| 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 |
8e-65 |
242.81 |
100.00 |
2,194,0,77,271,79,161 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 195 SEFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLATI--G 272
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWqaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 273 DPHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQTSL 352
cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 353 GYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPMPLVD 432
cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 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 |
| 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-37 |
150.82 |
96.18 |
3,17,0,25,48,25,64,112,91,60 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 18 HDALTGLPNRAAFQRSGEAAVARAVsrrlgvRREGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRKGDTV 97
cd01949 1 TDPLTGLPNRRAFEERLERLLARAR------RSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLV 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117928869 98 ARLGGDEFGLILRDT--ADPHDALCRIRGLIESELDVAGIPLAVEASIGYAVTPDDAATIEELLQYADVAVHHAKAR 172
cd01949 75 ARLGGDEFAILLPGTdlEEAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRS 151
|
|
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-64 |
242.12 |
99.17 |
2,195,2,76,271,80,161 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 196 EFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLATI--GD 273
smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqaQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 274 PHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQTSLG 353
smart00052 83 PPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117928869 354 YLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPMPLVD 432
smart00052 163 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 241
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 32382 |
COG2200 |
Rtn |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
false |
false |
false |
256 |
2e-60 |
227.90 |
98.05 |
2,190,1,83,273,85,167 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 191 LSLISEFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLAT 270
COG2200 2 LQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 271 IGD-PHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQ 349
COG2200 82 WPRaGPLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGTGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 350 TSLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPMP 429
COG2200 162 SSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPLP 241
|
250
....*....|.
gi 117928869 430 LVDLRRWLAGS 440
COG2200 242 ADALDALLSSS 252
|
|
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-49 |
190.32 |
99.15 |
5,195,2,76,271,83,28,300,111,20,321,131,52,374,183,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 196 EFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLATI---- 271
pfam00563 3 ALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWrgna 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 272 -GDPHLAVAVNISARNLSRHTFAADVKAAvRRAGIEPHRLVLELTETALLfDPTRAHDVFTDLTSYGIRVSIDDFGRGQT 350
pfam00563 83 lLPPDLPLSVNLSPASLLDPSFLEALLAL-KQGGLPPSRLVLEITESDLD-EDLRLLEALARLRSLGFRLALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117928869 351 SLGYLSALPLSEIKIDRTFVRDMvTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARP 427
pfam00563 161 SLSYLSRLPPDYIKIDRSFIKDL-SDPESRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 236
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
4e-34 |
141.23 |
95.71 |
4,13,0,29,48,29,64,114,93,6,120,103,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 14 YQARHDALTGLPNRAAFQRSGEAAVARAVsrrlgvRREGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRK 93
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQ------RQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 94 GDTVARLGGDEFGLILRDTadPHDALC----RIRGLIESELDVAGIPLAVEASIGYAVTPDDAATIEELLQYADVAVHHA 169
smart00267 75 GDLLARLGGDEFALLLPET--SLEEAIalaeRILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQA 152
|
....
gi 117928869 170 KARH 173
smart00267 153 KKAG 156
|
|
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 |
1e-33 |
139.30 |
98.12 |
4,15,0,33,54,33,62,116,97,12,128,112,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 16 ARHDALTGLPNRAAFQRSGEAAVARAVSRRLGVrregttAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRKGD 95
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPL------ALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 96 TVARLGGDEFGLILRDTADPH--DALCRIRGLIES---ELDVAGIPLAVEASIGYAVTPDDAATIEELLQYADVAVHHAK 170
pfam00990 75 LVARLGGDEFAILLPDTSLEGaqELAERIRRLLAAlkiPHTLSGLPLYVTISIGIAAYPNDGEDAEDLLKRADQALYQAK 154
|
...
