| 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 |
1e-33 |
138.88 |
98.73 |
3,160,1,117,278,118,5,283,124,32 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 161 DPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSVDE 240
cd01949 2 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGDE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94968987 241 FLILVPSSSVDSLGDIAERCRALVERANIQVGTEQLVaTISAG-ASAVDPLDTMEMFIRRLENYLQRSKYSGRNRI 315
cd01949 82 FAILLPGTDLEEAEELAERLRKAIEEPFFIDGEEIRV-TASIGiAEYPEDGEDLEELLRRADKALYQAKRSGRNRV 156
|
|
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 |
2e-31 |
131.60 |
99.38 |
3,158,1,111,269,114,21,290,136,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 159 FLDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSV 238
pfam00990 2 AHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94968987 239 DEFLILVPSSSVDSLGDIAERCRALVERANI--QVGTEQLVATISAGASAVDPL-DTMEMFIRRLENYLQRSKYSGRNR 314
pfam00990 82 DEFAILLPDTSLEGAQELAERIRRLLAALKIphTLSGLPLYVTISIGIAAYPNDgEDAEDLLKRADQALYQAKNQGRNR 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 |
4e-30 |
126.98 |
96.32 |
3,158,3,111,270,114,20,290,135,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 159 FLDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSV 238
smart00267 4 FRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94968987 239 DEFLILVPSSSVDSLGDIAERCRALVERANIqVGTEQLVATISAGASAVDPL-DTMEMFIRRLENYLQRSKYSGRNRI 315
smart00267 84 DEFALLLPETSLEEAIALAERILQQLREPII-IHGIPLYLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQV 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 |
8e-28 |
119.45 |
95.03 |
3,144,6,133,278,139,8,286,149,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 145 KARNQRAELLHSRGFLDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLA 224
COG2199 7 TRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVARRLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 225 NAVSEADILGRWSVDEFLILVPSSSVDSLGDIAERCRALVERANIQVGTEQLVaTISAGASA--VDPLDTMEMFIRRLEN 302
COG2199 87 SNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFFLGGEELRV-TVSIGVALypEDGSDDAELLLRRADL 165
|
170
....*....|...
gi 94968987 303 YLQRSKYSGRNRI 315
COG2199 166 ALYRAKRAGRNRV 178
|
|
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 |
4e-24 |
107.04 |
96.97 |
3,160,4,111,271,116,12,283,129,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 161 DPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSVDE 240
TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 241 FLILVPSSSVDSLGDIAERCRALVERANIQV-GTEQLVATISAG-ASAVDPLDTMEMFIRRLENYLQRSKYSGRNRITMK 318
TIGR00254 85 FVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGvACYPGHGLTLEELLKRADEALYQAKKAGRNRVVVA 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 |
| 128402 |
smart00091 |
PAS |
PAS domain |
PAS domain |
true |
false |
false |
67 |
1e-06 |
48.93 |
73.13 |
1,24,1,49 |
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 94968987 25 FFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQDNI 73
smart00091 2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
|
|
cl02459 |
141436 |
PAS |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most... |
-1 |
| 29035 |
cd00130 |
PAS |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most... |
false |
true |
false |
103 |
1e-04 |
42.57 |
71.84 |
3,32,0,41,75,41,11,90,52,22 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 33 LYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQDNIlnHVDDAGTQLCFgkcpLLTTIEHGVPHECEIYLHHKNG 112
cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI--HPEDREELRER----LENLLSGGEPVTLEVRLRRKDG 74
|
|
cl02459 |
141436 |
PAS |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most... |
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
2e-28 |
121.56 |
35.23 |
3,160,294,111,271,407,18,289,426,29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 161 DPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSVDE 240
PRK09581 295 DGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 241 FLILVPSSSVDSLGDIAERCRALVERANIQV--GTEQLVATISAGASAVDP-LDTMEMFIRRLENYLQRSKYSGRNRITM 317
PRK09581 375 FVVVMPDTDIEVAIAVAERIRRKIAEEPFAIsdGKERLNVTVSIGVAELRPsGESIEALIKRADKALYEAKNTGRNRVVA 454
|
.
gi 94968987 318 K 318
PRK09581 455 L 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 |
2e-27 |
117.71 |
39.31 |
3,147,259,126,273,387,16,289,404,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 148 NQRAELLHSRGFLDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAV 227
COG3706 260 RESLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 228 SEADILGRWSVDEFLILVPSSSVDSLGDIAERCRALVERANIQVGT--EQLVATISAGASAVDP-LDTMEMFIRRLENYL 304
COG3706 340 RGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHELsrEPLEVTISIGVAEGKPgEDSIEELLKRADKAL 419
|
170
....*....|.
gi 94968987 305 QRSKYSGRNRI 315
COG3706 420 YKAKASGRNRV 430
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
4e-26 |
113.65 |
61.43 |
2,133,105,47,182,152,133 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 134 AVEMFVEANSSKARNQRAELLHSRGFLDPLTDIGNRRYLEIELFKALqeFRQHGLPFGAILADIDHLRIVNEHYGHTVGD 213
PRK09894 106 AFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQL--RNREPLNLYLALLDIDRFKLVNDTYGHLIGD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 214 QVLRAVSLTLANAVSEADILGRWSVDEFLILVPSSSVDSLGDIAERCRALVERANIQVGTEQLVATISAGASAVDPLDTM 293
PRK09894 184 VVLRTLATYLASWTRPYETVYRYGGEEFIIILKAATDEEACRAGERIRQLIANQAITHSEGRINITATFGVTRAFPEEPL 263
|
170 180
....*....|....*....|..
