| 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 |
7e-39 |
156.59 |
100.00 |
2,249,0,110,362,110,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 250 TDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFGGE 329
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 330 EFVILLAGSDLEQAAVAAERVRQHIAHLTVdtpLHGDPVSVTVSVGVAAFRENGHSVLELLDAADAALYEAKRAGRNCVR 409
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFF---IDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
3e-37 |
151.24 |
100.00 |
1,247,0,160 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 248 ARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFG 327
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 328 GEEFVILLAGSDLEQAAVAAERVRQHIAHLTVDTPLHGDPVSVTVSVGVAAFRENGHSVLELLDAADAALYEAKRAGRNC 407
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 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
8e-36 |
146.62 |
100.00 |
2,245,0,112,360,112,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 246 HAARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGR 325
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 326 FGGEEFVILLAGSDLEQAAVAAERVRQHIAHLtvdTPLHGDPVSVTVSVGVAAFRENGHSVLELLDAADAALYEAKRAGR 405
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREP---IIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGR 157
|
....*.
gi 117928368 406 NCVRVA 411
smart00267 158 NQVAVY 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 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
2e-35 |
145.56 |
99.39 |
2,247,1,115,363,116,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 248 ARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFG 327
TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 328 GEEFVILLAGSDLEQAAVAAERVRQHIAHLTVDTPlHGDPVSVTVSVGVAAFRENGHSVLELLDAADAALYEAKRAGRNC 407
TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVA-GSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 117928368 408 VRVAT 412
TIGR00254 161 VVVAD 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 |
| 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 |
3e-33 |
137.94 |
98.34 |
3,231,3,128,362,131,22,384,154,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 232 VLVFQRTLLIAELRHAARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAG 311
COG2199 4 RLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 312 GLTHGLRPRDFVGRFGGEEFVILLAGSDLEQAAVAAERVRQHIAHLTVdtpLHGDPVSVTVSVGVAAFRENGH-SVLELL 390
COG2199 84 RLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFF---LGGEELRVTVSIGVALYPEDGSdDAELLL 160
|
170 180
....*....|....*....|.
gi 117928368 391 DAADAALYEAKRAGRNCVRVA 411
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 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
2e-32 |
135.43 |
35.23 |
1,247,291,161 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 248 ARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFG 327
PRK09581 292 AVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 328 GEEFVILLAGSDLEQAAVAAERVRQHIAHLTVDTPLHGDPVSVTVSVGVAAFRENGHSVLELLDAADAALYEAKRAGRNC 407
PRK09581 372 GEEFVVVMPDTDIEVAIAVAERIRRKIAEEPFAISDGKERLNVTVSIGVAELRPSGESIEALIKRADKALYEAKNTGRNR 451
|
.
gi 117928368 408 V 408
PRK09581 452 V 452
|
|
|
|
|
|
|
-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 |
9e-31 |
129.65 |
40.23 |
1,235,257,175 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 236 QRTLLIAELRHAARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTH 315
COG3706 258 QLRESLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 316 GLRPRDFVGRFGGEEFVILLAGSDLEQAAVAAERVRQHIAHLTVDTPLHGDPVSVTVSVGVAAFRENGHSVLELLDAADA 395
COG3706 338 TVRGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHELSREPLEVTISIGVAEGKPGEDSIEELLKRADK 417
|
170
....*....|....*
gi 117928368 396 ALYEAKRAGRNCVRV 410
COG3706 418 ALYKAKASGRNRVVV 432
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
8e-29 |
123.28 |
45.39 |
3,275,155,89,366,244,15,382,259,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 276 GGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFGGEEFVILLAGSDLEQAAVAAERVRQHIA 355
PRK09894 156 EPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEEFIIILKAATDEEACRAGERIRQLIA 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 117928368 356 HLTVDTPLHgdPVSVTVSVGVAAFREnGHSVLELLDAADAALYEAKRAGRNCVRVA 411
PRK09894 236 NQAITHSEG--RINITATFGVTRAFP-EEPLDEVIGRADRAMYEGKQAGRNRVMFI 288
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-18 |
88.03 |
42.59 |
3,250,212,108,362,320,5,367,326,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 251 DPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFGGEE 330
PRK10245 213 DGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 331 FVILLAGSDLEQAAVAAERVRQHIAHLTvdtpLHGDP-VSVTVSVGVAAFRENGHSVLELLDAADAALYEAKRAGRNCVR 409
PRK10245 293 FAVIMSGTPAESAITAMLRVHEGLNTLR----LPNAPqVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNRTE 368
|
..
