| 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 |
7e-67 |
250.52 |
92.08 |
4,570,0,126,696,127,16,712,144,37,750,181,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 571 QALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWREH 650
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 651 WPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQT-ICDEEALEPFLPLIRE-GLRLAIDDFGTGYSSL 728
cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESAlIDDLEEALATLRRLRAlGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15806634 729 SRLYRLPAQILKLDRSLIQDLsADNATDGPLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
cd01948 161 SYLKRLPVDYLKIDRSFVRDI-ETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRE 221
|
|
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-38 |
156.59 |
97.45 |
3,399,0,23,422,26,66,489,92,61 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 400 HDALTGLPNRLALHEALGQQVAA---DSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVGEQGQTFRRGGN 476
cd01949 1 TDPLTGLPNRRAFEERLERLLARarrSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15806634 477 EFVVLLPAVRAApDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSLTLQKNADLALHAAKQEGG 550
cd01949 81 EFAILLPGTDLE-EAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGR 153
|
|
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 |
2e-68 |
255.99 |
91.70 |
4,570,1,129,699,131,13,712,145,42,755,187,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 571 QALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWREH 650
smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 651 WPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQTICD-EEALEPFLPLIRE-GLRLAIDDFGTGYSSL 728
smart00052 82 GPPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDdDESAVATLQRLRElGVRIALDDFGTGYSSL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15806634 729 SRLYRLPAQILKLDRSLIQDLSADNAtDGPLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
smart00052 162 SYLKRLPVDLLKIDKSFVRDLQTDPE-DEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRS 222
|
|
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 |
2e-61 |
232.52 |
87.89 |
5,565,0,85,651,85,45,696,131,16,712,148,42,755,190,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 566 RLELTQALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLA 645
COG2200 1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 646 AWREHwPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQT-ICDEEALEPFLPLIRE-GLRLAIDDFGT 723
COG2200 81 TWPRA-GPLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESAlIDDLDTALALLRQLRElGVRIALDDFGT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15806634 724 GYSSLSRLYRLPAQILKLDRSLIQDLSADNAtDGPLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
COG2200 160 GYSSLSYLKRLPPDILKIDRSFVRDLETDAR-DQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRE 225
|
|
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-52 |
202.65 |
93.64 |
5,570,1,81,651,85,24,676,109,36,712,146,37,751,183,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 571 QALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWREH 650
pfam00563 2 QALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWRGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 651 W---PELRVSVNMAPRQLQQPGSCQEIRdALRAYALPPDALELEITEQTICDEEALEPFLPLIRE-GLRLAIDDFGTGYS 726
pfam00563 82 AllpPDLPLSVNLSPASLLDPSFLEALL-ALKQGGLPPSRLVLEITESDLDEDLRLLEALARLRSlGFRLALDDFGTGYS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15806634 727 SLSRLYRLPAQILKLDRSLIQDLsaDNATDGPLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
pfam00563 161 SLSYLSRLPPDYIKIDRSFIKDL--SDPESRALLRALIALARELGIKVVAEGVETEEQLELLKE 222
|
|
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 |
6e-33 |
137.76 |
95.71 |
3,396,1,26,422,30,66,489,96,61 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 397 QLRHDALTGLPNRLALHEALGQQVAA---DSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVGEQGQTFRR 473
smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRaqrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15806634 474 GGNEFVVLLPAVRAApDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSLTLQKNADLALHAAKQEGG 550
smart00267 82 GGDEFALLLPETSLE-EAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGR 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... |
-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 |
2e-32 |
136.40 |
95.03 |
4,381,3,43,424,49,64,489,113,43,532,157,18 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 382 RRLKEEGRTQQRLAAQLRHDALTGLPNRLALHEALGQQVAADS---APFALLCLDLDHFKTVNHTLGQPAGDALLLYIGE 458
COG2199 4 RLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARrhgEPLALLLLDLDHFKQINDTYGHAAGDEVLREVAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 459 RVQAAVGEQGQTFRRGGNEFVVLLPAVRAApDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSL-TLQKN 537
COG2199 84 RLRSNLREGDLVARLGGDEFAVLLPGTSLE-EAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDDAeLLLRR 162
|
170
....*....|...
