| 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-42 |
169.31 |
100.00 |
4,400,0,20,420,24,87,508,111,18,526,130,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 401 RDALTGLANRRALDMALEAL----AKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECREDDVVARFGGD 476
cd01949 1 TDPLTGLPNRRAFEERLERLlaraRRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927307 477 EFVLVLHGAPRKTGIRVGERIRSAVKAFSWEkIAPDLRVSVSIGVAEFQP-GMDLSEALLTADSALYAAKQQGRDRVA 553
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFFI-DGEEIRVTASIGIAEYPEdGEDLEELLRRADKALYQAKRSGRNRVV 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... |
0 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
2e-37 |
152.40 |
100.00 |
4,396,0,16,412,20,89,502,109,23,525,133,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 397 HEALRDALTGLANRRA----LDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECREDDVVAR 472
smart00267 1 RLAFRDPLTGLPNRRYfeeeLEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 473 FGGDEFVLVLHGAPRKTGIRVGERIRSAVkAFSWEKIAPDLRVSVSIGVAEFQ-PGMDLSEALLTADSALYAAKQQGRDR 551
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 117927307 552 VAAA 555
smart00267 160 VAVY 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 |
1e-35 |
146.62 |
100.00 |
4,398,0,14,412,18,90,502,110,22,524,133,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 399 ALRDALTGLANRRA----LDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECREDDVVARFG 474
pfam00990 1 AAHDPLTGLPNRRYfeeeLEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 475 GDEFVLVLHGAPRKTGIRVGERIRSAVK--AFSWEKIAPDLRVSVSIGVAEF-QPGMDLSEALLTADSALYAAKQQGRDR 551
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 |
| 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 |
1e-35 |
146.42 |
100.00 |
4,379,0,33,412,37,96,509,133,26,535,161,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 380 MVRMQMLELAAENERVEHEALRDALTGLANRRA----LDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRS 455
COG2199 1 ALLRLLTRLRKAEERLERLALHDPLTGLPNRRAfeerLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 456 IAAILRGECREDDVVARFGGDEFVLVLHGAPRKTGIRVGERIRSAVKAFSWEKiAPDLRVSVSIGVAEFQPGMDLSEALL 535
COG2199 81 VARRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFFLG-GEELRVTVSIGVALYPEDGSDDAELL 159
|
170 180
....*....|....*....|..
gi 117927307 536 --TADSALYAAKQQGRDRVAAA 555
COG2199 160 lrRADLALYRAKRAGRNRVVVF 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 |
1e-35 |
146.33 |
98.79 |
5,398,1,20,418,24,9,427,34,80,507,115,29,536,145,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 399 ALRDALTGLANRRALDMALE---ALAKSDTVS-SLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECREDDVVARFG 474
TIGR00254 2 AVRDPLTGLYNRRYLEEMLDselKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 475 GDEFVLVLHGAPRKTGIRVGERIRSAVKAFSWE-KIAPDLRVSVSIGVAEFQPGMDLSEALLT-ADSALYAAKQQGRDRV 552
TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGLTLEELLKrADEALYQAKKAGRNRV 161
|
...
gi 117927307 553 AAA 555
TIGR00254 162 VVA 164
|
|
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 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
1e-37 |
153.15 |
35.89 |
4,398,291,29,427,324,74,501,400,35,536,436,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 399 ALRDALTGLANRRALDMALEALAKSDTVS----SLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECREDDVVARFG 474
PRK09581 292 AVTDGLTGLHNRRYFDMHLKQLIERANERgkplSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 475 GDEFVLVLHGAPRKTGIRVGERIRSAV--KAFSWEKIAPDLRVSVSIGVAEFQPGMDLSEALLT-ADSALYAAKQQGRDR 551
PRK09581 372 GEEFVVVMPDTDIEVAIAVAERIRRKIaeEPFAISDGKERLNVTVSIGVAELRPSGESIEALIKrADKALYEAKNTGRNR 451
|
....
