|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
248-408 |
2.43e-57 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation 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. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 185.53 E-value: 2.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 248 SQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYG 327
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 328 GEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSKYVTISLGFTVYTGGlkmGQD--RLIHAADQALYRAKQLG 405
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPND---GEDpeDLLKRADTALYQAKQAG 157
|
...
gi 445935519 406 RNQ 408
Cdd:pfam00990 158 RNR 160
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
136-409 |
3.34e-57 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 189.03 E-value: 3.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 136 LLLSVGNMALKNQSMLLLSFLYMLGFILSGIKPLHMLCVGLLAAFLVFAFLILLDVNCDYIALGRALFGSCILGFSISSM 215
Cdd:COG2199 4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 216 LISRERSLFLNNQLAEINEQILRIEasELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYND 295
Cdd:COG2199 84 LLLLLALLLLLLALEDITELRRLEE--RLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 296 FYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkyVTISLG 375
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELR--VTVSIG 239
|
250 260 270
....*....|....*....|....*....|....
gi 445935519 376 FTVYTGGlKMGQDRLIHAADQALYRAKQLGRNQI 409
Cdd:COG2199 240 VALYPED-GDSAEELLRRADLALYRAKRAGRNRV 272
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
249-409 |
1.56e-55 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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 adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 180.83 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 249 QQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGG 328
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 329 EEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLvskYVTISLGFTVYTGGlKMGQDRLIHAADQALYRAKQLGRNQ 408
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI---RVTASIGIATYPED-GEDAEELLRRADEALYRAKRSGRNR 156
|
.
gi 445935519 409 I 409
Cdd:cd01949 157 V 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
247-411 |
2.89e-53 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 175.22 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 247 LSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARY 326
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 327 GGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkYVTISLGFTVYTG-GLKMGQdrLIHAADQALYRAKQLG 405
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETL-TVTVSIGVACYPGhGLTLEE--LLKRADEALYQAKKAG 157
|
....*.
gi 445935519 406 RNQIYY 411
Cdd:TIGR00254 158 RNRVVV 163
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
246-409 |
4.51e-48 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 161.65 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 246 HLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVAR 325
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 326 YGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLvskYVTISLGFTVYTGGlKMGQDRLIHAADQALYRAKQLG 405
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL---YLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAG 156
|
....
gi 445935519 406 RNQI 409
Cdd:smart00267 157 RNQV 160
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
229-410 |
3.19e-43 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 156.98 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 229 LAEINEQI--------LRIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQ 300
Cdd:PRK09581 265 LARVRTQIrrkryqdaLRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 301 MGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQ--AIPHAASLVSkyVTISLGFTV 378
Cdd:PRK09581 345 AGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLN--VTVSIGVAE 422
|
170 180 190
....*....|....*....|....*....|..
gi 445935519 379 YTGGLKMGQDrLIHAADQALYRAKQLGRNQIY 410
Cdd:PRK09581 423 LRPSGDTIEA-LIKRADKALYEAKNTGRNRVV 453
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
56-413 |
2.27e-39 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 149.54 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 56 FLASGVLTYLIFILLALPTDYLVIGVPYITLDFIHCLLSAMNIALALLLFWVFAKFTKLSEHFYLAACGIVFLTIIINAM 135
Cdd:COG5001 56 LLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 136 LLLSVGNMALKNQSMLLLSFLYMLGFILSGIKPLHMLCVGLLAAFLVFAFLILLDVNCDYIALGRALFGSCILGFSISSM 215
Cdd:COG5001 136 LLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 216 LISRERSLFLNNQLAEINEQI---LRIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKN 292
Cdd:COG5001 216 LLLLGLLLLLLLVAVLAIARLiteRKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 293 YNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETP-AQGAYSVAANIYKAIeRQAIPHAASLVskYVT 371
Cdd:COG5001 296 INDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAAL-AEPFELDGHEL--YVS 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 445935519 372 ISLGFTVYTGGlkmGQDR--LIHAADQALYRAKQLGRNQI-YYQP 413
Cdd:COG5001 373 ASIGIALYPDD---GADAeeLLRNADLAMYRAKAAGRNRYrFFDP 414
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
214-409 |
2.38e-38 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 138.96 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 214 SMLISRERSLFLN--NQLAEInEQILRI---------EASELLH-LSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLA 281
Cdd:NF038266 49 SAARERELSLAERydRQLRRL-EKIVRIsdryqrmmrDLNEALReASTRDPLTGLPNRRLLMERLREEVERARRSGRPFT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 282 VLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPH 361
Cdd:NF038266 128 LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRV 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445935519 362 AASLVSkyVTISLGFTVYtgglKMGQDRLIHA---ADQALYRAKQLGRNQI 409
Cdd:NF038266 208 GDDVLS--VTASAGLAEH----RPPEEGLSATlsrADQALYQAKRAGRDRV 252
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
220-409 |
7.99e-36 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 134.49 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 220 ERSLFLN-NQLAEIneqilRIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYG 298
Cdd:NF041606 154 EKEIIMNiASLAAI-----AINNALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 299 HQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkyVTISLGFTV 378
Cdd:NF041606 229 HACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIR--VTISIGVAE 306
|
170 180 190
....*....|....*....|....*....|.