gi 15806634 538 ADLALHAAKQEGG 550
COG2199 163 ADLALYRAKRAGR 175
|
|
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 |
2e-32 |
136.22 |
97.50 |
3,399,2,20,419,25,67,486,94,64 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 400 HDALTGLPNRLALHEALGQQ---VAADSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVGEQGQTFRRGGN 476
pfam00990 3 HDPLTGLPNRRYFEEELEQElqrAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15806634 477 EFVVLLPAVR--AAPDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSLTLQKNADLALHAAKQEGG 550
pfam00990 83 EFAILLPDTSleGAQELAERIRRLLAALKIPHTLSGLPLYVTISIGIAAYPNDGEDAEDLLKRADQALYQAKNQGR 158
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
2e-25 |
113.20 |
93.33 |
5,399,3,21,420,27,68,489,95,14,503,110,5,508,116,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 400 HDALTGLPNRLALHEALGQQV---AADSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVGEQGQTFRRGGN 476
TIGR00254 4 RDPLTGLYNRRYLEEMLDSELkraRRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15806634 477 EFVVLLPAVRAApDALTIAQTLLDTIN-EPLLL-DGQALVVTASIGLALFPEDGRDSLTLQKNADLALHAAKQEG 549
TIGR00254 84 EFVVILPGTPLE-DALSKAERLRDAINsKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAG 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... |
-1 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
6e-04 |
41.62 |
76.86 |
11,584,32,8,593,40,18,611,60,7,618,68,12,636,80,17,653,99,13,669,112,16,686,128,10,699,138,52,753,190,4,757,195,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 585 HYQPIVEVrSGKTVAVEALVRWQHPRL--GLLSPDR-FIGLAEDNGLIVplgrwvLNTALRQLAAWREHWPE--LRVSVN 659
PRK11596 33 TFQPIYRT-CGRLMAVELLTVVTHPSNpsQRLSPDRyFAEITVSHRLDV------VKEQLDLLAQKADFFVRhgLLASVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 660 MAPRQLQqpgSCQEIRDALRAYALPPdALELEITEQTicdEEALEPFLPLIREGLRLAIDDFGTGYSSLSRLYRLPAQIL 739
PRK11596 106 IDGPTLI---ALRQQPKILRLIERLP-WLRFELVEHI---RLPKDSTFASMCEFGPLWLDDFGTGMANFSALSEVRYDYI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15806634 740 KLDRSLIQDLSAdnATDG-PLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
PRK11596 179 KVARELFVMLRQ--SPEGrTLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQR 228
|
|
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 |
| 29151 |
cd00189 |
TPR |
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here |
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[... |
true |
true |
true |
100 |
5e-04 |
41.99 |
99.00 |
3,125,1,31,162,32,39,207,71,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 126 AWLGLGLAHLNERRMARGLQAYLEALKICESlnapelSLRVLTNLASAYAKLEQYDTAQPYLTEAHDTARQLGQPFdlmi 205
cd00189 2 ALLNLGNLYYKLGDYDEALEYYEKALELDPD------NADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAY---- 71
|
90 100 110
....*....|....*....|....*....|.
