| 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-35 |
144.97 |
95.00 |
4,30,9,27,57,38,40,97,81,23,120,109,128 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 31 EQPRLVFQPIVDLDRAVVAGYEALARF--AVSPPVAPDVWFAAAAAGGLAAELERRVVRRVLAARSHLP---PNCFLTVN 105
cd01948 10 GEFELYYQPIVDLRTGRIVGYEALLRWrhPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQaggPDLRLSVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 106 VSPQALTTDDVLDEF-----RHGGDLAGIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRPE 180
cd01948 90 LSARQLRDPDFLDRLlellaETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927737 181 LMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPVD 248
cd01948 170 YLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 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-33 |
138.15 |
92.19 |
5,18,4,11,31,15,26,57,43,43,100,88,20,120,113,127 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 19 CARLLPGLLRDpeQPRLVFQPIVDLDRAVVAGYEALARF--AVSPPVAPDVWFAAAAAGGLAAELERRVVRRVLAARSHL 96
COG2200 5 ERDLRQALENG--EFSLYYQPIVDLATGRIVGYEALLRWrhPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRTW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 97 PPNC--FLTVNVSPQALTTDDVLDEF-----RHGGDLAGIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYS 169
COG2200 83 PRAGplRLAVNLSPVQLRSPGLVDLLlrllaRLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGTGYS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927737 170 GLQRLVALRPELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
COG2200 163 SLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPL 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 |
| 109613 |
pfam00563 |
EAL |
EAL domain |
EAL domain |
false |
false |
false |
236 |
2e-31 |
132.16 |
94.49 |
6,33,13,24,57,39,39,96,84,25,121,113,16,138,129,62,201,191,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 34 RLVFQPIVDLDRAVVAGYEALARF--AVSPPVAPDVWFAAAAAGGLAAELERRVVRRVLAARSHL------PPNCFLTVN 105
pfam00563 14 SLYFQPIVDLRTGKVLGYEALLRWqhPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWrgnallPPDLPLSVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 106 VSPQALTTDDVLDEFR----HGGDLAGIFVELTEQQhVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRPEL 181
pfam00563 94 LSPASLLDPSFLEALLalkqGGLPPSRLVLEITESD-LDEDLRLLEALARLRSLGFRLALDDFGTGYSSLSYLSRLPPDY 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117927737 182 MKIDRSLVSGIDSDEAKKAcVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHP 246
pfam00563 173 IKIDRSFIKDLSDPESRAL-LRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 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 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
9e-27 |
116.16 |
94.19 |
5,30,10,27,58,37,3,61,43,36,97,82,24,121,111,126 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 31 EQPRLVFQPIVDLDRAVVAGYEALARFaVSP---PVAPDVWFAAAAAGGLAAELERRVVRRVLAARSHLP---PNCFLTV 104
smart00052 11 GQFLLYYQPIVSLRTGRLVGVEALIRW-QHPeggIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQaqgPPLRISI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 105 NVSPQALTTDDVLDEFR-----HGGDLAGIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRP 179
smart00052 90 NLSARQLISPDLVPRVLelleeTGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927737 180 ELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
smart00052 170 DLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 237
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
8e-04 |
40.08 |
34.12 |
1,160,156,87 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 161 MDDAGSGYSGLQRLVALRPELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQG 240
PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFVMLRQSPEGRTLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQG 236
|
....*..
gi 117927737 241 FLLGHPV 247
PRK11596 237 YFLSRPA 243
|
|
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 |
1e-20 |
96.25 |
37.71 |
5,12,393,23,35,418,22,57,442,63,120,510,127,247,639,4 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 13 EGSIEACARLLPGLLRDPEQPRL--VFQPIVDLDRAVVAGYEALARF--AVSPPVAPDVWFAAAAAGGLAAELERRVVRR 88
COG5001 394 EAAIRDMAVVEQALRSADLEQELsvHFQPIVDIVSGKTIALEALARWhsPEIGPVPPDVFIGIAERSGQIVELTRLLLAK 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 89 VLAARSHLPPNCFLTVNVSPQALTTDDVLDEF-----RHGGDLAGIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDD 163
COG5001 474 ALREARAWPMDVRVSINLSARDLASMENVRRLlaivsESCIAPHRLDFEITETAIVCDFDQARDALAALHELGVRTALDD 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 164 AGSGYSGLQRLVALRPELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLL 243
COG5001 554 FGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHY 633
|
250
....*....|
gi 117927737 244 GHPV--DDWR 251
COG5001 634 ARPMpaEERR 643
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
5e-19 |
90.56 |
22.32 |
2,103,496,25,128,526,118 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 104 VNVSPQALTTDDVLDEFRHGGDLAG-----IFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALR 178
PRK10060 497 VNVSARQLADQTIFTALKQVLQELNfeycpIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFP 576
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927737 179 PELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHP 246
PRK10060 577 IDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
|
|
|
|
|
-1 |
| 34551 |
COG4943 |
COG4943 |
Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms] |
