| 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-72 |
269.01 |
96.25 |
2,576,0,181,761,181,50 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 577 QDLRHAVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQARAWQLP 656
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 657 ERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVHRDPRLAKQTLRELQALGVKVAMDDFGTGYSSL 736
cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15807290 737 SMLKSLPFGLLKIDREFLQDLsaasEQFAASQQFIEVMVRLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGYW 811
cd01948 161 SYLKRLPVDYLKIDRSFVRDI----ETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYL 231
|
|
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 |
168.15 |
98.09 |
3,402,0,25,427,26,62,490,88,66 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 403 HDQLTGLANRSFFYTRARQALDLLA-PGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVRPGDLVGRLSGD 481
cd01949 1 TDPLTGLPNRRAFEERLERLLARARrSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15807290 482 EFVMLLSDlASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGYVVAPQDGGDVELLQKRADLALFQAKAQGRN 556
cd01949 81 EFAILLPG-TDLEEAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRN 154
|
|
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-71 |
266.77 |
95.85 |
2,576,1,181,761,182,50 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 577 QDLRHAVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQARAWQLP 656
smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 657 ERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVHRDPRLAKQTLRELQALGVKVAMDDFGTGYSSL 736
smart00052 82 GPPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15807290 737 SMLKSLPFGLLKIDREFLQDLsaasEQFAASQQFIEVMVRLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGYW 811
smart00052 162 SYLKRLPVDLLKIDKSFVRDL----QTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYL 232
|
|
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-67 |
253.32 |
91.80 |
3,571,0,83,655,83,102,761,185,50 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 572 RRMLSQDLRHAVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQAR 651
COG2200 1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 652 AWQlPERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVHRDPRLAKQTLRELQALGVKVAMDDFGT 731
COG2200 81 TWP-RAGPLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 732 GYSSLSMLKSLPFGLLKIDREFLQDLsaasEQFAASQQFIEVMVRLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGYW 811
COG2200 160 GYSSLSYLKRLPPDILKIDRSFVRDL----ETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYL 235
|
|
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 |
6e-53 |
204.57 |
97.88 |
5,576,1,77,653,81,29,683,110,26,710,136,47,762,183,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 577 QDLRHAVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQARAW--- 653
pfam00563 2 QALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWrgn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 654 QLPERGLTMAVNVSALQFEQSDFVAGVRAcLEQHGLPGHSLVLELTESMVHRDPRLaKQTLRELQALGVKVAMDDFGTGY 733
pfam00563 82 ALLPPDLPLSVNLSPASLLDPSFLEALLA-LKQGGLPPSRLVLEITESDLDEDLRL-LEALARLRSLGFRLALDDFGTGY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15807290 734 SSLSMLKSLPFGLLKIDREFLQDLsaaseQFAASQQFIEVMVRLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGYW 811
pfam00563 160 SSLSYLSRLPPDYIKIDRSFIKDL-----SDPESRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYL 232
|
|
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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
1e-39 |
160.10 |
99.38 |
3,400,0,24,424,25,74,498,101,58 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 401 ASHDQLTGLANRSFFYTRARQALD-LLAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVRPGDLVGRLS 479
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQrAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15807290 480 GDEFVMLLSDLASPGDLRL--VAERLLQQLREPCVCGTELVVPTVSLGYVVAPQDGGDVELLQKRADLALFQAKAQGRN 556
pfam00990 81 GDEFAILLPDTSLEGAQELaeRIRRLLAALKIPHTLSGLPLYVTISIGIAAYPNDGEDAEDLLKRADQALYQAKNQGRN 159
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
1e-38 |
157.41 |
100.00 |
3,398,0,26,424,27,65,490,92,71 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 399 RQASHDQLTGLANRSFFYTRARQALD-LLAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVRPGDLVGR 477
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 478 LSGDEFVMLLSDlASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGYVVAPQDGGDVELLQKRADLALFQAKAQGRNM 557
smart00267 81 LGGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 15807290 558 AVAF 561
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 |
1e-35 |
146.80 |
100.00 |
4,381,0,46,427,47,62,490,109,45,535,155,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 382 ERAQAASALRETRVELSRQASHDQLTGLANRSFFYTRARQALDLLA-PGRSLGLIVADIDHLKAINDRFGYAVGDLLITE 460
COG2199 1 ALLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARrHGEPLALLLLDLDHFKQINDTYGHAAGDEVLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 461 LARRLCEAVRPGDLVGRLSGDEFVMLLSDlASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGYVVAPQDGGD-VELL 539
COG2199 81 VARRLRSNLREGDLVARLGGDEFAVLLPG-TSLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDdAELL 159
|
170 180
....*....|....*....|..