gi 15806634 206 tsLNLACVCQLSGGTGAALTLIEEALRHAKT 236
cd00189 72 --YNLGLAYYKLGKYEEALEAYEKALELDPN 100
|
|
cl02429 |
141413 |
TPR |
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here |
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[... |
2 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
6e-79 |
290.86 |
61.24 |
12,385,224,36,421,261,32,457,293,8,465,304,8,473,313,10,483,324,9,494,333,55,549,389,44,594,433,110,706,543,6,712,553,45,758,598,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 386 EEGRTQQRLAAQLRHDALTGLPNRLALHEALGQQVA-ADSAPFALLCLDLDHFKTVNHTLGQPAGDALLlyigERVQAAV 464
PRK10060 225 EERRAQERLRILANTDSITGLPNRNAIQELIDHAIAqADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLL----QDVSLAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 465 G---EQGQTFRR-GGNEFVVLLP-AVRAAPDALtiAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSLTLQKNAD 539
PRK10060 301 LsclEEDQTLARlGGDEFLVLAShTSQAALEAM--ASRILTRLRLPFRIGLIEVYTGCSIGIALSPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 540 LALHAAKQEG-GQAQRYRNALSQAANERLELTQALRSGIGNGELVLHYQPIVEVRsGKTVAVEALVRWQHPRLGLLSPDR 618
PRK10060 379 TAMYTAKEGGrGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 619 FIGLAEDNGLIVPLGRWVLNTALRQLAAWREHWPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQTIC 698
PRK10060 458 FISYAEESGLIVPLGRWVILDVVRQAAKWRDKGINLRVAVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESCLI 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 699 DEEALEpfLPLIRE----GLRLAIDDFGTGYSSLSRLYRLPAQILKLDRSLIQDLSADNATDGpLVSALIAFAQRFGMQV 774
PRK10060 538 ENEELA--LSVIQQfsqlGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQS-LVRAIVAVAQALNLQV 614
|
410
....*....|....*.
gi 15806634 775 TAEGIETAEQLHLLRQ 790
PRK10060 615 IAEGVETAKEDAFLTK 630
|
|
|
|
|
|
|
-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 |
6e-73 |
270.74 |
62.29 |
8,376,208,22,400,230,22,422,255,127,549,383,99,651,482,45,696,528,16,712,545,38,751,583,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 377 TLAEKRRLKEEGRTQQRLAAQLrhDALTGLPNRLALHEALGQQVAA---DSAPFALLCLDLDHFKTVNHTLGQPAGDALL 453
COG5001 209 TLTQRAEETRRLSDENDRLANL--DSLTGLPNRRRFFAELDARLAAarqSGRRLVLGVIDLDGFKPVNDAFGHATGDRLL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 454 LYIGERVQAAVGEQGQTFRRGGNEFVVLLPAVRAAPDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSLT 533
COG5001 287 IEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQ 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 534 LQKNADLALHAAKQEG-GQAQRYRNALSQAANERLELTQALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLG 612
COG5001 367 LFERADYALYHAKQNGkGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 613 LLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWRehwPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEI 692
COG5001 447 PVPPDVFIGIAERSGQIVELTRLLLAKALREARAWP---MDVRVSINLSARDLASMENVRRLLAIVSESCIAPHRLDFEI 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 693 TEQT-ICDEEALEPFLPLIRE-GLRLAIDDFGTGYSSLSRLYRLPAQILKLDRSLIQDLSaDNATDGPLVSALIAFAQRF 770
COG5001 524 TETAiVCDFDQARDALAALHElGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLE-ENPTSEDIVRTVLQLGRNL 602
|
410
....*....|....*....
gi 15806634 771 GMQVTAEGIETAEQLHLLR 789
COG5001 603 RMECVVEGVETEAQRDRVA 621
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
5e-70 |
260.93 |
50.56 |
9,385,363,41,427,404,61,489,465,34,525,499,27,552,527,97,649,627,4,655,631,43,698,676,59,758,735,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 386 EEGRTQQRLAAQLRHDALTGLPNRLALHEALGQQVAADSAPfALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVG 465
PRK11359 364 EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP-VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 466 EQGQTFRRGGNEFVVLLPAVRAApDALTIAQTLLDTINEPLLLDGQALVVTASIGLALfpEDGRDSLTLQKNADLALHAA 545
PRK11359 443 PDQYLCRIEGTQFVLVSLENDVS-NITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 546 KQEGGQA-QRYRNALSQAANERLELTQALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAE 624
PRK11359 520 RKNGGNGwQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 625 DNGLIVPLGRWVLNTALRQLAAWRE---HWPElrVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQTIC--D 699
PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSqniHIPA--LSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMehD 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 700 EEALEPFLPLIREGLRLAIDDFGTGYSSLSRLYRLPAQILKLDRSLIQDLSADNATDGpLVSALIAFAQRFGMQVTAEGI 779
PRK11359 678 TEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILA-LLEAITSIGQSLNLTVVAEGV 756
|
410
....*....|.
