| 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 |
3e-48 |
189.34 |
100.00 |
2,723,0,114,837,116,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 724 TDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARFGGD 803
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94967216 804 EFVILMPETGVDQAQILAERLRLWIATDPMLSEH--QITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAGGNKVA 878
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFFIDGEeiRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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 |
| 28958 |
cd00077 |
HDc |
Metal dependent phosphohydrolases with conserved 'HD' motif |
Metal dependent phosphohydrolases with conserved 'HD' motif |
true |
false |
true |
145 |
9e-15 |
78.20 |
95.86 |
3,956,5,44,1007,49,26,1033,82,62 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 957 HGEQVARTAEIIARELGIGGQDIQDLIFAARIHDVGKIVVPEKIlnkpamlTEDEHYLVAMHANVGAEIIDAIPDAQ--- 1033
cd00077 6 HSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAI-------TEEESELEKDHAIVGAEILRELLLEEvik 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94967216 1034 ----HIRQMVRHHHEAFDGSGYPDGLKGEQIPLYARIISVAEAYVSMMVDRSYRAARSQADAVREL 1095
cd00077 79 lideLILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEEDLEEL 144
|
|
cl00076 |
140417 |
HDc |
Metal dependent phosphohydrolases with conserved 'HD' motif |
Metal dependent phosphohydrolases with conserved 'HD' motif |
2 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
2e-43 |
173.68 |
100.00 |
2,720,0,118,838,122,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 721 QSITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARF 800
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 801 GGDEFVILMPETGVDQAQILAERLRLWIATDPMLSEHQ----ITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAGGNK 876
TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSetltVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 94967216 877 VATAD 881
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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
2e-42 |
170.12 |
100.00 |
2,721,0,116,837,121,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 722 SITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARFG 801
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 802 GDEFVILMPETGVDQAQILAERLRLWIATDPMLSEH-----QITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAGGNK 876
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 |
2e-42 |
169.74 |
98.77 |
2,719,0,119,838,121,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 720 QQSITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVAR 799
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 800 FGGDEFVILMPETGVDQAQILAERLRLWIATDPMLSEHQ--ITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAGGNKV 877
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPlyLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
.
gi 94967216 878 A 878
smart00267 161 A 161
|
|
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 |
6e-38 |
154.89 |
91.71 |
3,715,13,123,838,138,15,853,154,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 716 QKMQQQSITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSN 795
COG2199 14 ERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVARRLRSNLREGD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 796 VVARFGGDEFVILMPETGVDQAQILAERLRLWIATDPMLSEHQ--ITGSFGVATYPIHGS-SVEDIMRVADAGMYVSKHA 872
COG2199 94 LVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFFLGGEElrVTVSIGVALYPEDGSdDAELLLRRADLALYRAKRA 173
|
....*.