gi 15807290 540 QKRADLALFQAKAQGRNMAVAF 561
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 |
3e-33 |
139.01 |
100.00 |
5,399,0,29,428,30,69,498,99,5,503,107,7,511,114,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 400 QASHDQLTGLANRSFFYTRARQALDLLAP-GRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVRPGDLVGRL 478
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 479 SGDEFVMLLSDLASPGDLRlVAERL---LQQLREPcVCGTELVVPTVSLGYVVAPQDGGDVELLQKRADLALFQAKAQGR 555
TIGR00254 81 GGEEFVVILPGTPLEDALS-KAERLrdaINSKPIE-VAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGR 158
|
....*..
gi 15807290 556 NMAVAFA 562
TIGR00254 159 NRVVVAD 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 |
0.009 |
37.77 |
85.10 |
13,579,21,21,601,42,14,615,60,2,619,62,5,624,68,11,641,79,13,654,94,12,666,108,9,677,117,8,687,125,3,692,128,10,707,138,73,784,211,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 580 RHAVRHGQLQLHYQGIFLLPGqRLSGFEALVRWPHP----KRgmIPPDR-FIALAEESRLIlelgrwVLDEACRQARAWQ 654
PRK11596 22 RRFWLQCERAYTFQPIYRTCG-RLMAVELLTVVTHPsnpsQR--LSPDRyFAEITVSHRLD------VVKEQLDLLAQKA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 655 --LPERGLTMAVNV--SALQFEQSDfvAGVRACLEqhGLPghSLVLELTESMvhrdpRLAKQTLRELQALGVKVAMDDFG 730
PRK11596 93 dfFVRHGLLASVNIdgPTLIALRQQ--PKILRLIE--RLP--WLRFELVEHI-----RLPKDSTFASMCEFGPLWLDDFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 731 TGYSSLSMLKSLPFGLLKIDREFLQDLSAASEQFAASQQFIEVMVRLAHNlqmrVVAEGVETAEQYDLLCGMGCDEAQGY 810
PRK11596 162 TGMANFSALSEVRYDYIKVARELFVMLRQSPEGRTLFSQLLHLMNRYCRG----VIVEGVETPEEWRDVQRSPAFAAQGY 237
|
.
gi 15807290 811 W 811
PRK11596 238 F 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 |
| 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 |
5e-75 |
277.68 |
65.46 |
5,370,197,45,417,242,11,428,256,225,656,481,101,761,582,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 371 REAELQRKRRNERAQAASALRETRVELSRQASHDQLTGLANRSFFytRARQALDLLAP---GRSLGLIVADIDHLKAIND 447
COG5001 198 REFSDMVQSQVTLTQRAEETRRLSDENDRLANLDSLTGLPNRRRF--FAELDARLAAArqsGRRLVLGVIDLDGFKPVND 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 448 RFGYAVGDLLITELARRLCEAVRPGDLVGRLSGDEFVMLLSDLASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGYV 527
COG5001 276 AFGHATGDRLLIEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 528 VAPQDGGDVELLQKRADLALFQAKAQGRNMAVAFAGDMSAEEEERRMLSQDLRHAVRHGQLQLHYQGIFLLPGQRLSGFE 607
COG5001 356 PFPSGADTSEQLFERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 608 ALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQARAWqlpERGLTMAVNVSALQFEQSDFVAGVRACLEQH 687
COG5001 436 ALARWHSPEIGPVPPDVFIGIAERSGQIVELTRLLLAKALREARAW---PMDVRVSINLSARDLASMENVRRLLAIVSES 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 688 GLPGHSLVLELTESMVHRDPRLAKQTLRELQALGVKVAMDDFGTGYSSLSMLKSLPFGLLKIDREFLQDLsaasEQFAAS 767
COG5001 513 CIAPHRLDFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDL----EENPTS 588
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15807290 768 QQFIEVMVRLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGY 810