gi 117928869 171 ARH 173
pfam00990 155 NQG 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 |
5e-30 |
127.54 |
97.79 |
4,0,4,42,48,46,72,120,120,35,155,156,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 1 MTRRLRTEVARNAYQARHDALTGLPNRAAFQRSGEAAVARAVsrrlgvRREGTTAVAVIDLDRFKAINDTLGPRNGDVLL 80
COG2199 5 LLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARAR------RHGEPLALLLLDLDHFKQINDTYGHAAGDEVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 81 RRIAERLASHTRKGDTVARLGGDEFGLILRDTADPHDALC--RIRGLIESELDVAGIPLAVEASIGYAVTPDDAATI-EE 157
COG2199 79 REVARRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLaeRIRAALEEPFFLGGEELRVTVSIGVALYPEDGSDDaEL 158
|
170 180
....*....|....*....|...
gi 117928869 158 LLQYADVAVHHAKARHLGVVRYH 180
COG2199 159 LLRRADLALYRAKRAGRNRVVVF 181
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
4e-26 |
114.36 |
98.79 |
7,14,0,27,48,27,4,52,32,60,113,92,7,120,102,8,128,111,8,136,120,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 15 QARHDALTGLPNRAAFQRSGEAAVARAvsrrlgvRREG-TTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRK 93
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRA-------RRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 94 GDTVARLGGDEFGLILRDTaDPHDALC---RIRGLIES-ELDVAGIP-LAVEASIGYAVTPDDAATIEELLQYADVAVHH 168
TIGR00254 74 SDVVGRYGGEEFVVILPGT-PLEDALSkaeRLRDAINSkPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQ 152
|
170
....*....|.
gi 117928869 169 AKARHLGVVRY 179
TIGR00254 153 AKKAGRNRVVV 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 |
| 34606 |
COG5001 |
COG5001 |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms] |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF... |
false |
true |
false |
663 |
3e-79 |
290.77 |
66.82 |
8,1,216,7,11,223,19,30,244,18,56,262,72,128,337,68,196,406,71,268,477,167,435,646,13 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 2 TRRLRTEvarNAYQARHDALTGLPNRAAF--QRSGEAAVARAVSRRLGVrregttavAVIDLDRFKAINDTLGPRNGDVL 79
COG5001 217 TRRLSDE---NDRLANLDSLTGLPNRRRFfaELDARLAAARQSGRRLVL--------GVIDLDGFKPVNDAFGHATGDRL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 80 LRRIAERLASHTRKGDTVARLGGDEFGLILRDTADPHDALCRIRGLIES---ELDVAGIPLAVEASIGYAVTPDDAATIE 156
COG5001 286 LIEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESlqaPYDLRGVRVQVGASIGIAPFPSGADTSE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 157 ELLQYADVAVHHAKARHLGVVRYHPSQNHYDAASLSLISE-FRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPAR 235
COG5001 366 QLFERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQaLRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEI 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 236 GLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDlATIGDPHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELT 315
COG5001 446 GPVPPDVFIGIAERSGQIVELTRLLLAKALRE-ARAWPMDVRVSINLSARDLASMENVRRLLAIVSESCIAPHRLDFEIT 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 316 ETALLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQTSLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGL 395
COG5001 525 ETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLRM 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 117928869 396 IVVAEGVETAEVGDELRECGCDVAQGYWFARPMPLVDLRR--WLAGSDRGDFSLA 448
COG5001 605 ECVVEGVETEAQRDRVAALGATVMQGYHYARPMPAEERRRrgRGAGPDVWDADFC 659
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
2e-70 |
261.59 |
64.71 |
9,10,226,5,15,236,25,48,261,67,115,334,8,123,347,4,136,351,42,178,394,39,218,433,56,274,491,164 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 11 RNAYQ-----ARHDALTGLPNRAAFQRSGEAAVARavsrrlgvRREGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAE 85
PRK10060 227 RRAQErlrilANTDSITGLPNRNAIQELIDHAIAQ--------ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 86 RLASHTRKGDTVARLGGDEFGLILRDTADP------HDALCRIR-----GLIEseldvagipLAVEASIGYAVTPDDAAT 154