gi 94967216 873 GGNKVA 878
COG2199 174 GRNRVV 179
|
|
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 |
| 128747 |
smart00471 |
HDc |
Metal dependent phosphohydrolases with conserved 'HD' motif. |
Metal dependent phosphohydrolases with conserved 'HD' motif. |
false |
false |
false |
124 |
2e-10 |
63.46 |
92.74 |
6,956,7,19,977,26,32,1017,58,9,1026,69,5,1031,76,13,1050,89,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 957 HGEQVARTAEIIARELGIGgqDIQDLIFAARIHDVGKIVVPEKILNKPAMLTEdehylvamHANVGAEII--DAIPD--A 1032
smart00471 8 HSLRVAQLAAALAEELGLL--DIELLLLAALLHDIGKPGTPDSFLVKTSVLED--------HHFIGAEILleEEEPRilE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 94967216 1033 QHIRQMVRHHHEafdgsgYPDGLKGEQIPLYARIISVAEAYVSMMVDRSYR 1083
smart00471 78 EILATAILSHHE------RPDGLRGEPITLEARIVKVADRLDALRRDRRYR 122
|
|
cl00076 |
140417 |
HDc |
Metal dependent phosphohydrolases with conserved 'HD' motif |
Metal dependent phosphohydrolases with conserved 'HD' motif |
-1 |
| 128379 |
smart00065 |
GAF |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
true |
false |
false |
149 |
2e-08 |
57.39 |
100.00 |
3,411,0,27,438,28,25,463,55,94 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 412 DPDEVLAAVHRELGRLFDTSNFYVAFL-EGLELRYEFETVGAIRQPRRSRRSK--NGLSDFVIRTGQPILIRSDMKRVSQ 488
smart00065 1 DLEELLQTILEELRQLLGADRVLIYLVdEDDRGELVLVAADGLTLPLLGLRYPlgEGLAGRVAETGRPLNIPDVEADPVF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94967216 489 RLGIEPSSHPAKCFIGVPIRIGAVSVGVVAALNFDREFVYEQRDVEVLATAAGQVAVAIENARMFAHEQ 557
smart00065 81 ALDLLGRYQGVRSFLAVPLVADGELVGVLALHNKDSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 110919 |
pfam01966 |
HD |
HD domain |
HD domain |
false |
false |
false |
108 |
7e-08 |
55.32 |
97.22 |
6,956,3,18,977,21,20,999,41,13,1017,54,19,1036,74,15,1057,89,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 957 HGEQVARTAEIIARELGIggqDIQDLIFAARIHDVGKIVVPekILNKPAMLTEDEHylvamHANVGAEIIDAIPDAQHIR 1036
pfam01966 4 HSLRVALLARELAEELGL---DPELLLLAALLHDIGKDPFG--FLEKLEDFGIFKS-----HSVVGAEILRELEKRLGVD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 94967216 1037 -QMVRHHHEAFDGSGYpdglkgEQIPLYARIISVAEAYVSM 1076
pfam01966 74 lELILEHHESWEGAGY------EPISLEARIVKLADRLDAL 108
|
|
cl00076 |
140417 |
HDc |
Metal dependent phosphohydrolases with conserved 'HD' motif |
Metal dependent phosphohydrolases with conserved 'HD' motif |
-1 |
| 32385 |
COG2203 |
FhlA |
FOG: GAF domain [Signal transduction mechanisms] |
FOG: GAF domain [Signal transduction mechanisms] |
false |
false |
false |
175 |
1e-06 |
51.17 |
98.29 |
4,397,3,42,439,51,12,451,65,40,491,106,69 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 398 ELLTQIGQVISSRLDPDEVLAAVHRELGRLFDTSNFYVAFLE------GLELRYEFETVG--AIRQPRRSRRSKNGLSDF 469
COG2203 4 ALLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDedglldGALVAEAAEAGLeqLIDELFGLVILPACLIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 470 VIRTGQPILIRSDMKRVSQRLG-IEPSSHPAKCFIGVPIRIGAVSVGVVAALNFDREFVYEQRDVEVLATAAGQVAVAIE 548
COG2203 84 ALREGRPVVVEDILQDPRFRDNpLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIE 163
|
170
....*....|..