gi 15806634 780 ETAEQLHLLRQ 790
PRK11359 757 ETKEQFEMLRK 767
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
6e-58 |
220.79 |
62.83 |
8,388,214,11,399,232,10,410,242,114,525,356,24,549,381,150,699,533,34,733,570,21,758,591,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 389 RTQQRLAAQLR-------HDALTGLPNRlALHEALGQQVAADSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQ 461
PRK13561 215 LNQQLLQRHYEeqnenamRFPVSDLPNK-ALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 462 AAVGEQGQTFRRGGNEFVVLLPAVRAAPDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFpEDGRDSLTLQKNADLA 541
PRK13561 294 SVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAVSA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 542 LHAAKQEG-GQAQRYRNALSQAANERLELTQALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFI 620
PRK13561 373 AFTARRKGkNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPDGLI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 621 GLAEDNGLIVPLGRWVLNTALRQLAAWREHWPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQTICD- 699
PRK13561 453 DRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDd 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 700 -EEALEPFLPLIREGLRLAIDDFGTGYSSLSRLYR---LPAQILKLDRSLIQDLSADNAtdgpLVSALIAFAQRFGMQVT 775
PRK13561 533 pHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVDGLPEDSS----MVAAIIMLAQSLNLQMI 608
|
410
....*....|....*
gi 15806634 776 AEGIETAEQLHLLRQ 790
PRK13561 609 AEGVETEAQRDWLAK 623
|
|
|
|
|
|
|
-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 |
2e-49 |
192.87 |
43.32 |
3,563,263,149,712,413,44,757,457,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 564 NERLELTQALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQ 643
COG4943 264 RRYLSPRRRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRD 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 644 LAAWREHWPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQTICDEEALEPFLPLIRE-GLRLAIDDFG 722
COG4943 344 LGDLLRQHRDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFADPKKMTPIILRLREaGHEIYIDDFG 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15806634 723 TGYSSLSRLYRLPAQILKLDRSLIQDLSADNATDgPLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
COG4943 424 TGYSNLHYLQSLPVDALKIDKSFVDTLGTDSASH-LIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRK 490
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
5e-45 |
177.97 |
36.83 |
13,386,675,7,393,683,25,418,710,13,431,724,54,486,778,18,504,797,45,549,843,23,572,868,31,603,900,36,640,936,60,700,997,12,712,1010,37,750,1047,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 387 EGRTQQR-LAAQLRHDALTGLPNRLALHEALGQ--QVAADSAPFALLC-LDLDHFKTVNHTLGQPAGDALLLYIGERVQA 462
PRK09776 676 ESRAMLRqLSYSASHDALTGLANRASFEKQLREalQTVNSTHQRHALVfIDLDRFKAVNDSAGHAAGDALLRELASLMLS 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 463 AVGEQGQTFRRGGNEFVVLLPAVrAAPDALTIAQTLLDTINE-PLLLDGQALVVTASIGLALFPEDGRDSLTLQKNADLA 541
PRK09776 756 MLRSSDVLARLGGDEFGLLLPDC-NVESARFIATRIISAINDyRFPWEGRVYRVGASAGITAIDDNNHQASEVMSQADIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 542 LHAAKQEG-GQAQRYRNALSQAANERLELTQA--LRSGIGNGELVLHYQPIVEVRSGKTVAVEAL-VRWQHPRLGLLSPD 617
PRK09776 835 CYAAKNAGrGRVTVYEPQQAAAHSERRELSLAeqWRSMLEENQLMLQAQEIASPRIPEARNLWLIsLRLWDCEGEIIDEG 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 618 RFIGLAEDNGLIVPLGRWVLNTaLRQLAAWREHWPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEITEQTI 697
PRK09776 915 AFRPAAEDPALMHALDRWVIHE-LFQQGARAVASKGLSIAIPLSVASLSSATLLPFLLEQLENSPLPPRLLHLEITETAL 993
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 698 CDE-EALEPFLPLIRE-GLRLAIDDFGTGYSSLSRLYRLPAQILKLDRSLIQDLsADNATDGPLVSALIAFAQRFGMQVT 775
PRK09776 994 LNHaEAASRLVQKLRLaGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANL-QGNLMDEMLVSIINGIAQRLGMKTI 1072
|
410
....*....|....
