| 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 |
5e-76 |
280.18 |
100.00 |
2,215,0,79,298,79,161 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 216 GELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDh 295
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 296 pvtAQQDFSMRINASAADLQSLEFVDAVSAALAEEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAG 375
cd01948 80 ---GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 376 YSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPL 455
cd01948 157 YSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
|
....
gi 119962652 456 PEAE 459
cd01948 237 PAEE 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 |
2e-35 |
145.42 |
98.73 |
2,42,0,130,172,131,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 43 TDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLGGD 122
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119962652 123 EFAVLLPATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGLRTAEPH-HSIEDILQEADLAMEDSKNEGRNK 196
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFFIDGEEIRVTASIGIAEYPEDgEDLEELLRRADKALYQAKRSGRNR 155
|
|
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 |
8e-76 |
279.48 |
99.17 |
2,216,2,79,299,81,160 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 217 ELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDHp 296
smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 297 vtaQQDFSMRINASAADLQSLEFVDAVSAALAEEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGY 376
smart00052 82 ---GPPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 377 SSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPLP 456
smart00052 159 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 238
|
...
gi 119962652 457 EAE 459
smart00052 239 LDD 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 |
6e-74 |
273.35 |
98.05 |
2,210,0,86,301,86,165 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 211 QRQIVGELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLR 290
COG2200 1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 291 RWRDHPvtaqqDFSMRINASAADLQSLEFVDAVSAALAEEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEID 370
COG2200 81 TWPRAG-----PLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 371 DFGAGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYY 450
COG2200 156 DFGTGYSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYL 235
|
250
....*....|....*.
gi 119962652 451 FGRPLPEAEFTEQLSR 466
COG2200 236 FSRPLPADALDALLSS 251
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 109613 |
pfam00563 |
EAL |
EAL domain |
EAL domain |
false |
false |
false |
236 |
6e-58 |
219.98 |
99.15 |
6,216,2,77,293,80,11,306,91,17,324,108,31,356,139,45,402,184,52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 217 ELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWR-DH 295
pfam00563 3 ALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWRgNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 296 PVTAQQDFSmrINASAADLQSLEFVDAVsAALAEEHLAPDSLVLELTESAIIQNNELDRYtLASLHRLGVGLEIDDFGAG 375
pfam00563 83 LLPPDLPLS--VNLSPASLLDPSFLEAL-LALKQGGLPPSRLVLEITESDLDEDLRLLEA-LARLRSLGFRLALDDFGTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119962652 376 YSSMGYLRKLPVDRVKVDRQFVKDLGkDPSQLGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRP 454
pfam00563 159 YSSLSYLSRLPPDYIKIDRSFIKDLS-DPESRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 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 |
| 32381 |
COG2199 |
COG2199 |
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms] |
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction... |
false |
false |
false |
181 |
4e-33 |
137.56 |
100.00 |
2,21,0,151,172,153,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 22 HVQALMQELHQARYEQRRDALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVT 101
COG2199 1 ALLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 102 VAMRIRSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGLRTAEPH--HSIEDIL 179
COG2199 81 VARRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDgsDDAELLL 160
|
170 180
....*....|....*....|.
gi 119962652 180 QEADLAMEDSKNEGRNKLKVF 200
COG2199 161 RRADLALYRAKRAGRNRVVVF 181
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
4e-32 |
134.30 |
98.77 |
2,40,2,126,166,129,34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 41 ALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLG 120
smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 121 GDEFAVLLPATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGL-RTAEPHHSIEDILQEADLAMEDSKNEGRNKLKV 199
smart00267 83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVaAYPNPGEDAEDLLKRADTALYQAKKAGRNQVAV 162
|
.
