| 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 |
3e-52 |
200.06 |
100.00 |
4,2,0,11,14,11,66,80,81,105,187,186,54 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 3 RELAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAW-- 80
cd01948 1 ADLRRALERGE-FELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWqa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 81 --PQLRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSN 158
cd01948 80 ggPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 159 LSRLRAPWVRGVKLDRSLTSDLPEPSGefSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLT 238
cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPE--DRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 15807665 239 AEQ 241
cd01948 238 AEE 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 |
| 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-53 |
204.02 |
98.83 |
4,0,3,13,14,16,68,82,87,103,187,190,66 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 1 MARELAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAW 80
COG2200 4 LERDLRQALENGE-FSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRTW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 81 PQ---LRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYS 157
COG2200 83 PRagpLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFGTGYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 158 NLSRLRAPWVRGVKLDRSLTSDLPEPSGefSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPL 237
COG2200 163 SLSYLKRLPPDILKIDRSFVRDLETDAR--DQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSRPL 240
|
250
....*....|....*.
gi 15807665 238 TAEQLSGLLAAQEQFA 253
COG2200 241 PADALDALLSSSQSRV 256
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
6e-48 |
185.88 |
99.59 |
5,2,1,11,14,12,66,80,82,100,181,182,5,187,187,54 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 3 RELAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAW-- 80
smart00052 2 RELRQALENGQ-FLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 81 --PQLRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSN 158
smart00052 81 qgPPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 159 LSRLRAPWVRGVKLDRSLTSDLpEPSGEfSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLT 238
smart00052 161 LSYLKRLPVDLLKIDKSFVRDL-QTDPE-DEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 238
|
...
gi 15807665 239 AEQ 241
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 |
| 109613 |
pfam00563 |
EAL |
EAL domain |
EAL domain |
false |
false |
false |
236 |
1e-41 |
164.90 |
100.00 |
5,1,0,12,14,12,66,80,85,28,110,113,74,187,187,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 2 ARELAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAW- 80
pfam00563 1 EQALREALENGE-FSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 81 ------PQLRLSVNVSAVQLSRPEFAAQLFGVLDstGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGA 154
pfam00563 80 gnallpPDLPLSVNLSPASLLDPSFLEALLALKQ--GGLPPSRLVLEITESDLDEDLRLLEALARLRSLGFRLALDDFGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 155 GYSNLSRLRAPWVRGVKLDRSLTSDLPEPSgefSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALS 234
pfam00563 158 GYSSLSYLSRLPPDYIKIDRSFIKDLSDPE---SRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFS 234
|
..
gi 15807665 235 YP 236
pfam00563 235 KP 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 |
| 34606 |
COG5001 |
COG5001 |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms] |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF... |
false |
true |
false |
663 |
5e-40 |
159.42 |
34.39 |
3,12,413,70,82,484,103,187,587,54 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 13 QGFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAWPQ-LRLSVNVSA 91
COG5001 414 QELSVHFQPIVDIVSGKTIALEALARWHSPEIGPVPPDVFIGIAERSGQIVELTRLLLAKALREARAWPMdVRVSINLSA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 92 VQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSNLSRLRAPWVRGVK 171
COG5001 494 RDLASMENVRRLLAIVSESCIAPHRLDFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIK 573
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 172 LDRSLTSDLPEPSGefSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLTAEQ 241
COG5001 574 IDRSFVSDLEENPT--SEDIVRTVLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMPAEE 641
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
4e-32 |
133.04 |
30.54 |
4,4,547,9,14,556,70,84,631,101,187,732,59 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 5 LAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAWPQLR 84
PRK11359 548 LKEAISNNQ-LKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQN 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 85 -----LSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSNL 159
PRK11359 627 ihipaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGL 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 160 SRLRAPWVRGVKLDRSLTSDLPEPSGefSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLTA 239
PRK11359 707 SRLVSLPVTEIKIDKSFVDRCLTEKR--ILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPA 784
|
....*..
gi 15807665 240 EQLSGLL 246
PRK11359 785 EEIPGWM 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 |
6e-30 |
125.84 |
47.14 |
5,2,270,11,14,281,66,80,351,55,136,406,49,187,455,62 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 3 RELAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAW-- 80
COG4943 271 RRLQRAIERRE-LCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDLlr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 81 --PQLRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLnIEQLYRRGIGITIDDFGAGYSN 158
COG4943 350 qhRDLHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFADPKKMTPI-ILRLREAGHEIYIDDFGTGYSN 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 159 LSRLRAPWVRGVKLDRSLTSDLPEPSGefSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLT 238
COG4943 429 LHYLQSLPVDALKIDKSFVDTLGTDSA--SHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKALP 506
|
250
....*....|.