COG5001 589 EDIVRTVLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGY 631
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
3e-73 |
271.60 |
62.29 |
5,390,226,39,430,265,59,490,324,110,601,434,156,761,590,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 391 RETRVELSRQASHDQLTGLANRSFFYTRARQALDLLAPGrSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVR 470
PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDHAIAQADNN-QVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 471 PGDLVGRLSGDEFVMLLSDlASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGYVVAPQDGGDVELLQKRADLALFQA 550
PRK10060 306 EDQTLARLGGDEFLVLASH-TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALSPEHGDDSESLIRSADTAMYTA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 551 KAQGRNMAVAFAGDMSAEEEERRMLSQDLRHAVRHGQLQLHYQGIFLLPGqRLSGFEALVRWPHPKRGMIPPDRFIALAE 630
PRK10060 385 KEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPPLEFISYAE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 631 ESRLILELGRWVLDEACRQARAWQLPERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVHRDPRLA 710
PRK10060 464 ESGLIVPLGRWVILDVVRQAAKWRDKGINLRVAVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESCLIENEELA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 711 KQTLRELQALGVKVAMDDFGTGYSSLSMLKSLPFGLLKIDREFLQDLsaasEQFAASQQFIEVMVRLAHNLQMRVVAEGV 790
PRK10060 544 LSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDI----HKQPVSQSLVRAIVAVAQALNLQVIAEGV 619
|
410 420
....*....|....*....|
gi 15807290 791 ETAEQYDLLCGMGCDEAQGY 810
PRK10060 620 ETAKEDAFLTKNGVNERQGF 639
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
2e-67 |
252.84 |
51.31 |
12,391,366,25,420,391,4,424,396,65,490,461,35,527,496,66,593,563,8,602,571,52,656,623,4,660,630,41,701,673,10,713,683,42,759,725,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 392 ETRVELSRQASHDQLTGLANRSFFYtrarQALD-LLAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVR 470
PRK11359 367 KSRQHIEQLIQFDPMTGLPNRNNLH----NYLDdLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 471 PGDLVGRLSGDEFVMLLSDlASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGyvVAPQDGGDVELLQKRADLALFQA 550
PRK11359 443 PDQYLCRIEGTQFVLVSLE-NDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIG--ISYDVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 551 KAQGRNMAVAFAGDMSAEEEERRMLSQDLRHAVRHGQLQLHYQ-GIFLLPGQrLSGFEALVRWPHPKRGMIPPDRFIALA 629
PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQpQIFAETGE-LYGIEALARWHDPLHGHVPPSRFIPLA 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 630 EESRLILELGRWVLDEACRQARAWQlpERGL---TMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTES--MVH 704
PRK11359 599 EEIGEIENIGRWVIAEACRQLAEWR--SQNIhipALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESmmMEH 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 705 RDPRLAKqtLRELQALGVKVAMDDFGTGYSSLSMLKSLPFGLLKIDREFLQdlsaASEQFAASQQFIEVMVRLAHNLQMR 784
PRK11359 677 DTEIFKR--IQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVD----RCLTEKRILALLEAITSIGQSLNLT 750
|
410 420
....*....|....*....|....*.