gi 119962652 200 F 200
smart00267 163 Y 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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
3e-30 |
128.13 |
100.00 |
3,40,0,103,143,106,23,166,130,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 41 ALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLG 120
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 121 GDEFAVLLPATPQNRATAVGNRI---LAALEPNIDLGNNSIRCGASVGL-RTAEPHHSIEDILQEADLAMEDSKNEGRNK 196
pfam00990 81 GDEFAILLPDTSLEGAQELAERIrrlLAALKIPHTLSGLPLYVTISIGIaAYPNDGEDAEDLLKRADQALYQAKNQGRNR 160
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
2e-26 |
115.51 |
99.39 |
4,40,1,108,148,113,11,161,124,11,172,136,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 41 ALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLG 120
TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 121 GDEFAVLLPATPQNRATAVGNRILAALE----PNIDLGNNSIRcgASVGLRTAEPH-HSIEDILQEADLAMEDSKNEGRN 195
TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINskpiEVAGSETLTVT--VSIGVACYPGHgLTLEELLKRADEALYQAKKAGRN 159
|
....*.
gi 119962652 196 KLKVFD 201
TIGR00254 160 RVVVAD 165
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
0.001 |
39.69 |
35.29 |
5,366,154,39,405,195,2,408,197,12,422,209,4,426,214,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 367 LEIDDFGAGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPS--QLgFLAAIQHVIHSCglEGVW-EGIETAEQAEALRSIGC 443
PRK11596 155 LWLDDFGTGMANFSALSEVRYDYIKVARELFVMLRQSPEgrTL-FSQLLHLMNRYC--RGVIvEGVETPEEWRDVQRSPA 231
|
90
....*....|...
gi 119962652 444 ASGQGYYFGRPLP 456
PRK11596 232 FAAQGYFLSRPAP 244
|
|
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 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
9e-83 |
302.80 |
65.46 |
11,19,225,11,40,236,14,54,253,15,74,268,98,172,367,30,207,397,5,214,402,3,217,412,20,238,432,56,300,488,7,307,497,162 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 20 ERHVQALMQELhqaryeqrrdALTDALTGLGNRQA---LVNSFIEAQDAAAKGavppaLLLVNLDGFKALKNSAGHAASD 96
PRK10060 226 ERRAQERLRIL----------ANTDSITGLPNRNAiqeLIDHAIAQADNNQVG-----IVYLDLDNFKKVNDAYGHMFGD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 97 QILVTVAMRIRSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGLRTAEPH-HSI 175
PRK10060 291 QLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALSPEHgDDS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 176 EDILQEADLAMEDSKNEGRNKLKVFDPatlhaQLLQRqiVGE-------LREAIRADQLVLYYQPIVELsTGRIEGCEAL 248
PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSP-----EMNQR--VFEylwldtnLRKALENDQLVIHYQPKITW-RGEVRSLEAL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 249 VRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDhpvtaqQDFSMRI--NASAADLQSLEFVDAVSAA 326
PRK10060 443 VRWQSPERGLIPPLEFISYAEESGLIVPLGRWVILDVVRQAAKWRD------KGINLRVavNVSARQLADQTIFTALKQV 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 327 LAEEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQ 406
PRK10060 517 LQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVS 596
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119962652 407 LGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPLPEAEFTEQLSRLRT 469
PRK10060 597 QSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYQK 659
|
|
|
|
|
|
|
-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-81 |
296.55 |
63.20 |
7,35,222,107,142,330,27,170,357,3,173,362,28,202,390,13,215,404,79,301,483,158 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 36 EQRRDALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDV 115
COG5001 223 ENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDGAPIL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 116 VTRLGGDEFAVLLPATPQNRATAVGNR-ILAALEPNIDLGNNSIRCGASVGLRTAePHH--SIEDILQEADLAMEDSKNE 192
COG5001 303 AARLGGDEFALIIPALEDDALRVAGARaLCESLQAPYDLRGVRVQVGASIGIAPF-PSGadTSEQLFERADYALYHAKQN 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 193 GRNKLKVFDpATLHAQLLQRQIV-GELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEAT 271
COG5001 382 GKGAAVLFD-ARHEAAIRDMAVVeQALRSADLEQELSVHFQPIVDIVSGKTIALEALARWHSPEIGPVPPDVFIGIAERS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 272 GLIAELGRWVLRTAVRQLRRWRDhpvtaqqDFSMRINASAADLQSLEFVDAVSAALAEEHLAPDSLVLELTESAIIQNNE 351
COG5001 461 GQIVELTRLLLAKALREARAWPM-------DVRVSINLSARDLASMENVRRLLAIVSESCIAPHRLDFEITETAIVCDFD 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 352 LDRYTLASLHRLGVGLEIDDFGAGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLAAIQHVIHSCGLEGVWEGIET 431
COG5001 534 QARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTVLQLGRNLRMECVVEGVET 613
|
410 420
....*....|....*....|....*...