gi 445935519 379 YTGGLKMGQDrLIHAADQALYRAKQLGRNQI 409
Cdd:NF041606 307 YNFDVESAKS-LVERADKALYESKQNGRNRV 336
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
248-408 |
2.43e-57 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation 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. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 185.53 E-value: 2.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 248 SQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYG 327
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 328 GEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSKYVTISLGFTVYTGGlkmGQD--RLIHAADQALYRAKQLG 405
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPND---GEDpeDLLKRADTALYQAKQAG 157
|
...
gi 445935519 406 RNQ 408
Cdd:pfam00990 158 RNR 160
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
136-409 |
3.34e-57 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 189.03 E-value: 3.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 136 LLLSVGNMALKNQSMLLLSFLYMLGFILSGIKPLHMLCVGLLAAFLVFAFLILLDVNCDYIALGRALFGSCILGFSISSM 215
Cdd:COG2199 4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 216 LISRERSLFLNNQLAEINEQILRIEasELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYND 295
Cdd:COG2199 84 LLLLLALLLLLLALEDITELRRLEE--RLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 296 FYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkyVTISLG 375
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELR--VTVSIG 239
|
250 260 270
....*....|....*....|....*....|....
gi 445935519 376 FTVYTGGlKMGQDRLIHAADQALYRAKQLGRNQI 409
Cdd:COG2199 240 VALYPED-GDSAEELLRRADLALYRAKRAGRNRV 272
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
249-409 |
1.56e-55 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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 adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 180.83 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 249 QQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGG 328
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 329 EEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLvskYVTISLGFTVYTGGlKMGQDRLIHAADQALYRAKQLGRNQ 408
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI---RVTASIGIATYPED-GEDAEELLRRADEALYRAKRSGRNR 156
|
.
gi 445935519 409 I 409
Cdd:cd01949 157 V 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
247-411 |
2.89e-53 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 175.22 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 247 LSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARY 326
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 327 GGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkYVTISLGFTVYTG-GLKMGQdrLIHAADQALYRAKQLG 405
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETL-TVTVSIGVACYPGhGLTLEE--LLKRADEALYQAKKAG 157
|
....*.
gi 445935519 406 RNQIYY 411
Cdd:TIGR00254 158 RNRVVV 163
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
246-409 |
4.51e-48 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 161.65 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 246 HLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVAR 325
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 326 YGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLvskYVTISLGFTVYTGGlKMGQDRLIHAADQALYRAKQLG 405
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL---YLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAG 156
|
....
gi 445935519 406 RNQI 409
Cdd:smart00267 157 RNQV 160
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
229-410 |
3.19e-43 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 156.98 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 229 LAEINEQI--------LRIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQ 300
Cdd:PRK09581 265 LARVRTQIrrkryqdaLRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 301 MGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQ--AIPHAASLVSkyVTISLGFTV 378
Cdd:PRK09581 345 AGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLN--VTVSIGVAE 422
|
170 180 190
....*....|....*....|....*....|..