gi 15807290 785 VVAEGVETAEQYDLLCGMGCDEAQGY 810
PRK11359 751 VVAEGVETKEQFEMLRKIHCRVIQGY 776
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
2e-52 |
202.69 |
63.59 |
8,388,218,35,426,253,99,527,352,7,534,360,120,656,480,6,662,488,77,739,568,18,764,586,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 389 ALRETRVELSRQASHDQLTGLANRSFFYTRARQALdllAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEA 468
PRK13561 219 LLQRHYEEQNENAMRFPVSDLPNKALLMALLEQVV---ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 469 VRPGDLVGRLSGDEFVMLLSDLASPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGyvVAPQDGG-DVELLQKRADLAL 547
PRK13561 296 LSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIG--IAMFYGDlTAEQLYSRAVSAA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 548 FQAKAQGRNMAVAFAGDMSAEEEERRMLSQDLRHAVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIA 627
PRK13561 374 FTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPDGLID 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 628 LAEESRLILELGRWVLDEACRQARAWQlpERGLTM--AVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVHR 705
PRK13561 454 RIESCGLMVTVGHWVLEESCRLLAAWQ--ERGIMLplSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRID 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 706 DPRLAKQTLRELQALGVKVAMDDFGTGYSSLSML---KSLPFGLLKIDREFLQDLsaaseqfAASQQFIEVMVRLAHNLQ 782
PRK13561 532 DPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGL-------PEDSSMVAAIIMLAQSLN 604
|
410 420
....*....|....*....|....*...
gi 15807290 783 MRVVAEGVETAEQYDLLCGMGCDEAQGY 810
PRK13561 605 LQMIAEGVETEAQRDWLAKAGVGVAQGF 632
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
1e-48 |
189.92 |
37.10 |
8,395,682,29,424,712,69,494,781,15,509,797,69,578,868,31,609,900,41,651,941,106,761,1047,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 396 ELSRQASHDQLTGLANRSFFYTRARQALD-LLAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVRPGDL 474
PRK09776 683 QLSYSASHDALTGLANRASFEKQLREALQtVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 475 VGRLSGDEFVMLLSDLASPgDLRLVAERLLQQLRE-PCVCGTELVVPTVSLGYVVAPQDGGDVELLQKRADLALFQAKAQ 553
PRK09776 763 LARLGGDEFGLLLPDCNVE-SARFIATRIISAINDyRFPWEGRVYRVGASAGITAIDDNNHQASEVMSQADIACYAAKNA 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 554 GRNMAVAFAGDMSAEEEERRMLSQD--LRHAVRHGQLQLHYQGIFLLPGQRLSGFEAL-VRWPHPKRGMIPPDRFIALAE 630
PRK09776 842 GRGRVTVYEPQQAAAHSERRELSLAeqWRSMLEENQLMLQAQEIASPRIPEARNLWLIsLRLWDCEGEIIDEGAFRPAAE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 631 ESRLILELGRWVLDEACRQArAWQLPERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVHRDPRLA 710
PRK09776 922 DPALMHALDRWVIHELFQQG-ARAVASKGLSIAIPLSVASLSSATLLPFLLEQLENSPLPPRLLHLEITETALLNHAEAA 1000
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 711 KQTLRELQALGVKVAMDDFGTGYSSLSMLKSLPFGLLKIDREFLQDLsaasEQFAASQQFIEVMVRLAHNLQMRVVAEGV 790
PRK09776 1001 SRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANL----QGNLMDEMLVSIINGIAQRLGMKTIAGPV 1076
|
410 420
....*....|....*....|
gi 15807290 791 ETAEQYDLLCGMGCDEAQGY 810
PRK09776 1077 ELPLTLDTLSGIGVDLAQGY 1096
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
7e-46 |
181.05 |
61.54 |
5,357,257,24,381,282,4,387,286,348,735,637,38,780,675,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 358 GLLAEQIRYEVLRREAELQRKRRN-ERAQaaSALRETRVELSRQASHDQLTGLANRSFFYTRARQALDLLAPGRSLGLIV 436