gi 119962652 432 AEQAEALRSIGCASGQGYYFGRPLPEAE 459
COG5001 614 EAQRDRVAALGATVMQGYHYARPMPAEE 641
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
6e-73 |
269.79 |
54.69 |
8,14,349,20,36,369,7,43,378,16,63,394,103,167,497,36,204,533,12,216,546,84,303,630,156 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 15 RIEKLERHVQALMQELHQARyeQRRDALT--DALTGLGNRQALVNSFieaqDAAAKGAVPPALLLVNLDGFKALKNSAGH 92
PRK11359 350 RVADISQHMAALALEQEKSR--QHIEQLIqfDPMTGLPNRNNLHNYL----DDLVDKAVSPVVYLIGVDHIQDVIDSLGY 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 93 AASDQILVTVAMRIRSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGLrTAEPH 172
PRK11359 424 AWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGI-SYDVG 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 173 HSIEDILQEADLAMEDSKNEGRNKLKVFDPAtLHAQLLQRQIVG-ELREAIRADQLVLYYQPIVELSTGRIEGCEALVRW 251
PRK11359 503 KNRDYLLSTAHNAMDYIRKNGGNGWQFFSPA-MNEMVKERLVLGaALKEAISNNQLKLVYQPQIFAETGELYGIEALARW 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 252 NHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDHPVTAQqdfSMRINASAADLQSLEFVDAVSAALAEEH 331
PRK11359 582 HDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIP---ALSVNLSALHFRSNQLPNQVSDAMHAWG 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 332 LAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLA 411
PRK11359 659 IDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLE 738
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 119962652 412 AIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPLPEAE 459
PRK11359 739 AITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
4e-57 |
217.33 |
68.20 |
12,12,202,39,52,241,9,62,250,9,73,259,8,84,267,13,97,283,31,128,315,80,210,395,7,217,404,81,302,485,82,384,570,21,408,591,55 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 13 DSRIEKLERHVQALMQELHQARYEQRRDALTDALTGLGNrQALVNSFIEaQDAAAKGAVppALLLVNLDgfkALKNSAGH 92
PRK13561 203 DDEIGMLVRSYNLNQQLLQRHYEEQNENAMRFPVSDLPN-KALLMALLE-QVVARKQTT--ALMIITCE---TLRDTAGV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 93 AASDQ---ILVTVAMRIRSAVRENDVVTRLGGDEFAVLL-PATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGLRT 168
PRK13561 276 LKEAQreiLLLTLVEKLKSVLSPRMVLAQISGYDFAIIAnGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAM 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 169 AEPHHSIEDILQEADLAMEDSKNEGRNKLKVFDPATLHAQllQRQIVGE--LREAIRADQLVLYYQPIVELSTGRIEGCE 246
PRK13561 356 FYGDLTAEQLYSRAVSAAFTARRKGKNQIQFFDPQQMEAA--QKRLTEEsdILNALENHQFAIWLQPQVEMRSGKLVSAE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 247 ALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDHPVTaqqdFSMRINASAADLQSLEFVDAVSAA 326
PRK13561 434 ALLRMQQPDGSWDLPDGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIM----LPLSVNLSALQLMHPNMVADMLEL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 327 LAEEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGYSSMGYLRK---LPVDRVKVDRQFVKDLGKD 403
PRK13561 510 LTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVDGLPED 589
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 404 PSqlgFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPLPEAEFTEQ 463
PRK13561 590 SS---MVAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPLPIEIFEER 646
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
7e-55 |
209.95 |
39.43 |
10,27,671,11,38,685,109,155,794,4,159,807,7,167,814,2,169,818,33,202,853,33,237,886,8,245,897,46,296,943,168 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 28 QELHQARYEQR---RDALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAM 104
PRK09776 672 QDVTESRAMLRqlsYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELAS 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 105 RIRSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALepnidlgnNSIR---------CGASVGLrTA--EPHH 173
PRK09776 752 LMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAI--------NDYRfpwegrvyrVGASAGI-TAidDNNH 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 174 SIEDILQEADLAMEDSKNEGRNKLKVFDP--ATLHAQLLQRQIVGELREAIRADQLVLYYQPIVelSTGRIEGC---EAL 248