gi 445935519 379 YTGGLKMGQDrLIHAADQALYRAKQLGRNQIY 410
Cdd:PRK09581 423 LRPSGDTIEA-LIKRADKALYEAKNTGRNRVV 453
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
250-409 |
1.08e-39 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 149.39 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 250 QDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGE 329
Cdd:PRK15426 400 HDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 330 EFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASlVSKYVTISLGFTVYTGGLKMGQDRLIHAADQALYRAKQLGRNQI 409
Cdd:PRK15426 480 EFCVVLPGASLAEAAQVAERIRLRINEKEILVAKS-TTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRV 558
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
56-413 |
2.27e-39 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 149.54 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 56 FLASGVLTYLIFILLALPTDYLVIGVPYITLDFIHCLLSAMNIALALLLFWVFAKFTKLSEHFYLAACGIVFLTIIINAM 135
Cdd:COG5001 56 LLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 136 LLLSVGNMALKNQSMLLLSFLYMLGFILSGIKPLHMLCVGLLAAFLVFAFLILLDVNCDYIALGRALFGSCILGFSISSM 215
Cdd:COG5001 136 LLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 216 LISRERSLFLNNQLAEINEQI---LRIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKN 292
Cdd:COG5001 216 LLLLGLLLLLLLVAVLAIARLiteRKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 293 YNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETP-AQGAYSVAANIYKAIeRQAIPHAASLVskYVT 371
Cdd:COG5001 296 INDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAAL-AEPFELDGHEL--YVS 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 445935519 372 ISLGFTVYTGGlkmGQDR--LIHAADQALYRAKQLGRNQI-YYQP 413
Cdd:COG5001 373 ASIGIALYPDD---GADAeeLLRNADLAMYRAKAAGRNRYrFFDP 414
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
214-409 |
2.38e-38 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 138.96 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 214 SMLISRERSLFLN--NQLAEInEQILRI---------EASELLH-LSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLA 281
Cdd:NF038266 49 SAARERELSLAERydRQLRRL-EKIVRIsdryqrmmrDLNEALReASTRDPLTGLPNRRLLMERLREEVERARRSGRPFT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 282 VLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPH 361
Cdd:NF038266 128 LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRV 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445935519 362 AASLVSkyVTISLGFTVYtgglKMGQDRLIHA---ADQALYRAKQLGRNQI 409
Cdd:NF038266 208 GDDVLS--VTASAGLAEH----RPPEEGLSATlsrADQALYQAKRAGRDRV 252
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
235-407 |
1.86e-36 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 135.19 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 235 QILRIEASELLHLSQQDALTQISNRRTFDEMFDffYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIK 314
Cdd:PRK09894 116 ALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFD--HQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 315 NSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkyVTISLGFTVYTGGLKMgqDRLIHAA 394
Cdd:PRK09894 194 SWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRIN--ITATFGVSRAFPEETL--DVVIGRA 269
|
170
....*....|...
gi 445935519 395 DQALYRAKQLGRN 407
Cdd:PRK09894 270 DRAMYEGKQTGRN 282
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
220-409 |
7.99e-36 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 134.49 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 220 ERSLFLN-NQLAEIneqilRIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYG 298
Cdd:NF041606 154 EKEIIMNiASLAAI-----AINNALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 299 HQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkyVTISLGFTV 378
Cdd:NF041606 229 HACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIR--VTISIGVAE 306
|
170 180 190
....*....|....*....|....*....|.
gi 445935519 379 YTGGLKMGQDrLIHAADQALYRAKQLGRNQI 409
Cdd:NF041606 307 YNFDVESAKS-LVERADKALYESKQNGRNRV 336
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
247-408 |
4.83e-22 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 96.82 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 247 LSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARY 326
Cdd:PRK10245 204 MSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRF 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 327 GGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVskyVTISLGFTVYTGglKMGQDR-LIHAADQALYRAKQLG 405
Cdd:PRK10245 284 GGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVT---LRISVGVAPLNP--QMSHYReWLKSADLALYKAKNAG 358
|
...
gi 445935519 406 RNQ 408
Cdd:PRK10245 359 RNR 361
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
232-408 |
9.47e-20 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 91.67 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 232 INEQIL----------RIEASELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKrpLAVLFIDIDFFKNYNDFYGHQM 301
Cdd:PRK10060 211 KNEIFLicsgtditeeRRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMF 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 302 GDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIykaIERQAIPHAASLVSKYVTISLGFTVYTg 381
Cdd:PRK10060 289 GDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRI---LTRLRLPFRIGLIEVYTGCSIGIALAP- 364
|
170 180
....*....|....*....|....*....
gi 445935519 382 glKMGQDR--LIHAADQALYRAKQLGRNQ 408
Cdd:PRK10060 365 --EHGDDSesLIRSADTAMYTAKEGGRGQ 391
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
243-415 |
3.36e-16 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 80.87 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 243 ELLHLSQQDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDF 322
Cdd:PRK09776 660 QLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 323 VARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHAASLVSkyVTISLGFTVYTGGLKMGQDrLIHAADQALYRAK 402
Cdd:PRK09776 740 LARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYR--VGASAGITLIDANNHQASE-VMSQADIACYAAK 816
|
170
....*....|....