gi 15806634 776 AEGIETAEQLHLLR 789
PRK09776 1073 AGPVELPLTLDTLS 1086
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
1e-43 |
173.35 |
57.14 |
9,383,278,12,395,296,6,401,303,25,426,330,123,549,454,151,702,605,10,712,619,15,727,637,27,758,664,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 384 LKEEGRTQQRLA------AQLRHD-ALTGLPNRLALHEALGQQVAADSAP--FALLCLDLDHFKTVNHTLGQPAGDALLL 454
PRK11829 279 VRNYNRNQQLLAdayadmGRISHRfPVTELPNRSLFISLLEKEIASSTRTdhFHLLVIGIETLQEVSGAMSEAQHQQLLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 455 YIGERVQAAVGEQGQTFRRGGNEFVVLLPAVRAAPDALTIAQTLLDTINEPLLLDGQALVVTASIGLALFPEDGRDSLTL 534
PRK11829 359 TIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 535 QKNADLALHAAKQEG-GQAQRYRNALSQAANERLELTQALRSGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGL 613
PRK11829 439 MRNASTAMMAAHHEGrNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSY 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 614 LSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWREHWPELRVSVNMAPRQLQQPGSCQEIRDALRAYALPPDALELEIT 693
PRK11829 519 VLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEIT 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 694 EQTICDEeaLEPFLPLIRE----GLRLAIDDFGTGYSS---LSRLYRLPAQILKLDRSLIQDLSADNAtdgpLVSALIAF 766
PRK11829 599 ETAQIQD--LDEALRLLRElqglGLLIALDDFGIGYSSlryLNHLKSLPIHMIKLDKSFVKNLPEDDA----IARIISCV 672
|
410 420
....*....|....*....|..
gi 15806634 767 AQRFGMQVTAEGIETAEQLHLL 788
PRK11829 673 SDVLKVRVMAEGVETEEQRQWL 694
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
3e-38 |
155.60 |
41.89 |
7,574,269,79,653,349,23,677,372,3,681,375,8,689,385,11,700,397,55,756,452,34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 575 SGIGNGELVLHYQPIVEVRSGKTVAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWREHWPE- 653
PRK10551 270 TAIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLPVg 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 654 LRVSVNMAPRQLQQPGSCQEIRDaLRAyALPPDALE--LEITEQTICDE-EALEPFLPLIREGLRLAIDDFGTGYSSLSR 730
PRK10551 350 AKLGINIAPAHLHSDSFKADVQR-LLA-SLPADHFQivLEITERDMLQEeEALKLFAWLHSQGIEIAIDDFGTGHSALIY 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 731 LYRLPAQILKLDRSLIQDLSADNATdGPLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
PRK10551 428 LERFTLDYLKIDRGFINAIGTETVT-SPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRE 486
|
|
|
|
|
|
|
-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-19 |
93.06 |
42.30 |
5,371,242,18,389,261,25,414,289,70,485,359,19,504,381,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 372 RLRSETLAEKRRLKEEGR-TQQRLAAQLRHDALTGLPNRLALHE---ALGQQVAADSAPFALLCLDLDHFKTVNHTLGQP 447
COG3706 243 RARLRRQLRRKRYERQLReSLERLQELALVDGLTGLFNRRYFDEhlaDLWKRALREGRPLSLLMLDIDDFKEINDTYGHD 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 448 AGDALLLYIGERVQAAVGEQGQTFRRGGNEFVVLLPAvRAAPDALTIAQTLLDTINE---PLLLDGQALVVTASIGLALF 524