PRK09776 823 QASEVMSQADIACYAAKNAGRGRVTVYEPqqAAAHSERRELSLAEQWRSMLEENQLMLQAQEIA--SPRIPEARnlwLIS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 249 VRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRwrdhpVTAQQDFSMRINASAADLQSLEFVDAVSAALA 328
PRK09776 901 LRLWDCEGEIIDEGAFRPAAEDPALMHALDRWVIHELFQQGAR-----AVASKGLSIAIPLSVASLSSATLLPFLLEQLE 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 329 EEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLG 408
PRK09776 976 NSPLPPRLLHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEM 1055
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 119962652 409 FLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPLPEAEFTEQL 464
PRK09776 1056 LVSIINGIAQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRPQPLDLLLNSS 1111
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
2e-52 |
201.47 |
61.54 |
9,12,271,44,57,315,77,134,393,32,166,426,39,205,468,8,216,476,82,302,558,79,381,640,37,421,677,42 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 13 DSRIEKLERHVQALMQELHQARYEQRRDALTDALTGLGNRQALVnSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGH 92
PRK11829 272 DDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFI-SLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 93 AASDQILVTVAMRIRSAVRENDVVTRLGGDEFAVLLPATPQN-RATAVGNRILAALEPNIDLGNNSIRCGASVGL-RTAE 170
PRK11829 351 AQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSfPAMQLARRIMSQVTQPLFFDEITLRPSASIGItRYQA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 171 PHHSIEDILQEADLAMEDSKNEGRNKLKVFDPATL---HAQLLQRQivgELREAIRADQLVLYYQPIVELSTGRIEGCEA 247
PRK11829 431 QQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIektHKRLTQEN---DLLQAIENHDFTLFLQPQWDMKRQQVIGAEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 248 LVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDHPVTaqqdFSMRINASAADLQSLEFVDAVSAAL 327
PRK11829 508 LLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVS----LPLSVNISGLQVQNKQFLPHLKTLI 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 328 AEEHLAPDSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGYSSMGY---LRKLPVDRVKVDRQFVKDLGKDP 404
PRK11829 584 SHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYlnhLKSLPIHMIKLDKSFVKNLPEDD 663
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 119962652 405 SQLGFLAAIQHVIHscgLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPLPEAEFTEQ 463
PRK11829 664 AIARIISCVSDVLK---VRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEAQ 719
|
|
|
|
|
|
|
-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-50 |
195.18 |
47.52 |
3,215,270,77,296,347,56,353,403,116 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 216 GELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWrdh 295
COG4943 271 RRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDL--- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 296 pVTAQQDFSMRINASAADLQSLEFVDAVSAALAEEHLAPDSLVLELTESAIIQNNELdRYTLASLHRLGVGLEIDDFGAG 375
COG4943 348 -LRQHRDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFADPKKM-TPIILRLREAGHEIYIDDFGTG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 376 YSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGRPL 455
COG4943 426 YSNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKAL 505
|
250
....*....|....
gi 119962652 456 PEAEFTEQLSRLRT 469
COG4943 506 PAQAFLDWAEQQPA 519
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
9e-38 |
153.29 |
46.33 |
6,216,266,79,295,346,5,304,351,25,331,376,4,335,382,19,355,401,105 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 217 ELREAIRADQLVLYYQPIVELSTGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDH- 295
PRK10551 267 EILTAIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVl 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 296 PVTAQqdfsMRINASAADLQSLEFVDAVSAALAEehLAPD--SLVLELTESAIIQNNELDRyTLASLHRLGVGLEIDDFG 373
PRK10551 347 PVGAK----LGINIAPAHLHSDSFKADVQRLLAS--LPADhfQIVLEITERDMLQEEEALK-LFAWLHSQGIEIAIDDFG 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 374 AGYSSMGYLRKLPVDRVKVDRQFVKDLGKDPSQLGFLAAIQHVIHSCGLEGVWEGIETAEQAEALRSIGCASGQGYYFGR 453
PRK10551 420 TGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISR 499
|
....*..