gi 445935519 403 QLGRNQIY-YQPLQ 415
Cdd:PRK09776 817 NAGRGRVTvYEPQQ 830
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
317-402 |
1.54e-14 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 71.48 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 317 IRHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERqaiphaasLVSKYVTISLGFTvytgglkmgQDRLIHAADq 396
Cdd:COG3706 112 LARVDLVARYGGEEFAILLPGTDLEGALAVAERIREAVAE--------LPSLRVTVSIGVA---------GDSLLKRAD- 173
|
....*.
gi 445935519 397 ALYRAK 402
Cdd:COG3706 174 ALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
279-402 |
6.52e-14 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 68.15 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 279 PLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSI-RHVDFVARYGGEEFVVLLPETPAQGAYSVAANIYKAIERQ 357
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 445935519 358 AIP-----------HAASLVSKYVTISLGFTVYtgglkmgqDRLIHAADQALYRAK 402
Cdd:cd07556 81 NQSegnpvrvrigiHTGPVVVGVIGSRPQYDVW--------GALVNLASRMESQAK 128
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
225-403 |
5.62e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 66.95 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 225 LNNQLAEINEQILRIEA--SELLHLSQQDALTQISNRRTFDEMFDFFYyRANQEKRPLAVLFIDIDFFKNYNDFYGHQMG 302
Cdd:PRK09966 223 FNSLLDEMEEWQLRLQAknAQLLRTALHDPLTGLANRAAFRSGINTLM-NNSDARKTSALLFLDGDNFKYINDTWGHATG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 303 DKVISSIAAAIKN--SIRHVDFvaRYGGEEFVVLLPETpaQGAYSV---AANIYKAIERQAIPHAASLVSkyVTISLGFT 377
Cdd:PRK09966 302 DRVLIEIAKRLAEfgGLRHKAY--RLGGDEFAMVLYDV--QSESEVqqiCSALTQIFNLPFDLHNGHQTT--MTLSIGYA 375
|
170 180
....*....|....*....|....*.
gi 445935519 378 VYTGglKMGQDRLIHAADQALYRAKQ 403
Cdd:PRK09966 376 MTIE--HASAEKLQELADHNMYQAKH 399
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
219-413 |
1.62e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 63.25 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 219 RERSLFLNnQLAEINEQI--LRIEASE----LLHLSQQDALTQISNR----RTFDEMFDffyyranqEKRPLAVLFIDID 288
Cdd:PRK11359 342 AETSAFIE-RVADISQHLaaLALEQEKsrqhIEQLIQFDPLTGLPNRnnlhNYLDDLVD--------KAVSPVVYLIGVD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 289 FFKNYNDFYGHQMGDKVISSIAAAIKNSIRHVDFVARYGGEEFVVLLPETPAQGAYSVAAniykaiERQAIPHAASLVSK 368
Cdd:PRK11359 413 HFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIAD------ELRNVVSKPIMIDD 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445935519 369 YV---TISLGFTvYTGGlKMGQDRLIHAADQALYRAKQLGRNQIYYQP 413
Cdd:PRK11359 487 KPfplTLSIGIS-YDVG-KNRDYLLSTAHNAMDYIRKNGGNGWQFFSP 532
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
250-420 |
9.75e-06 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 47.93 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 250 QDALTQISNRRTFDEMFDFFYYRANQEKRPLAVLFIDIDFFKNYNDFYGHQMGDKVISSIAAAIKNSI-RHVDFV-ARYG 327
Cdd:PRK11059 230 QDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPGALlARYS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445935519 328 GEEFVVLLPETPAQGAYSVAANIYKAIERQAIPHaasLVSKYVTISLGFTVYTGGLKMGQdrLIHAADQALyRAKQL--G 405
Cdd:PRK11059 310 RSDFAVLLPHRSLKEADSLASQLLKAVDALPPPK---MLDRDDFLHIGICAYRSGQSTEQ--VMEEAEMAL-RSAQLqgG 383
|
170
....*....|....*
gi 445935519 406 RNQIYYQPLQVAEIA 420
Cdd:PRK11059 384 NGWFVYDKAQLPEKG 398
|
|
| |