Predicted signal transduction protein containing sensor and EAL domains [Signal... |
false |
true |
false |
524 |
6e-18 |
86.94 |
42.94 |
5,31,280,29,60,311,36,96,350,24,120,379,17,138,396,109 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 32 QPRLVFQPIVDLDRAVVAGYEALARFAVS--PPVAPDVWFAAAAAGGLAAELERRVVRRVLAARSHL---PPNCFLTVNV 106
COG4943 281 ELCVHYQPIVDLATGKCVGAEALARWPQEdgTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDLlrqHRDLHVSINL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 107 SPQALTTDDVLDEF-----RHGGDLAGIFVELTEQQhVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRPEL 181
COG4943 361 SASDLASPRLIDRLnrklaQYQVRPQQIALELTERT-FADPKKMTPIILRLREAGHEIYIDDFGTGYSNLHYLQSLPVDA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927737 182 MKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
COG4943 440 LKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKAL 505
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
1e-15 |
79.43 |
23.20 |
4,101,487,19,120,511,50,170,564,26,199,590,48 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 102 LTVNVSPQALTTDDVLDEF-----RHGGDLAGIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSG---LQR 173
PRK13561 488 LSVNLSALQLMHPNMVADMlelltRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGlrqLQH 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117927737 174 LVALRPELMKIDRSLVSGIDSDEakkACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
PRK13561 568 MKSLPIDVLKIDKMFVDGLPEDS---SMVAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPL 638
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
1e-14 |
75.86 |
43.63 |
7,30,274,27,57,303,10,68,313,27,95,345,27,122,377,14,140,391,11,151,405,95 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 31 EQPRLVFQPIVDLDRAVVAGYEALARF--AVSPPVAPDVwFAAAAAGGLAAELERRVVRRVLAARSH-----LPPNCFLT 103
PRK10551 275 EQFYVVYQPVVDTQTLRVTGLEVLLRWrhPTAGEIPPDA-FINYAEAQKLIVPLTQHLFELIARDAAelqkvLPVGAKLG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 104 VNVSPQALTTDDVLDEFRH-----GGDLAGIFVELTEQqhvlDLAATHKALEE---LRQHGAMIAMDDAGSGYSGLQRLV 175
PRK10551 354 INIAPAHLHSDSFKADVQRllaslPADHFQIVLEITER----DMLQEEEALKLfawLHSQGIEIAIDDFGTGHSALIYLE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117927737 176 ALRPELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHP 246
PRK10551 430 RFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISRP 500
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
2e-14 |
75.65 |
28.41 |
7,31,555,26,57,587,4,61,595,7,69,602,29,101,631,15,116,653,10,128,663,119 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 32 QPRLVFQPIVDLDRAVVAGYEALARF------AVSP----PVAPDVWfAAAAAGGLAAELERRVVRRVLAARSHLPPncf 101
PRK11359 556 QLKLVYQPQIFAETGELYGIEALARWhdplhgHVPPsrfiPLAEEIG-EIENIGRWVIAEACRQLAEWRSQNIHIPA--- 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 102 LTVNVSPQALTTDDV-------LDEFRHGGDLagIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRL 174
PRK11359 632 LSVNLSALHFRSNQLpnqvsdaMHAWGIDGHQ--LTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRL 709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117927737 175 VALRPELMKIDRSLVSGIDSDEAKKACVEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
PRK11359 710 VSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
3e-11 |
64.34 |
16.90 |
3,124,588,55,179,646,17,199,663,48 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 125 DLAGIFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRP---ELMKIDRSLVSGIDSDEakkAC 201
PRK11829 589 DPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLPEDD---AI 665
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 117927737 202 VEMLRVLAGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
PRK11829 666 ARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPL 711
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
2e-09 |
58.95 |
10.66 |
1,128,983,119 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 129 IFVELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRPELMKIDRSLVSGIDSDEAKKACVEMLRVL 208
PRK09776 984 LHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEMLVSIINGI 1063
|
90 100 110
....*....|....*....|....*....|....*....
gi 117927737 209 AGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
PRK09776 1064 AQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRPQ 1102
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
9e-04 |
39.87 |
18.38 |
2,128,521,2,131,523,116 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 129 IFvELTEQQHVLDLAATHKALEELRQHGAMIAMDDAGSGYSGLQRLVALRPELMKIDRSLVSGIDSDEAKKACVEMLRVL 208
PRK11059 522 IF-ELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHQRTENQLFVRSLVGA 600
|
90 100 110
....*....|....*....|....*....|....*....
gi 117927737 209 AGRLDAWLLAEGVETPEELRTLVSLEVPLAQGFLLGHPV 247
PRK11059 601 CAGTETQVFAEGVESREEWQTLQILGVSGGQGDFFASPQ 639
|
|
|
|
|
|
|
-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 |
0.003 |
38.33 |
26.54 |
6,128,85,13,143,98,20,163,119,15,179,134,11,194,145,18,216,163,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927737 129 IFVELTEQQHVLDlaATHKALEELRQHGAMIAMDD-AGSGYSGLQRLVALRpELMKIDRSLVSgidsDEAKKACVEMLRV 207
COG3434 86 VVIEILEDCPPTE--KLLSAIKELKQKGYLLALDDfIFSNVSEWKPLLPLS-DIVKIDFKRVT----FDKARLFDRDLGY 158
|
90 100 110
....*....|....*....|....*....|....*....
gi 117927737 208 LAGRLdawlLAEGVETPEELRTLVSLEVPLAQGFLLGHP 246
COG3434 159 INKKF----LAEKVETEEEFEQAKKAGFDLFQGYFFSKP 193
|
|
|
|
|
|
|
-1 |
|