gi 117928368 410 VA 411
PRK10245 369 VA 370
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
9e-17 |
83.22 |
16.22 |
4,231,667,5,236,677,4,241,681,114,357,795,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 232 VLVFQ-----RTLLiAELRHAARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVL 306
PRK09776 668 VLVFQdvtesRAML-RQLSYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 307 RAVAGGLTHGLRPRDFVGRFGGEEFVILLAGSDLEQAAVAAERVRQHIAhlTVDTPLHGDPVSVTVSVGVAAFRENGHSV 386
PRK09776 747 RELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAIN--DYRFPWEGRVYRVGASAGITAIDDNNHQA 824
|
170 180
....*....|....*....|....
gi 117928368 387 LELLDAADAALYEAKRAGRNCVRV 410
PRK09776 825 SEVMSQADIACYAAKNAGRGRVTV 848
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
4e-13 |
71.30 |
24.43 |
4,243,232,17,262,249,93,360,342,10,370,354,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 244 LRHAARTDPKTGLANAAywREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFV 323
PRK10060 233 LRILANTDSITGLPNRN--AIQELIDHAIAQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 324 GRFGGEEFVILLAGSDLEQAAVAAERVRQHIAhltvdTPLHGDPVSV--TVSVGVAAFRENGHSVLELLDAADAALYEAK 401
PRK10060 311 ARLGGDEFLVLASHTSQAALEAMASRILTRLR-----LPFRIGLIEVytGCSIGIALSPEHGDDSESLIRSADTAMYTAK 385
|
....*....
gi 117928368 402 RAGRNCVRV 410
PRK10060 386 EGGRGQFCV 394
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
7e-11 |
63.71 |
15.27 |
4,248,376,13,265,389,85,351,474,9,362,483,15 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 249 RTDPKTGLANAAYwrevAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRPRDFVGRFGG 328
PRK11359 377 QFDPMTGLPNRNN----LHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 117928368 329 EEFVILLAGSDLEQAAVAAERVrQHIAHLTVDtpLHGDPVSVTVSVGVA 377
PRK11359 453 TQFVLVSLENDVSNITQIADEL-RNVVSKPIM--IDDKPFPLTLSIGIS 498
|
|
|
|
|
|
|
-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 |
2e-09 |
58.88 |
31.07 |
4,239,219,98,339,317,74,413,394,22,435,420,5 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 240 LIAELRHAARTDPKTGLANAAYWREVAEREIARARSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTHGLRP 319
COG5001 220 LSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDGA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 320 RDFVGRFGGEEFVILLAGsdLEQAAVAAERVRQHIAHLTVDTPLHGDPVSVTVSVGVAAFRENGHSVLELLDAADAALYE 399
COG5001 300 PILAARLGGDEFALIIPA--LEDDALRVAGARALCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQLFERADYALYH 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 117928368 400 AKRAGRNCVRVATG---VRQQVLDLTGDTPRLIDLRTER----QPIVD 440
COG5001 378 AKQNGKGAAVLFDArheAAIRDMAVVEQALRSADLEQELsvhfQPIVD 425
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
6e-09 |
57.34 |
32.92 |
8,241,241,32,274,273,41,315,316,7,324,323,18,348,341,10,358,353,4,362,359,2,364,362,13 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928368 242 AELRHAARTDPKTGLANAAYWREVAEREIARArSGGESVAILLVDVDHFKAVNDRFGHLIGDDVLRAVAGGLTH--GLRP 319
PRK09966 242 AQLLRTALHDPLTGLANRAAFRSGINTLMNNS-DARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRH 320
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117928368 320 RDFvgRFGGEEFVILLAGSDLEQaavaaeRVRQHIAHLT--VDTP--LH-GDPVSVTVSVGVA 377
PRK09966 321 KAY--RLGGDEFAMVLYDVQSES------EVQQICSALTqiFNLPfdLHnGHQTTMTLSIGYA 375
|
|
|
|
|
|
|
-1 |