gi 119962652 454 PLPEAEF 460
PRK10551 500 PLPLDDF 506
|
|
|
|
|
|
|
-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-27 |
118.87 |
46.44 |
4,3,233,21,25,254,125,150,382,23,173,406,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 4 TKPHRLVPADSRIEKLERHVQaLMQELHQARYEQRRDALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGF 83
COG3706 234 TKPIEEGELRARLRRQLRRKR-YERQLRESLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDF 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 84 KALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALEPN---IDLGNNSIRC 160
COG3706 313 KEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELpfvHELSREPLEV 392
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 119962652 161 GASVGLRTAEPHH-SIEDILQEADLAMEDSKNEGRNKLKVFDP 202
COG3706 393 TISIGVAEGKPGEdSIEELLKRADKALYKAKASGRNRVVVKRA 435
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
7e-25 |
110.18 |
62.12 |
4,12,107,22,40,129,19,61,148,89,150,238,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 13 DSRIEKLERHVQALMQELHQARyeqrrdALTDALTGLGNRQALVNSFieAQDAAAKGAVPPALLLVNLDGFKALKNSAGH 92
PRK09894 108 QEGLLSFTAALTDYKIYLLTIR------SNMDVLTGLPGRRVLDESF--DHQLRNREPLNLYLALLDIDRFKLVNDTYGH 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 93 AASDQILVTVAMRIRSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALEPN-IDLGNNSIRCGASVGLRTAEP 171
PRK09894 180 LIGDVVLRTLATYLASWTRPYETVYRYGGEEFIIILKAATDEEACRAGERIRQLIANQaITHSEGRINITATFGVTRAFP 259
|
170 180 190
....*....|....*....|....*....|
gi 119962652 172 HHSIEDILQEADLAMEDSKNEGRNKLKVFD 201
PRK09894 260 EEPLDEVIGRADRAMYEGKQAGRNRVMFID 289
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
2e-24 |
108.85 |
35.01 |
3,40,291,109,149,403,24,173,428,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 41 ALTDALTGLGNRQALVNSFIEAQDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLG 120
PRK09581 292 AVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 121 GDEFAVLLPATPQNRATAVGNRILAALEP---NIDLGNNSIRCGASVGLRTAEPHH-SIEDILQEADLAMEDSKNEGRNK 196
PRK09581 372 GEEFVVVMPDTDIEVAIAVAERIRRKIAEepfAISDGKERLNVTVSIGVAELRPSGeSIEALIKRADKALYEAKNTGRNR 451
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
8e-22 |
100.34 |
67.91 |
19,25,205,12,37,224,20,57,247,7,67,254,45,112,301,36,148,339,7,155,348,8,163,359,5,175,364,33,208,406,9,225,415,11,237,426,57,298,483,6,306,489,23,329,514,5,335,519,69,404,589,3,411,592,15,426,610,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 26 LMQELHQARYEQ-------RRDALTDALTGLGNRQALVN---SFIEAQDaaaKGAVPPALLLVNLDGFKALKNSAGHAAS 95
PRK11059 206 LLEELQDARKERsrfdtfiRSNAFLDAKTGLGNRLFFDNqldTLLEDQE---KVGAHGVVMLIRLPDFDLLQEELGESQV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 96 DQILVTVAMRIRSAVRE--NDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALE--PNIDLGN--NSIRCGAS---VGL 166
PRK11059 283 DELLFELINLLSTFVQRypGALLARYSRSDFAVLLPHRSLKEADSLASQLLKAVDslPPPKMLDrdDFLHIGIAayrSGQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 167 RTaephhsiEDILQEADLAMEDSKNEGRNKLKVFDPATLHAQ---------LLQRQIVGElreairadQLVLYYQPIVEl 237