PRK10060 299 AILSCLEEDQTLARLGGDEFLVLASHTSQAaleamaSRILTRLRlpfriGLIE---------VYTGCSIGIALSPEHGDD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 155 IEELLQYADVAVHHAKARHLGVVR-YHPSQNHYDAASLSLISEFRRAVTDNQLVLHYQPKAKLSdGAVEAIEALVRWHHP 233
PRK10060 370 SESLIRSADTAMYTAKEGGRGQFCvFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSP 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 234 ARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLATIGDP--HLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLV 311
PRK10060 449 ERGLIPPLEFISYAEESGLIVPLGRWVILDVVRQAAKWRDKgiNLRVAVNVSARQLADQTIFTALKQVLQELNFEYCPID 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 312 LELTETALLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQTSLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGH 391
PRK10060 529 VELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQ 608
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 117928869 392 NLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPMPLVDLRRWLA 438
PRK10060 609 ALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYK 655
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
3e-63 |
237.68 |
37.63 |
7,12,684,33,51,717,65,116,791,18,140,809,37,177,849,35,212,885,60,272,946,158 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 13 AYQARHDALTGLPNRAAFQRSGEAAVARAVSRRlgvrreGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTR 92
PRK09776 685 SYSASHDALTGLANRASFEKQLREALQTVNSTH------QRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 93 KGDTVARLGGDEFGLILRDTADPH---------DALCRIRGLIESELDVAGiplaveASIGYAVTPDDAATIEELLQYAD 163
PRK09776 759 SSDVLARLGGDEFGLLLPDCNVESarfiatriiSAINDYRFPWEGRVYRVG------ASAGITAIDDNNHQASEVMSQAD 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 164 VAVHHAKARHLGVV---RYHPSQNHYDAASLSLISEFRRAVTDNQLVLHYQP-KAKLSDGAVEAIEALVRWHHPARGLLY 239
PRK09776 833 IACYAAKNAGRGRVtvyEPQQAAAHSERRELSLAEQWRSMLEENQLMLQAQEiASPRIPEARNLWLISLRLWDCEGEIID 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 240 PDVFVPLVEQTDLIDDLTRWVLRHALEDLATIG-DPHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETA 318
PRK09776 913 EGAFRPAAEDPALMHALDRWVIHELFQQGARAVaSKGLSIAIPLSVASLSSATLLPFLLEQLENSPLPPRLLHLEITETA 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 319 LLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQTSLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVV 398
PRK09776 993 LLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEMLVSIINGIAQRLGMKTI 1072
|
410 420 430
....*....|....*....|....*....|..
gi 117928869 399 AEGVETAEVGDELRECGCDVAQGYWFARPMPL 430
PRK09776 1073 AGPVELPLTLDTLSGIGVDLAQGYVIGRPQPL 1104
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
2e-57 |
218.56 |
51.94 |
7,16,376,28,54,404,58,113,462,5,118,470,26,146,496,33,179,530,97,276,630,161 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 17 RHDALTGLPNRAAFQRSGEAAVARAVSRrlgvrregttAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRKGDT 96
PRK11359 377 QFDPMTGLPNRNNLHNYLDDLVDKAVSP----------VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQY 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 97 VARLGGDEFGLILRDTaDPHDA---LCRIRGLIESELDVAGIPLAVEASIGyaVTPDDAATIEELLQYADVAVHHAKARH 173
PRK11359 447 LCRIEGTQFVLVSLEN-DVSNItqiADELRNVVSKPIMIDDKPFPLTLSIG--ISYDVGKNRDYLLSTAHNAMDYIRKNG 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 174 LGVVRY-HPSQNHYDAASLSLISEFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDL 252
PRK11359 524 GNGWQFfSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGE 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 253 IDDLTRWVLRHALEDLATIGDPHL---AVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLFDPTRAHDV 329
PRK11359 604 IENIGRWVIAEACRQLAEWRSQNIhipALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKR 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 330 FTDLTSYGIRVSIDDFGRGQTSLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGD 409
PRK11359 684 IQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFE 763
|
410 420
....*....|....*....|....*...
