwRETETVITSLVD-DHDIRGLVLNTRDV 470
pfam00989 83 GRP--RHVEVRASPVRDaGGEILGFLGVLRDI 112
|
|
|
|
|
|
|
-1 |
| 117024 |
pfam08447 |
PAS_3 |
PAS fold |
PAS fold |
false |
true |
false |
90 |
0.006 |
38.52 |
88.89 |
2,380,0,21,401,23,57 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928688 381 IRYQTPSATRVLGYDPNAMVG--QRFVSLVAPADVHRLEAILLDAVLRPRSTHTIEFAMRHAAGHWRETETVITSLVDDH 458
pfam08447 1 IIYWSPRFEEILGYTPEELKSsyEDWLDLVHPEDRERVRRALQEFSLKKGEPYSGEYRIRRKDGEYRWVEARGRPIRDEN 80
|
|
|
|
|
|
|
-1 |
|