PRK11829 258 GVLHHQLTLPAHHQDDELGVLVRNyNRNQ--QLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 437 ADIDHLKAINDRFGYAVGDLLITELARRLCEAVRPGDLVGRLSGDEFVMLLSDLASPGDLRLVAERLLQQLREPCVCGTE 516
PRK11829 336 IGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 517 LVVPTVSLGYVVAPQDGGDVELLQKRADLALFQAKAQGRNMAVAFAGDMSAEEEERRMLSQDLRHAVRHGQLQLHYQGIF 596
PRK11829 416 TLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 597 LLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQARAWQLPERGLTMAVNVSALQFEQSDF 676
PRK11829 496 DMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 677 VAGVRACLEQHGLPGHSLVLELTESMVHRDPRLAKQTLRELQALGVKVAMDDFGTGYSS---LSMLKSLPFGLLKIDREF 753
PRK11829 576 LPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSlryLNHLKSLPIHMIKLDKSF 655
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15807290 754 LQDLSAASEQFAASQQFIEVmvrlahnLQMRVVAEGVETAEQYDLLCGMGCDEAQGY 810
PRK11829 656 VKNLPEDDAIARIISCVSDV-------LKVRVMAEGVETEEQRQWLLEHGIQCGQGF 705
|
|
|
|
|
|
|
-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-41 |
164.36 |
44.66 |
3,571,265,132,704,397,68,776,465,34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 572 RRMLSQDLRHAVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQAR 651
COG4943 266 YLSPRRRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLG 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 652 AWQLPERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHSLVLELTESMVhRDPRLAKQTLRELQALGVKVAMDDFGT 731
COG4943 346 DLLRQHRDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTF-ADPKKMTPIILRLREAGHEIYIDDFGT 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15807290 732 GYSSLSMLKSLPFGLLKIDREFLQDLSAASEQFAASQQFIEvmvrLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGY 810
COG4943 425 GYSNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIE----MAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGW 499
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
1e-34 |
143.27 |
43.63 |
8,581,270,73,654,345,2,657,347,29,688,376,4,692,382,8,700,391,6,708,397,49,761,446,50 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 582 AVRHGQLQLHYQGIFLLPGQRLSGFEALVRWPHPKRGMIPPDRFIALAEESRLILELGRWVLDEACRQARAWQ--LPeRG 659
PRK10551 271 AIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQkvLP-VG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 660 LTMAVNVSALQFEQSDFVAGVRACLEQhgLPGH--SLVLELTE-SMVHRDprLAKQTLRELQALGVKVAMDDFGTGYSSL 736
PRK10551 350 AKLGINIAPAHLHSDSFKADVQRLLAS--LPADhfQIVLEITErDMLQEE--EALKLFAWLHSQGIEIAIDDFGTGHSAL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15807290 737 SMLKSLPFGLLKIDREFLQDLsaasEQFAASQQFIEVMVRLAHNLQMRVVAEGVETAEQYDLLCGMGCDEAQGYW 811
PRK10551 426 IYLERFTLDYLKIDRGFINAI----GTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYW 496
|
|
|
|
|
|
|
-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 |
6e-28 |
121.56 |
44.14 |
5,367,242,16,389,258,35,424,294,66,491,360,18,509,381,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 368 VLRREAELQRKRRNERaqaasaLRETRVELSRQASHDQLTGLANRSFFYTRARQALD-LLAPGRSLGLIVADIDHLKAIN 446
COG3706 243 RARLRRQLRRKRYERQ------LRESLERLQELALVDGLTGLFNRRYFDEHLADLWKrALREGRPLSLLMLDIDDFKEIN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 447 DRFGYAVGDLLITELARRLCEAVRPGDLVGRLSGDEFVMLLSDLaSPGDLRLVAERLLQQLRE---PCVCGTELVVPTVS 523
COG3706 317 DTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLPDT-DLEAAIAIAERIRQKINElpfVHELSREPLEVTIS 395
|
170 180 190
....*....|....*....|....*....|....*....