COG3706 323 VGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLPD-TDLEAAIAIAERIRQKINElpfVHELSREPLEVTISIGVAEG 401
|
170 180
....*....|....*....|....*
gi 15806634 525 PEDGRDSLTLQKNADLALHAAKQEG 549
COG3706 402 KPGEDSIEELLKRADKALYKAKASG 426
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
1e-17 |
87.28 |
42.45 |
10,358,262,10,380,272,3,388,275,12,400,294,9,409,305,4,413,310,75,489,385,13,502,399,10,512,411,37,555,448,8 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 359 EQLAAVNLQLeaerlrsetlaeKRRlkeegRTQQRLAAQLRH-------DALTGLPNR--LALH-EALGQQVAADSAPFA 428
PRK09581 263 ELLARVRTQI------------RRK-----RYQDALRQNLEQsiemavtDGLTGLHNRryFDMHlKQLIERANERGKPLS 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 429 LLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVGEQGQTFRRGGNEFVVLLPAVRAApDALTIAQTLLDTI-NEPLL 507
PRK09581 326 LMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYGGEEFVVVMPDTDIE-VAIAVAERIRRKIaEEPFA 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15806634 508 LDGQA--LVVTASIGLALFPEDGRDSLTLQKNADLALHAAKQEGgqaqryRNALSQAA 563
PRK09581 405 ISDGKerLNVTVSIGVAELRPSGESIEALIKRADKALYEAKNTG------RNRVVALA 456
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
1e-17 |
86.86 |
65.42 |
19,371,204,5,377,209,5,384,214,29,413,246,58,471,306,13,485,319,14,499,336,15,517,351,9,527,360,25,552,386,13,565,404,9,578,413,13,592,426,58,652,484,32,684,517,16,700,534,12,712,547,35,747,584,8,758,592,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 372 RLRSEtLAEKRrlKEEGRTQQRLAAQLRHDALTGLPNRLALH---EALGQQVAADSAPFALLCLDLDHFKTVNHTLGQPA 448
PRK11059 205 HLLEE-LQDAR--KERSRFDTFIRSNAFLDAKTGLGNRLFFDnqlDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 449 GDALLLYIGERVQAAVGEQGQTF--RRGGNEFVVLLPAvRAAPDALTIAQTLL---DTINEPLLLDGQALVvtaSIGLAL 523
PRK11059 282 VDELLFELINLLSTFVQRYPGALlaRYSRSDFAVLLPH-RSLKEADSLASQLLkavDSLPPPKMLDRDDFL---HIGIAA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 524 FPEdGRDSLTLQKNADLALHAAKQEGGQA-QRYRNALSQAANE-----RLELTQALRsgigNGELVLHYQPIVEvRSGKT 597
PRK11059 358 YRS-GQSTEQVMEEAEMALRSAQLQGGNSwFMYDKAQDPEKGRgsvrwRTLLEQALV----RGGPRLYQQPVVT-RDGQV 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 598 VAVEALVRWQHPRLGLLSPDRFIGLAEDNGLIVPLGRWVLNTALRQLAAWREHwpELRVSVNMAPRQLQQPGSCQEIRDA 677
PRK11059 432 HHRELMCRIRDGQGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLSYWPEE--SQNLSINLSVDSLLSRAFQRWLRDT 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 678 LRAYALP-PDALELEITEQTICDE-EALEPFLPLIRE-GLRLAIDDFGTGYSSLSRLYRLPAQILKLDRSLIQ--DLSAD 752
PRK11059 510 LLQCERSqRKRLIFELAEADVVQHiDRLRPVLRMLRGlGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRniHQRTE 589
|
410 420 430
....*....|....*....|....*....|....*...