gi 15807665 239 AEQLSGLLAAQ 249
COG4943 507 AQAFLDWAEQQ 517
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
1e-28 |
121.37 |
37.71 |
7,4,412,9,14,421,11,26,432,55,81,491,81,162,573,3,166,576,18,186,594,68 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 5 LAQAFYDGQgFSLAYQPIYDLaSGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAWP--- 81
PRK10060 413 LRKALENDQ-LVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVILDVVRQAAKWRdkg 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 82 -QLRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSNLS 160
PRK10060 491 iNLRVAVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLS 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 161 RL-RAPwVRGVKLDRSLTSDLPEPSgeFSRQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLTA 239
PRK10060 571 QLaRFP-IDAIKLDQSFVRDIHKQP--VSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPA 647
|
250
....*....|....*
gi 15807665 240 EQLSGLLAAQEQFAL 254
PRK10060 648 VAFERWYKRYQKLRL 662
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
5e-23 |
103.31 |
36.10 |
4,10,409,72,82,485,80,162,568,22,189,590,54 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 11 DGQGFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAWPQ----LRLS 86
PRK13561 410 ENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPDGLIDRIESCGLMVTVGHWVLEESCRLLAAWQErgimLPLS 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 87 VNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSNLSRL---R 163
PRK13561 490 VNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLqhmK 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 164 APWVRGVKLDRSLTSDLPEPSgefsrQLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPLTAEQLS 243
PRK13561 570 SLPIDVLKIDKMFVDGLPEDS-----SMVAAIIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPLPIEIFE 644
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
8e-19 |
88.99 |
32.28 |
5,3,476,6,10,482,71,81,557,77,158,637,27,190,664,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 4 ELAQAFyDGQGFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAWP-- 81
PRK11829 477 DLLQAI-ENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKar 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 82 --QLRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSN- 158
PRK11829 556 gvSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSl 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 159 --LSRLRAPWVRGVKLDRSLTSDLPEPSGefsrqLTRNAVNLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYP 236
PRK11829 636 ryLNHLKSLPIHMIKLDKSFVKNLPEDDA-----IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 710
|
.
gi 15807665 237 L 237
PRK11829 711 L 711
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
6e-17 |
82.79 |
46.53 |
7,2,265,11,14,276,57,71,337,11,82,349,53,136,402,46,185,448,11,196,460,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 3 RELAQAFYDGQgFSLAYQPIYDLASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLD----EACRAAQ 78
PRK10551 266 REILTAIKREQ-FYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFEliarDAAELQK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 79 AWPQ-LRLSVNVSAVQLSRPEFAAQLFGVLDSTGMTTQRLELELTETALLHENEQVQLnIEQLYRRGIGITIDDFGAGYS 157
PRK10551 345 VLPVgAKLGINIAPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMLQEEEALKL-FAWLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 158 NLSRLRAPWVRGVKLDRSLTSDLPEpsgEFSRQLTRNAV-NLAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYP 236
PRK10551 424 ALIYLERFTLDYLKIDRGFINAIGT---ETVTSPVLDAVlTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISRP 500
|
....*.
gi 15807665 237 LTAEQL 242
PRK10551 501 LPLDDF 506
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
6e-05 |
43.16 |
19.18 |
5,35,899,40,75,942,98,184,1040,13,197,1062,39,239,1101,12 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 36 LLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACR---AAQAWPQLRLSVNVSAVQLSRPEFAAQLFGVLDSTGM 112
PRK09776 900 SLRLWDCEGEIIDEGAFRPAAEDPALMHALDRWVIHELFQqgaRAVASKGLSIAIPLSVASLSSATLLPFLLEQLENSPL 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 113 TTQRLELELTETALLHENEQVQLNIEQLYRRGIGITIDDFGAGYSNLSRLRAPWVRGVKLDrsltsdlpepsGEFSRQLT 192
PRK09776 980 PPRLLHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKID-----------GELCANLQ 1048
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15807665 193 RNAVN---------LAQYQHTVITAEGLESAAHVEAARQLGCPLGQGYALSYPltaEQLSGLLAAQEQ 251
PRK09776 1049 GNLMDemlvsiingIAQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGYVIGRP---QPLDLLLNSSYF 1113
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
6e-04 |
39.48 |
14.80 |
3,13,415,11,25,426,56,81,484,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807665 14 GFSLAYQPIYDlASGVPVKVEALLRWRHPQLGQISPAEFIPIAQRTGQIAQIGLXVLDEACRAAQAWP--QLRLSVNVSA 91
PRK11059 416 GPRLYQQPVVT-RDGQVHHRELMCRIRDGQGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLSYWPeeSQNLSINLSV 494
|
90
....*....|....*.
gi 15807665 92 VQLSRPEFAAQLFGVL 107
PRK11059 495 DSLLSRAFQRWLRDTL 510
|
|
|
|
|
|
|
-1 |
|