gi 117927307 552 VAAA 555
PRK09581 452 VVAL 455
|
|
|
|
|
|
|
-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 |
8e-36 |
146.99 |
39.54 |
4,387,258,40,427,302,75,502,379,34,536,414,16 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 388 LAAENERVEHEALRDALTGLANRRALDMALEALAKSDTVS----SLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGE 463
COG3706 259 LRESLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREgrplSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQT 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 464 CREDDVVARFGGDEFVLVLHGAPRKTGIRVGERIRSAVK--AFSWEKIAPDLRVSVSIGVAEFQPGMDLSEALLT-ADSA 540
COG3706 339 VRGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINelPFVHELSREPLEVTISIGVAEGKPGEDSIEELLKrADKA 418
|
170
....*....|..
gi 117927307 541 LYAAKQQGRDRV 552
COG3706 419 LYKAKASGRNRV 430
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
3e-28 |
121.74 |
59.73 |
3,385,111,15,400,131,19,419,152,134 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 386 LELAAENERVEHEAL-----RDALTGLANRRALDMALEA--LAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAA 458
PRK09894 112 LSFTAALTDYKIYLLtirsnMDVLTGLPGRRVLDESFDHqlRNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLAT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 459 ILRGECREDDVVARFGGDEFVLVLHGAPRKTGIRVGERIRSAVKAFSWEKIAPDLRVSVSIGVAEFQPGMDLSEALLTAD 538
PRK09894 192 YLASWTRPYETVYRYGGEEFIIILKAATDEEACRAGERIRQLIANQAITHSEGRINITATFGVTRAFPEEPLDEVIGRAD 271
|
170
....*....|....*
gi 117927307 539 SALYAAKQQGRDRVA 553
PRK09894 272 RAMYEGKQAGRNRVM 286
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
4e-23 |
104.98 |
46.63 |
4,386,197,31,417,232,89,507,321,22,529,344,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 387 ELAAENERVEHEALRDALTGLANRRALDMAL----EALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRG 462
PRK10245 198 KLAEHKRRLQVMSTRDGMTGVYNRRHWETMLrnefDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 463 ECREDDVVARFGGDEFVLVLHGAPRKTGIRVGERIRSAVKAFSWeKIAPDLRVSVSIGVAEFQPGMD-LSEALLTADSAL 541
PRK10245 278 TLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRL-PNAPQVTLRISVGVAPLNPQMShYREWLKSADLAL 356
|
170
....*....|....
gi 117927307 542 YAAKQQGRDRVAAA 555
PRK10245 357 YKAKKAGRNRTEVA 370
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
1e-22 |
103.25 |
14.43 |
5,396,685,14,410,703,93,503,798,4,509,802,15,524,818,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 397 HEALRDALTGLANR----RALDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECREDDVVAR 472
PRK09776 686 YSASHDALTGLANRasfeKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLAR 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 473 FGGDEFVLVLHGAPRKTGIRVGERIRSAVKA--FSWEkiAPDLRVSVSIGVAEF-QPGMDLSEALLTADSALYAAKQQGR 549
PRK09776 766 LGGDEFGLLLPDCNVESARFIATRIISAINDyrFPWE--GRVYRVGASAGITAIdDNNHQASEVMSQADIACYAAKNAGR 843
|
...
gi 117927307 550 DRV 552
PRK09776 844 GRV 846
|
|
|
|
|
|
|
-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-21 |
98.56 |
27.15 |
4,378,203,23,401,230,11,412,245,124,536,370,13 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 379 VMVRMQMLELAAENERVEHEALR----DALTGLANRRA----LDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGD 450
COG5001 204 VQSQVTLTQRAEETRRLSDENDRlanlDSLTGLPNRRRffaeLDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 451 EVLRSIAAILRGECREDDVVARFGGDEFVLVLHGAPRKTGIRVGERIRSAVKAFSWEKIAPDLRVSVSIGVAEFQPGMDL 530
COG5001 284 RLLIEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADT 363
|
170 180
....*....|....*....|
gi 117927307 531 SEALLT-ADSALYAAKQQGR 549
COG5001 364 SEQLFErADYALYHAKQNGK 383
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
1e-19 |
93.25 |
24.74 |
8,392,225,9,401,239,12,413,252,14,427,267,51,478,319,6,484,328,23,512,351,12,524,364,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 393 ERVEHEALR-----DALTGLANRRAL-DMALEALAKSDTVS-SLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECR 465
PRK10060 226 ERRAQERLRilantDSITGLPNRNAIqELIDHAIAQADNNQvGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 466 EDDVVARFGGDEF-VLVLHG---APRKTGIRVGERIRSAVKAFSWEkiapdLRVSVSIGVAEF-QPGMDLSEALLTADSA 540
PRK10060 306 EDQTLARLGGDEFlVLASHTsqaALEAMASRILTRLRLPFRIGLIE-----VYTGCSIGIALSpEHGDDSESLIRSADTA 380
|
....*....