gi 117928869 410 ELRECGCDVAQGYWFARPMPLVDLRRWL 437
PRK11359 764 MLRKIHCRVIQGYFFSRPLPAEEIPGWM 791
|
|
|
|
|
|
|
-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 |
1e-42 |
169.37 |
47.52 |
3,190,266,81,271,349,49,321,398,117 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 191 LSLISEFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLAT 270
COG4943 267 LSPRRRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 271 I--GDPHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLfDPTRAHDVFTDLTSYGIRVSIDDFGRG 348
COG4943 347 LlrQHRDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFA-DPKKMTPIILRLREAGHEIYIDDFGTG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 349 QTSLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPM 428
COG4943 426 YSNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKAL 505
|
250
....*....|
gi 117928869 429 PLVDLRRWLA 438
COG4943 506 PAQAFLDWAE 515
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
2e-41 |
164.94 |
64.36 |
10,14,229,27,51,256,69,120,328,32,153,360,13,168,373,7,175,383,99,274,484,82,356,569,20,379,589,54,433,644,4 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 15 QARHDALTGLPNRAAFQRSGEAAVARAvsrrlgvrreGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRKG 94
PRK13561 230 NAMRFPVSDLPNKALLMALLEQVVARK----------QTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 95 DTVARLGGDEFGLILRDTADPHDALC---RIRGLIESELDVAGIPLAVEASIGYAVTPDDAaTIEELLQYADVAVhhAKA 171
PRK13561 300 MVLAQISGYDFAIIANGVKEPWHAITlgqQVLTIINERLPIQRIQLRPSCSIGIAMFYGDL-TAEQLYSRAVSAA--FTA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 172 RHLG---VVRYHPSQNHYDAASLSLISEFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVE 248
PRK13561 377 RRKGknqIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPDGLIDRIE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 249 QTDLIDDLTRWVLRHALEDLATIGDP--HLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLFDPTRA 326
PRK13561 457 SCGLMVTVGHWVLEESCRLLAAWQERgiMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAA 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 327 HDVFTDLTSYGIRVSIDDFGRGQTSLGYLS---ALPLSEIKIDRTFVRDMVTNaahAAIVRSVVELGHNLGLIVVAEGVE 403
PRK13561 537 VAILRPLRNAGVRIALDDFGMGYAGLRQLQhmkSLPIDVLKIDKMFVDGLPED---SSMVAAIIMLAQSLNLQMIAEGVE 613
|
410 420 430
....*....|....*....|....*....|....*
gi 117928869 404 TAEVGDELRECGCDVAQGYWFARPMPLVDL-RRWL 437
PRK13561 614 TEAQRDWLAKAGVGVAQGFLFARPLPIEIFeERYL 648
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
1e-30 |
129.02 |
47.10 |
5,195,266,72,267,341,32,301,373,7,308,382,12,321,394,116 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 196 EFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALED---LATIG 272
PRK10551 267 EILTAIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDaaeLQKVL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 273 DPHLAVAVNISARNLSRHTFAADVKAAvrRAGIEPH--RLVLELTETALLfDPTRAHDVFTDLTSYGIRVSIDDFGRGQT 350
PRK10551 347 PVGAKLGINIAPAHLHSDSFKADVQRL--LASLPADhfQIVLEITERDML-QEEEALKLFAWLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 351 SLGYLSALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPMPL 430
PRK10551 424 ALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISRPLPL 503
|
....*..