gi 94967216 549 NARMFAHEQRRA 560
COG2203 164 RARLYEELQEAE 175
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 110584 |
pfam01590 |
GAF |
GAF domain |
GAF domain |
false |
false |
false |
153 |
2e-05 |
46.85 |
100.00 |
6,411,0,27,438,29,5,444,34,18,462,54,18,480,87,41,522,128,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 412 DPDEVLAAVHRELGRLFDTSNFYVAFL--EGLELrYEFETVGAIRQPRRSRRS--KNGLSDFVIRTGQPILIR------- 480
pfam01590 1 DLEELLQTILEELRELLGADRCAILLAdaDGLLL-YLVAGDGLSDIPLAARGLplGGGVVGEVIAGGNPIVVPdvqddpr 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94967216 481 --------SDMKRVSQRLGIEPSSHPAKCFIGVPIRIGAVSVGVVAALNfDREFVYEQRDVEVLATAAGQVAVAI 547
pfam01590 80 frdltalaEELPAPVGCHEHYLRGLGIRSCLAVPLLGGGKLIGVLVLHS-TSPRAFTEEELELLQALADQVAIAL 153
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 32139 |
COG1956 |
COG1956 |
GAF domain-containing protein [Signal transduction mechanisms] |
GAF domain-containing protein [Signal transduction mechanisms] |
true |
false |
false |
163 |
0.001 |
41.03 |
33.13 |
3,640,90,12,652,104,4,657,108,36 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 94967216 641 TGDTSLVQDTAA--THLAgILPDSRSALCIPITYAEQLLGVLNIESRRENAFTEE 693
COG1956 91 TGETVRVDDVHAfpGHIA-CDAASNSEIVVPIFKDGKLIGVLDIDSPTPGRFDEE 144
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 32388 |
COG2206 |
COG2206 |
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms] |
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms] |
false |
true |
false |
344 |
2e-42 |
169.93 |
54.07 |
3,931,125,15,946,141,88,1034,230,81 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 932 KREVMMDAILALNRA-SESRELFASGHGEQVARTAEIIARELGIGGQDIQDLIFAARIHDVGKIVVPEKILNKPAMLTED 1010
COG2206 126 AREIVKKALVALARGdIKAKDDYTYGHSVRVAELAEAIAKKLGLSEEKIEELALAGLLHDIGKIGIPDSILNKPGKLTEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 1011 EHYLVAMHANVGAEIIDAIPDAQH-IRQMVRHHHEAFDGSGYPDGLKGEQIPLYARIISVAEAYVSMMVDRSYRAARSQA 1089
COG2206 206 EFEIIKKHPIYGYDILKDLPEFLEsVRAVALRHHERWDGTGYPRGLKGEEIPLEARIIAVADVYDALTSDRPYKKAKSPE 285
|
170 180
....*....|....*....|....*.
gi 94967216 1090 DAVRELESRSGSQFDGMLVRILIRQF 1115
COG2206 286 EALEELRKNSGGKFDPKVVDAFLKAL 311
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
1e-39 |
160.85 |
36.32 |
2,720,290,118,838,413,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 721 QSITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARF 800
PRK09581 291 MAVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 801 GGDEFVILMPETGVDQAQILAERLRLWIATDPMLSEHQ-----ITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAGGN 875
PRK09581 371 GGEEFVVVMPDTDIEVAIAVAERIRRKIAEEPFAISDGkerlnVTVSIGVAELRPSGESIEALIKRADKALYEAKNTGRN 450
|
....*.
gi 94967216 876 KVATAD 881
PRK09581 451 RVVALA 456
|
|
|
|
|
|
|
-1 |
| 33243 |
COG3437 |
COG3437 |
Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription / Signal transduction mechanisms] |
Response regulator containing a CheY-like receiver domain and an HD-GYP domain [... |
false |
true |
false |
360 |
4e-37 |
152.37 |
48.06 |
2,941,173,88,1029,262,84 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 942 ALNRASESRELFASGHGEQVARTAEIIARELGIGGQDIQDLIFAARIHDVGKIVVPEKILNKPAMLTEDEHYLVAMHANV 1021
COG3437 174 ELAALLEVRDYETGDHLERVAQYSELLAELLGLSEEEVDLIKKAAPLHDIGKVAIPDSILLKPGKLTSEEFEIMKGHPIL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 1022 GAEIIDAI-PDAQHIRQMVRHHHEAFDGSGYPDGLKGEQIPLYARIISVAEAYVSMMVDRSYRAARSQADAVRELESRSG 1100
COG3437 254 GAEILKSSeRLMQVAAEIARHHHERWDGSGYPDGLKGDEIPLSARIVAIADVFDALVSGRPYKEAMSTEEALEIIRAQSG 333
|
170
....*....|...