gi 15806634 753 NATdgpLVSALIAFAQRFGMQVTAEGIETAEQLHLLRQ 790
PRK11059 590 NQL---FVRSLVGACAGTETQVFAEGVESREEWQTLQI 624
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
5e-16 |
81.60 |
41.77 |
5,379,230,19,399,249,26,425,277,81,506,359,22,529,381,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 380 EKRRLKEEGRTQQRLAAQLrHDALTGLPNRLALHEALGQQVAADSA--PFALLCLDLDHFKTVNHTLGQPAGDALLLYIG 457
PRK09966 231 EEWQLRLQAKNAQLLRTAL-HDPLTGLANRAAFRSGINTLMNNSDArkTSALLFLDGDNFKYINDTWGHATGDRVLIEIA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 458 ERVQAAVGEQGQTFRRGGNEFVVLLPAVRAAPDALTIAQTLLDTINEPL-LLDGQALVVTASIGLALFPEDGrDSLTLQK 536
PRK09966 310 KRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFdLHNGHQTTMTLSIGYAMTIEHA-SAEKLQE 388
|
170
....*....|..
gi 15806634 537 NADLALHAAKQE 548
PRK09966 389 LADHNMYQAKHQ 400
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
9e-15 |
77.44 |
50.85 |
5,400,132,19,419,152,103,522,256,3,525,260,9,537,269,12 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 401 DALTGLPNRLALHEALGQQ-VAADSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGERVQAAVGEQGQTFRRGGNEFV 479
PRK09894 133 DVLTGLPGRRVLDESFDHQlRNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEEFI 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15806634 480 VLLPAVRAAPDALTIAQTLLDTINEPLLLDGQALVVTASIGLA-LFP-EDGRDSLTLqknADLALHAAKQEG 549
PRK09894 213 IILKAATDEEACRAGERIRQLIANQAITHSEGRINITATFGVTrAFPeEPLDEVIGR---ADRAMYEGKQAG 281
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
1e-07 |
53.75 |
44.74 |
7,382,197,7,392,204,30,422,237,63,486,300,36,522,337,6,528,345,4,535,349,14 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 383 RLKEEGRtqqRLAAQLRHDALTGLPNRLALHEALGQQVAA---DSAPFALLCLDLDHFKTVNHTLGQPAGDALLLYIGER 459
PRK10245 198 KLAEHKR---RLQVMSTRDGMTGVYNRRHWETMLRNEFDNcrrHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 460 VQAAVGEQGQTFRRGGNEFVVLLPAVrAAPDALTIAQTLLDTINEPLLLDGQALVVTASIGLA-LFPEDG--RDSLtlqK 536
PRK10245 275 LQITLRGSDVIGRFGGDEFAVIMSGT-PAESAITAMLRVHEGLNTLRLPNAPQVTLRISVGVApLNPQMShyREWL---K 350
|
170
....*....|...
gi 15806634 537 NADLALHAAKQEG 549
PRK10245 351 SADLALYKAKKAG 363
|
|
|
|
|
|
|
-1 |
| 137202 |
PRK09303 |
PRK09303 |
adaptive-response sensory kinase; Validated |
adaptive-response sensory kinase; Validated |
true |
true |
false |
378 |
8e-04 |
41.10 |
25.40 |
2,297,106,41,344,147,55 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15806634 298 GRPAEARPALEAGLRAAQDLRLNDAEGRARRCYAQLLEDQDdyqgalAQVRALAQLEHDLREQLAAVNLQLEAERLRSET 377
PRK09303 107 GLGLSLRPSESDVGRTQELLQLSDELFVLRQENETLLEQLK------FKDRLLAMLAHDLRTPLTAASLAVETLELGQID 180
|
90 100
....*....|....*....|..
gi 15806634 378 LAEKRRLKEEGRTQQRLAAQLR 399
PRK09303 181 PSEELSPALIEQLQDQARRQLE 202
|
|
|
|
|
|
|
-1 |
|