gi 117928869 431 VDLRRWL 437
PRK10551 504 DDFVKWL 510
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
2e-30 |
128.66 |
56.04 |
8,20,304,22,49,326,71,120,400,24,144,427,43,189,470,80,269,552,87,356,642,33,392,675,37 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 21 LTGLPNRAAFQRSGEAAVARAVsrrlgvrREGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRKGDTVARL 100
PRK11829 305 VTELPNRSLFISLLEKEIASST-------RTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 101 GGDEFGLILRDTADPHDALC---RIRGLIESELDVAGIPLAVEASIG---YAVTPDDAATIEELLQYADVAVHHAKARHL 174
PRK11829 378 SKTEFAVLARGTRRSFPAMQlarRIMSQVTQPLFFDEITLRPSASIGitrYQAQQDTAESMMRNASTAMMAAHHEGRNQI 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 175 GVVRYHPSQNHYDaaSLSLISEFRRAVTDNQLVLHYQPKAKLSDGAVEAIEALVRWHHPARGLLYPDVFVPLVEQTDLID 254
PRK11829 458 MVFEPHLIEKTHK--RLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMV 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 255 DLTRWVLRHALEDLA--TIGDPHLAVAVNISARNLSRHTFAADVKAAVRRAGIEPHRLVLELTETALLFDPTRAHDVFTD 332
PRK11829 536 PLGNWVLEEACRILAdwKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRE 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 333 LTSYGIRVSIDDFGRGQTSLGYLS---ALPLSEIKIDRTFVRDMVTNAAHAAIVRSVVELghnLGLIVVAEGVETAEVGD 409
PRK11829 616 LQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDV---LKVRVMAEGVETEEQRQ 692
|
410 420
....*....|....*....|
gi 117928869 410 ELRECGCDVAQGYWFARPMP 429
PRK11829 693 WLLEHGIQCGQGFLFSPPLP 712
|
|
|
|
|
|
|
-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 |
5e-22 |
100.76 |
38.62 |
5,2,256,40,48,296,64,113,360,7,120,370,8,128,381,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 3 RRLRTEVARNAYQARHDALTGLPNRAAFQRSGEAAVARAVsrrlgvRREGTTAVAVIDLDRFKAINDTLGPRNGDVLLRR 82
COG3706 257 RQLRESLERLQELALVDGLTGLFNRRYFDEHLADLWKRAL------REGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 83 IAERLASHTRKGDTVARLGGDEFGLILRDTaDPHDALC---RIRGLIES---ELDVAGIPLAVEASIGYAVTPDDAATIE 156
COG3706 331 VARRLRQTVRGLDLVARYGGEEFAVVLPDT-DLEAAIAiaeRIRQKINElpfVHELSREPLEVTISIGVAEGKPGEDSIE 409
|
170
....*....|....*
gi 117928869 157 ELLQYADVAVHHAKA 171
COG3706 410 ELLKRADKALYKAKA 424
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
3e-21 |
98.07 |
36.76 |
5,1,277,45,52,322,60,113,382,7,120,392,9,129,404,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 2 TRRLRTEVARNAYQARHDALTGLPNRAAFQRSGEAAVARAVSRRLgvrregTTAVAVIDLDRFKAINDTLGPRNGDVLLR 81
PRK09581 278 QDALRQNLEQSIEMAVTDGLTGLHNRRYFDMHLKQLIERANERGK------PLSLMMLDIDHFKQVNDTYGHDAGDEVLR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 82 RIAERLASHTRKGDTVARLGGDEFGLILRDTaDPHDALC---RIRGLIESE---LDVAGIPLAVEASIGYAVTPDDAATI 155
PRK09581 352 EFAKRLRKNIRGTDLIARYGGEEFVVVMPDT-DIEVAIAvaeRIRRKIAEEpfaISDGKERLNVTVSIGVAELRPSGESI 430
|
170
....*....|....*
gi 117928869 156 EELLQYADVAVHHAK 170
PRK09581 431 EALIKRADKALYEAK 445
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
7e-20 |
93.62 |
49.83 |
5,18,132,28,54,160,60,114,222,12,126,235,22,149,257,21 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 19 DALTGLPNRAAFQRSGEAAVARAVSRRLgvrregttAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASHTRKGDTVA 98
PRK09894 133 DVLTGLPGRRVLDESFDHQLRNREPLNL--------YLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVY 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117928869 99 RLGGDEFGLILRDTAD--PHDALCRIRGLI-ESELDVAGIPLAVEASIGYAVTpDDAATIEELLQYADVAVHHAK 170
PRK09894 205 RYGGEEFIIILKAATDeeACRAGERIRQLIaNQAITHSEGRINITATFGVTRA-FPEEPLDEVIGRADRAMYEGK 278
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
1e-14 |
76.60 |
40.54 |
6,3,235,27,31,262,14,51,276,66,118,342,15,133,362,18,152,380,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 4 RLRTEVARNAYQARHDALTGLPNRAAFqRSGEAAVARAVSRRlgvrreGTTAVAVIDLDRFKAINDTLGPRNGDVLLRRI 83
PRK09966 236 RLQAKNAQLLRTALHDPLTGLANRAAF-RSGINTLMNNSDAR------KTSALLFLDGDNFKYINDTWGHATGDRVLIEI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 84 AERLASHTRKGDTVARLGGDEFGLILRDTADPHDaLCRIRGLIESELDVA-----GIPLAVEASIGYAVTPDDaATIEEL 158
PRK09966 309 AKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESE-VQQICSALTQIFNLPfdlhnGHQTTMTLSIGYAMTIEH-ASAEKL 386
|
170
....*....|....