gi 94967216 1101 SQFDGMLVRILIR 1113
COG3437 334 RLFDPKLVEAFIQ 346
|
|
|
|
|
|
|
-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 |
4e-35 |
145.83 |
38.39 |
2,715,263,123,838,391,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 716 QKMQQQSITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSN 795
COG3706 264 ERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLD 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 796 VVARFGGDEFVILMPETGVDQAQILAERLRLWIATDPMLSEHQ-----ITGSFGVATYPIHGSSVEDIMRVADAGMYVSK 870
COG3706 344 LVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHELSrepleVTISIGVAEGKPGEDSIEELLKRADKALYKAK 423
|
....*..
gi 94967216 871 HAGGNKV 877
COG3706 424 ASGRNRV 430
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
9e-31 |
131.37 |
53.92 |
4,724,132,19,745,151,90,835,244,10,846,254,36 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 725 DALTGSKTRRYFLEALQSEwkRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARFGGDE 804
PRK09894 133 DVLTGLPGRRVLDESFDHQ--LRNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 805 FVILMPETGVDQAQILAERLRLWIATDPMLS---EHQITGSFGVaTYPIHGSSVEDIMRVADAGMYVSKHAGGNKVATAD 881
PRK09894 211 FIIILKAATDEEACRAGERIRQLIANQAITHsegRINITATFGV-TRAFPEEPLDEVIGRADRAMYEGKQAGRNRVMFID 289
|
.
gi 94967216 882 E 882
PRK09894 290 E 290
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
3e-23 |
106.33 |
15.86 |
4,713,669,3,716,678,5,721,687,115,836,805,41 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 714 VFQ------KMQQQ----SITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARI 783
PRK09776 670 VFQdvtesrAMLRQlsysASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLREL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 784 ARLLEQKCRQSNVVARFGGDEFVILMPETGVDQAQILAERLRLWIATDPMLSE---HQITGSFGVATYPIHGSSVEDIMR 860
PRK09776 750 ASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYRFPWEgrvYRVGASAGITAIDDNNHQASEVMS 829
|
170
....*....|....*..
gi 94967216 861 VADAGMYVSKHAGGNKV 877
PRK09776 830 QADIACYAAKNAGRGRV 846
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
1e-19 |
94.03 |
22.62 |
4,723,238,21,746,259,70,816,333,15,833,348,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 724 TDALTGSKTRRYFLEALQSEWkrASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARFGGD 803
PRK10060 239 TDSITGLPNRNAIQELIDHAI--AQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGD 316
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94967216 804 EFVILMPETGVDQ----AQILAERLRLWIATDpmLSEHQITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAG 873
PRK10060 317 EFLVLASHTSQAAleamASRILTRLRLPFRIG--LIEVYTGCSIGIALSPEHGDDSESLIRSADTAMYTAKEGG 388
|
|
|
|
|
|
|
-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-19 |
93.17 |
22.93 |
4,724,230,91,815,326,10,828,336,9,837,346,36 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 725 DALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARFGGDE 804
COG5001 231 DSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDGAPILAARLGGDE 310
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94967216 805 FVILMPETGVD-----QAQILAERLRlwiATDPMLSEH-QITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAG 873
COG5001 311 FALIIPALEDDalrvaGARALCESLQ---APYDLRGVRvQVGASIGIAPFPSGADTSEQLFERADYALYHAKQNG 382
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
1e-18 |
91.11 |
45.01 |
2,715,203,109,824,314,56 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 716 QKMQQQSITDALTGSKTRRYFLEALQSEWKRASRSTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSN 795
PRK10245 204 RRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 796 VVARFGGDEFVILMPETGVDQAQILAERL--RLWIATDPMLSEHQITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAG 873
PRK10245 284 VIGRFGGDEFAVIMSGTPAESAITAMLRVheGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAG 363
|
....*..