PRK11059 363 ST-------EQVMEEAEMALRSAQLQGGNSWFMYDKAQDPEKgrgsvrwrtLLEQALVRG--------GPRLYQQPVVT- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 238 STGRIEGCEALVRWNHPVHGLIMPDQFIPIAEATGLIAELGRWVLRTAVRQLRRWRDhpvtAQQDFSmrINASAADLQSL 317
PRK11059 427 RDGQVHHRELMCRIRDGQGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLSYWPE----ESQNLS--INLSVDSLLSR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 318 EFVDAVSAALAE--EHLAPdSLVLELTESAIIQNNELDRYTLASLHRLGVGLEIDDFGAGYSSMGYLRKLPVDRVKVDRQ 395
PRK11059 501 AFQRWLRDTLLQceRSQRK-RLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPS 579
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119962652 396 FVKDLGKDP-SQLgflaAIQHVIHSCGLEGVW---EGIETAEQAEALRSIGCASGQGYYFGRPLPE 457
PRK11059 580 LVRNIHQRTeNQL----FVRSLVGACAGTETQvfaEGVESREEWQTLQILGVSGGQGDFFASPQPL 641
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
2e-15 |
78.78 |
45.82 |
5,32,199,11,43,212,10,53,226,6,63,232,111,174,344,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 33 ARYEQRRDALT--DALTGLGNRQ----ALVNSFieaqDAAAKGAVPPALLLVNLDGFKALKNSAGHAASDQILVTVAMRI 106
PRK10245 200 AEHKRRLQVMStrDGMTGVYNRRhwetMLRNEF----DNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 107 RSAVRENDVVTRLGGDEFAVLLPATPQNRATAVGNRILAALEPNIDLGNNSIRCGASVGLRTAEPHHS-IEDILQEADLA 185
PRK10245 276 QITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMShYREWLKSADLA 355
|
170
....*....|....
gi 119962652 186 MEDSKNEGRNKLKV 199
PRK10245 356 LYKAKKAGRNRTEV 369
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
2e-12 |
68.51 |
47.91 |
10,7,205,4,12,209,12,24,224,7,31,237,7,38,245,23,61,269,9,72,278,65,140,343,10,150,357,5,155,363,37 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 8 RLVPaDSRIEKLERHVQ---ALMQELH------QARYEQR-RDALTDALTGLGNRQALVNSFIE-AQDAAAKGAvpPALL 76
PRK09966 206 RRVS-EERIAEFHRFALdfnSLLDEMEewqlrlQAKNAQLlRTALHDPLTGLANRAAFRSGINTlMNNSDARKT--SALL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 77 LVNLDGFKALKNSAGHAASDQILVTVAMRIRSAVRENDVVTRLGGDEFAVLLPATPQNRATavgNRILAALEPN----ID 152
PRK09966 283 FLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEV---QQICSALTQIfnlpFD 359
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 119962652 153 LGN-NSIRCGASVGLRTAEPHHSIEDILQEADLAMEDSKNE 192
PRK09966 360 LHNgHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
|
|
|
|
|
|
-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 |
9e-04 |
40.26 |
28.26 |
7,329,78,25,356,103,23,380,126,6,386,133,7,393,149,8,403,157,8,426,165,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119962652 330 EHLAPDSLVLELTESAIIQNNELDRytLASLHRLGVGLEIDDFGAGYSSMgYLRKLP-VDRVKVD---------RQFVKD 399
COG3434 79 ELLPPDKVVIEILEDCPPTEKLLSA--IKELKQKGYLLALDDFIFSNVSE-WKPLLPlSDIVKIDfkrvtfdkaRLFDRD 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 119962652 400 LGkdPSQLGFLAaiqhvihscglegvwEGIETAEQAEALRSIGCASGQGYYFGRP 454
COG3434 156 LG--YINKKFLA---------------EKVETEEEFEQAKKAGFDLFQGYFFSKP 193
|
|
|
|
|
|
|
-1 |
|