gi 117927307 541 LYAAKQQGR 549
PRK10060 381 MYTAKEGGR 389
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
1e-13 |
73.13 |
41.77 |
7,385,234,41,426,278,65,494,343,7,501,351,6,507,360,15,522,378,10,535,388,16 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 386 LELAAENERVEHEALRDALTGLANRRALDMALEALAKSDTV---SSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRG 462
PRK09966 235 LRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDArktSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 463 ECREDDVVARFGGDEFVLVLHGAPRKTGIrvgERIRSAV-KAFSWE---KIAPDLRVSVSIGVA---EFQPGMDLSEall 535
PRK09966 315 FGGLRHKAYRLGGDEFAMVLYDVQSESEV---QQICSALtQIFNLPfdlHNGHQTTMTLSIGYAmtiEHASAEKLQE--- 388
|
170
....*....|....*.
gi 117927307 536 TADSALYAAKQQGRDR 551
PRK09966 389 LADHNMYQAKHQRAEK 404
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
4e-11 |
65.25 |
20.78 |
5,384,357,9,393,370,110,506,480,6,512,488,10,523,498,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 385 MLELAAENE----RVEHEALRDALTGLANRRALDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAIL 460
PRK11359 358 MAALALEQEksrqHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRF 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 461 RGECREDDVVARFGGDEFVLVLHGAPRKTGIRVGERIRSAVKAfswEKIAPD--LRVSVSIGVAeFQPGMDLSEALLTAD 538
PRK11359 438 REKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK---PIMIDDkpFPLTLSIGIS-YDVGKNRDYLLSTAH 513
|
170
....*....|
gi 117927307 539 SALYAAKQQG 548
PRK11359 514 NAMDYIRKNG 523
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
7e-07 |
50.92 |
25.50 |
4,387,219,101,488,321,15,503,337,7,512,344,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 388 LAAENERVEHEALRDALTGLANRRALDMALEALAKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVLRSIAAILRGECRED 467
PRK13561 220 LQRHYEEQNENAMRFPVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 468 DVVARFGGDEFVLVLHGAPRK-TGIRVGERIRSAVKA-FSWEKIApdLRVSVSIGVAEFQPGMDLSEALLTADSALYAAK 545
PRK13561 300 MVLAQISGYDFAIIANGVKEPwHAITLGQQVLTIINErLPIQRIQ--LRPSCSIGIAMFYGDLTAEQLYSRAVSAAFTAR 377
|
....*...
gi 117927307 546 QQGRDRVA 553
PRK13561 378 RKGKNQIQ 385
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
1e-04 |
43.33 |
23.68 |
8,401,230,19,420,253,33,453,290,8,464,298,6,470,305,12,485,317,19,506,336,10,516,350,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 402 DALTGLANRRALDMALEAL----AKSDTVSSLLFVDLDDFKTTNDSFSHTVGDEVL----RSIAAILRgecREDDVV-AR 472
PRK11059 231 DAKTGLGNRLFFDNQLDTLledqEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLfeliNLLSTFVQ---RYPGALlAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927307 473 FGGDEFVLVLhgaPRKTGIRVGERIRSAVKAFswEKIAPDLRVS----VSIGVAEFQPGMDLSEALLTADSALYAAKQQG 548
PRK11059 308 YSRSDFAVLL---PHRSLKEADSLASQLLKAV--DSLPPPKMLDrddfLHIGIAAYRSGQSTEQVMEEAEMALRSAQLQG 382
|
|
|
|
|
|
|
-1 |
|