gi 15807290 524 LGYVVAPQDGGDVELLQKRADLALFQAKAQGRNMAVAFA 562
COG3706 396 IGVAEGKPGEDSIEELLKRADKALYKAKASGRNRVVVKR 434
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
6e-28 |
121.56 |
40.70 |
7,373,270,9,388,279,3,391,285,6,400,291,24,424,316,65,490,381,19,509,403,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 374 ELQRKRRNEraqaasALR---ETRVELsrqASHDQLTGLANRSFFYTRARQALD-LLAPGRSLGLIVADIDHLKAINDRF 449
PRK09581 271 QIRRKRYQD------ALRqnlEQSIEM---AVTDGLTGLHNRRYFDMHLKQLIErANERGKPLSLMMLDIDHFKQVNDTY 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 450 GYAVGDLLITELARRLCEAVRPGDLVGRLSGDEFVMLLSDlASPGDLRLVAERLLQQLRE---PCVCGTELVVPTVSLGY 526
PRK09581 342 GHDAGDEVLREFAKRLRKNIRGTDLIARYGGEEFVVVMPD-TDIEVAIAVAERIRRKIAEepfAISDGKERLNVTVSIGV 420
|
170 180 190
....*....|....*....|....*....|....*.
gi 15807290 527 VVAPQDGGDVELLQKRADLALFQAKAQGRNMAVAFA 562
PRK09581 421 AELRPSGESIEALIKRADKALYEAKNTGRNRVVALA 456
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-19 |
92.27 |
46.36 |
8,384,193,45,429,239,59,490,298,5,495,308,7,503,315,8,514,323,13,527,337,12,540,349,16 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 385 QAASALRETRVELSRQASHDQLTGLANRSFFYTRARQALDLLAPG-RSLGLIVADIDHLKAINDRFGYAVGDLLITELAR 463
PRK10245 194 QTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHnRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 464 RLCEAVRPGDLVGRLSGDEFVMLLSdlASPGD-----LRLVAERlLQQLREPCvcgTELVVPTVSLGYV-VAPQDGGDVE 537
PRK10245 274 QLQITLRGSDVIGRFGGDEFAVIMS--GTPAEsaitaMLRVHEG-LNTLRLPN---APQVTLRISVGVApLNPQMSHYRE 347
|
170
....*....|....*....
gi 15807290 538 LLqKRADLALFQAKAQGRN 556
PRK10245 348 WL-KSADLALYKAKKAGRN 365
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
2e-16 |
83.22 |
59.73 |
7,387,115,12,399,128,24,424,152,65,490,217,19,509,237,22,532,259,24,557,283,7 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 388 SALRETRVELSR-QASHDQLTGLANRSFFYTRARQALdLLAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLC 466
PRK09894 116 AALTDYKIYLLTiRSNMDVLTGLPGRRVLDESFDHQL-RNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 467 EAVRPGDLVGRLSGDEFVMLLSDlASPGDLRLVAERLLQQLRE-PCVCGTELVVPTVSLGYVVAPQdGGDVELLQKRADL 545
PRK09894 195 SWTRPYETVYRYGGEEFIIILKA-ATDEEACRAGERIRQLIANqAITHSEGRINITATFGVTRAFP-EEPLDEVIGRADR 272
|
170
....*....|....*....
gi 15807290 546 ALFQAKAQGRNmAVAFAGD 564
PRK09894 273 AMYEGKQAGRN-RVMFIDE 290
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
4e-16 |
81.99 |
40.29 |
3,389,236,122,511,359,21,533,380,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 390 LRETRVELSRQASHDQLTGLANRSFFYTRARQALDLLAPGRSLGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAV 469
PRK09966 237 LQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 470 RPGDLVGRLSGDEFVMLLSDLASPGDLRLVAERLLQQLREPC-VCGTELVVPTVSLGYVVAPQDgGDVELLQKRADLALF 548
PRK09966 317 GLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFdLHNGHQTTMTLSIGYAMTIEH-ASAEKLQELADHNMY 395
|
....*
gi 15807290 549 QAKAQ 553
PRK09966 396 QAKHQ 400
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