gi 94967216 874 GNKVATA 880
PRK10245 364 RNRTEVA 370
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
1e-12 |
71.02 |
24.91 |
10,715,369,26,744,395,9,754,404,72,827,476,11,838,490,7,846,497,4,851,501,28,882,529,14,896,549,11,908,560,8 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 716 QKMQQQSITDALTGSKTRRYFLEALQsewKRASRSTRPfSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSN 795
PRK11359 370 QHIEQLIQFDPMTGLPNRNNLHNYLD---DLVDKAVSP-VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 796 VVARFGGDEFVILMPETGVDQAQILAERLRLwIATDPMLSEHQ---ITGSFGVaTYPIhGSSVEDIMRVADAGMYVSKHA 872
PRK11359 446 YLCRIEGTQFVLVSLENDVSNITQIADELRN-VVSKPIMIDDKpfpLTLSIGI-SYDV-GKNRDYLLSTAHNAMDYIRKN 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 94967216 873 GGNKVATadeFIDGQNTSVQRQLI------SAYVEGFLQREhYGPEYTSE 916
PRK11359 523 GGNGWQF---FSPAMNEMVKERLVlgaalkEAISNNQLKLV-YQPQIFAE 568
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
4e-08 |
56.18 |
38.57 |
6,716,242,29,745,272,7,754,279,55,809,336,32,841,370,13,855,383,16 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 717 KMQQQSITDALTGSKTRRYFLEALQSEWK-RASRSTRpfSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSN 795
PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNnSDARKTS--ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 796 VVARFGGDEFVILM--PETGVDQAQILAERLRLWIATDPMLSEHQITG--SFGVATYPIHGSSvEDIMRVADAGMYVSKH 871
PRK09966 321 KAYRLGGDEFAMVLydVQSESEVQQICSALTQIFNLPFDLHNGHQTTMtlSIGYAMTIEHASA-EKLQELADHNMYQAKH 399
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
1e-05 |
47.77 |
20.19 |
3,732,310,17,750,327,87,837,417,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 733 RRYFLEALQSEWKRASRsTRPFSVVMIDLDKFKQVNDTMGHLEGDLVLARIARLLEQKCRQSNVVARFGGDEFVILMPET 812
PRK11829 311 RSLFISLLEKEIASSTR-TDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGT 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94967216 813 GVDQAQILAERLRLWIATDPMLSEH---QITGSFGVATYPIHGSSVEDIMRVADAGMYVSKHAGGNKV 877
PRK11829 390 RRSFPAMQLARRIMSQVTQPLFFDEitlRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQI 457
|
|
|
|
|
|
|
-1 |
| 33404 |
COG3604 |
FhlA |
Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains [Transcription / Signal transduction mechanisms] |
Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains [... |
false |
true |
false |
550 |
6e-04 |
42.22 |
35.82 |
8,395,31,51,447,82,9,456,95,25,481,121,20,501,143,15,519,158,7,526,167,54,582,221,7 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 396 EFELLTQIGQVISSRLDPDEVLAAVHRELGRLFDTSNFYVAFLEGLELRYEfETVGAIRQP----RRSRRSKNGLSDFVI 471
COG3604 32 DIRILVELTNALLSPLRLERLLAEVAKELHSLFGCDASALLRLDSKNLIPL-ATDGLSKDHlgreQRFVVEGHPLLEQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94967216 472 RTGQPILIRS-DMKRVSQRLGIEPSSHPAKC--FIGVPIRIGAVSVGVvaaLNFDREF--VYEQRDVEVLATAAGQVAVA 546
COG3604 111 KAGRPLVFHPaDSLFPDPYDGLLPDTEGNKKhaCIGVPLKSGDKLIGA---LTLDHTEpdQFDEDLDEELRFLAALAALA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 94967216 547 IENARMFAHEQRRARYLSFLNNVSQTAISSQNAEemLSEIVGQ 589
COG3604 188 VANALLHRELSSLKERLEEENLALEEQLSEVVLE--VGGIIGR 228
|
|
|
|
|
|
|
-1 |
|