gi 117928869 159 LQYADVAVHHAKAR 172
PRK09966 387 QELADHNMYQAKHQ 400
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-09 |
58.37 |
42.32 |
6,2,203,9,18,212,9,31,221,22,55,243,57,114,300,24,138,328,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 3 RRLRTEVARnayqarhDALTGLPNRaafqRSGEAAVARAVSRRLGVRREGTtaVAVIDLDRFKAINDTLGPRNGDVLLRR 82
PRK10245 204 RRLQVMSTR-------DGMTGVYNR----RHWETMLRNEFDNCRRHNRDAT--LLIIDIDHFKSINDTWGHDVGDEAIVA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 83 IAERLASHTRKGDTVARLGGDEFGLILRDTadPHDALCRIRGLIESELDVAGIPLA----VEASIGYAVTPDDAATIEEL 158
PRK10245 271 LTRQLQITLRGSDVIGRFGGDEFAVIMSGT--PAESAITAMLRVHEGLNTLRLPNApqvtLRISVGVAPLNPQMSHYREW 348
|
170
....*....|..
gi 117928869 159 LQYADVAVHHAK 170
PRK10245 349 LKSADLALYKAK 360
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
3e-07 |
51.81 |
64.80 |
15,14,226,24,42,250,10,54,260,36,90,297,7,97,305,12,114,317,2,122,319,26,148,346,7,155,364,14,169,390,5,174,399,6,194,405,18,213,423,84,297,514,5,308,519,123 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 15 QARHDALTGLPNRAAFQRSGEAAVaravSRRLGVRREGttAVAVIDLDRFKAINDTLGPRNGDVLLRRIAERLASH-TRK 93
PRK11059 227 NAFLDAKTGLGNRLFFDNQLDTLL----EDQEKVGAHG--VVMLIRLPDFDLLQEELGESQVDELLFELINLLSTFvQRY 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 94 GDTV-ARLGGDEFGLILrdtadPHdalcriRGLIESELDVAGIPLAVEASIGYAVT-PDDAATI-----------EELLQ 160
PRK11059 301 PGALlARYSRSDFAVLL-----PH------RSLKEADSLASQLLKAVDSLPPPKMLdRDDFLHIgiaayrsgqstEQVME 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 161 YADVAVHHA------------KARHL----GVVRYHpsqnhydaaslsliSEFRRAVTDNQLVLHYQPkAKLSDGAVEAI 224
PRK11059 370 EAEMALRSAqlqggnswfmydKAQDPekgrGSVRWR--------------TLLEQALVRGGPRLYQQP-VVTRDGQVHHR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 225 EALVRWHHPARGLLYPDVFVPLVEQTDLIDDLTRWVLRHALEDLATIGDPHLAVAVNISARNLSRHTFAADVK------- 297
PRK11059 435 ELMCRIRDGQGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLSYWPEESQNLSINLSVDSLLSRAFQRWLRdtllqce 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928869 298 AAVRRagiephRLVLELTETALLFDPTRAHDVFTDLTSYGIRVSIDDFGRGQTSLGYLSALPLSEIKIDRTFVRDMVTNA 377
PRK11059 515 RSQRK------RLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHQRT 588
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 117928869 378 AHAAIVRSVVELGHNLGLIVVAEGVETAEVGDELRECGCDVAQGYWFARPMPLV 431
PRK11059 589 ENQLFVRSLVGACAGTETQVFAEGVESREEWQTLQILGVSGGQGDFFASPQPLD 642
|
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|
|
|
|
|
-1 |
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