1e-12 |
70.30 |
73.99 |
22,333,157,8,341,169,5,348,174,4,358,178,4,364,182,20,384,204,15,399,226,24,423,254,6,432,260,38,470,300,20,491,320,34,526,354,31,559,385,12,571,404,6,581,410,23,605,433,48,655,481,38,693,520,10,703,532,3,707,535,2,710,537,66,780,603,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 334 ALRCLREQ----RELEQqhRARLaeqragLLAEqiRYEVLRREAELQRKRRNERA--QAASALRETRVELSR-------Q 400
PRK11059 158 GVRWLRRQlagqELLEE--RARR------ILNG--EREQAVAGSGYEWPRLASRAldHLLEELQDARKERSRfdtfirsN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 401 ASHDQLTGLANRSFFYTRARQAL----DLLAPGrslGLIVADIDHLKAINDRFGYAVGDLLITELARRLCEAVR--PGDL 474
PRK11059 228 AFLDAKTGLGNRLFFDNQLDTLLedqeKVGAHG---VVMLIRLPDFDLLQEELGESQVDELLFELINLLSTFVQryPGAL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 475 VGRLSGDEFVMLLSDLaSPGDLRLVAERLLQQLREPCVCGTELVVPTVSLGyVVAPQDGGDVELLQKRADLALFQAKAQG 554
PRK11059 305 LARYSRSDFAVLLPHR-SLKEADSLASQLLKAVDSLPPPKMLDRDDFLHIG-IAAYRSGQSTEQVMEEAEMALRSAQLQG 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 555 RNMavAFAGDMSAEEEE-------RRMLSQdlrhAVRHGQLQLHYQGIFLLPGQRLSgFEALVRWPHPKRGMIPPDRFIA 627
PRK11059 383 GNS--WFMYDKAQDPEKgrgsvrwRTLLEQ----ALVRGGPRLYQQPVVTRDGQVHH-RELMCRIRDGQGNEVRAAEFMP 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 628 LAEESRLILELGRWVLDEACRQARAWqlPERGLTMAVNVSALQFEQSDFVAGVRACLEQHGLPGHS-LVLELTESMV--H 704
PRK11059 456 MVLQCGLSEQYDRQVIERVLPLLSYW--PEESQNLSINLSVDSLLSRAFQRWLRDTLLQCERSQRKrLIFELAEADVvqH 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 705 RDpRLaKQTLRELQALGVKVAMDDFGTGYSSLSMLKSLPFGLLKIDREFLQDLSAASEQFAASQQFIEVMVRlahnLQMR 784
PRK11059 534 ID-RL-RPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHQRTENQLFVRSLVGACAG----TETQ 607
|
490 500
....*....|....*....|....*
gi 15807290 785 VVAEGVETAEQYDLLCGMGCDEAQG 809
PRK11059 608 VFAEGVESREEWQTLQILGVSGGQG 632
|
|
|
|
|
|
|
-1 |
| 138753 |
PRK11788 |
PRK11788 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
true |
true |
false |
389 |
0.003 |
39.43 |
21.59 |
5,283,185,25,311,210,27,341,237,14,356,251,7,365,258,11 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 284 LGEAALVRGDLAQAREGLGRAEELAntpPLLARVRGSQSRLYEQLGDPAQALRCLreqRELEQQHRARLAEQrAGLLAEQ 363
PRK11788 186 LAQQALARGDLDAARALLKKALAAD---PQCVRASILLGDLALAQGDYAAAIEAL---ERVEEQDPEYLPEV-LPKLMEC 258
|
90
....*....|...
gi 15807290 364 irYEVLRREAELQ 376
PRK11788 259 --YQALGDEAEGL 269
|
|
|
|
|
|
|
-1 |
| 32733 |
COG2909 |
MalT |
ATP-dependent transcriptional regulator [Transcription] |
ATP-dependent transcriptional regulator [Transcription] |
false |
true |
false |
894 |
0.009 |
37.98 |
11.41 |
2,282,501,26,308,530,73 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807290 283 VLGEAALVRGDLAQAREGLGRAEELA---NTPPLLARVRGSQSRLYEQLGDPAQALRCLREQRELEQQHRARLAEQRAGL 359
COG2909 502 VLGEAAHIRGELTQALALMQQAEQMArqhDVYHLALWSLLQQSEILEAQGQVARAEQEKAFNLIREQHLEQKPRHEFLVR 581
|
90 100
....*....|....*....|..
gi 15807290 360 LAEQIRYEVLRREAELQRKRRN 381
COG2909 582 IRAQLLRAWLRLDLAEAEARLG 603
|
|
|
|
|
|
|
-1 |
|