gi 94968987 294 EMFIRRLENYLQRSKYSGRNRI 315
PRK09894 264 DEVIGRADRAMYEGKQAGRNRV 285
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
3e-15 |
77.44 |
20.25 |
7,29,563,42,71,607,7,78,618,13,92,631,7,105,638,33,140,671,19,160,690,99 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 30 LEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQD--NILNHVD----DAGTQLCFGKCPLlTTIEHGVphec 103
PRK09776 564 LDSIGEAVVCTDAAMKVTFMNPVAEKMTGWTQEEALGVPLLTvlHITFGDNgplmENPVEICLADTSR-SYLEQDV---- 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 104 eiYLHHKNGHRVPVRVHVTPVRDANNQIIGAVEMFveANSSKARNQRAELLHSRGFlDPLTDIGNRRYLEIELFKALQEF 183
PRK09776 639 --VLHSRSGGSYDVQYSIAPLSTLDGENIGSVLVF--QDVTESRAMLRQLSYSASH-DALTGLANRASFEKQLREALQTV 713
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94968987 184 RQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSVDEFLILVPSSSVDSLGDIAER 259
PRK09776 714 NSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATR 789
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
5e-13 |
69.92 |
43.94 |
5,148,203,9,160,212,92,252,308,12,269,320,20,289,341,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 149 QRAELLHSRgflDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVS 228
PRK10245 204 RRLQVMSTR---DGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 229 EADILGRWSVDEFLILVPSSSVDS----LGDIAERCRALVeraniQVGTEQLVATISAGASAVDP-LDTMEMFIRRLENY 303
PRK10245 281 GSDVIGRFGGDEFAVIMSGTPAESaitaMLRVHEGLNTLR-----LPNAPQVTLRISVGVAPLNPqMSHYREWLKSADLA 355
|
170
....*....|.
gi 94968987 304 LQRSKYSGRNR 314
PRK10245 356 LYKAKKAGRNR 366
|
|
|
|
|
|
|
-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-11 |
64.66 |
27.00 |
5,141,204,15,156,226,96,254,322,12,266,343,18,290,361,22 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 142 NSSKARNQRAELLHS-------RGFLDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQ 214
COG5001 205 QSQVTLTQRAEETRRlsdendrLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDR 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 215 VLRAVSLTLANAVSEADILGRWSVDEFLILVPSSSVDSlgDIAERCRALVER---------ANIQVGTEQLVATISAGAs 285
COG5001 285 LLIEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDA--LRVAGARALCESlqapydlrgVRVQVGASIGIAPFPSGA- 361
|
170 180
....*....|....*....|....*..
gi 94968987 286 avdplDTMEMFIRRLENYLQRSKYSGR 312
COG5001 362 -----DTSEQLFERADYALYHAKQNGK 383
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
3e-11 |
63.98 |
14.63 |
2,160,239,28,190,267,69 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 161 DPLTDIGNRRYLEIELFKALQEFRQHGLpfGAILADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSVDE 240
PRK10060 240 DSITGLPNRNAIQELIDHAIAQADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDE 317
|
90
....*....|....*....
gi 94968987 241 FLILVPSSSVDSLGDIAER 259
PRK10060 318 FLVLASHTSQAALEAMASR 336
|
|
|
|
|
|
|
-1 |
| 138539 |
PRK11360 |
PRK11360 |
sensory histidine kinase AtoS; Provisional |
sensory histidine kinase AtoS; Provisional |
true |
true |
false |
607 |
3e-07 |
51.23 |
34.43 |
12,4,233,12,16,253,50,66,304,2,75,306,10,88,316,14,102,331,10,113,341,33,146,377,14,160,400,6,168,406,21,191,427,9,200,437,5 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 5 SIPSTLTELGKI--------DAFVNSPTFFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIG-HYcqdniln 75
PRK11360 234 RLPPLPGELGQIsqainnlaQALREARTLNELIIENAADGIIAIDRQGDITTMNPAAEVITGYQRHELVGqPY------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 76 HVDDAGTQLCfgkCPLLTTIEHGVPHE-CEIYLHHKNGhRVPVRVHVTPVRDANNQIIGAVEMFVEANSSKA---RNQRA 151
PRK11360 307 SMLFDNTQFY---SPVLDTLEHGTEHVaLEISFPGRDR-TIELSVTTSRLHDTHGEMIGAVVIFSDLTARKRlqrRMARA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94968987 152 ELLHSRGFL---------DPLTDIgnRRYLEIELFKALQEFRQHGLPfgAILADIDHL-RIVNE 205
PRK11360 383 ERLAALGELmagvaheirNPLTAI--RGYVQILRQQTSDPIHQEYLS--VVLREVDSLnKVIQQ 442
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
3e-07 |
51.04 |
19.63 |
4,145,212,6,151,221,76,227,298,4,231,303,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 146 ARNQRA---ELLHSRGFLDPLTDIGNRRYLEIELFKALQEFRQHGLPFGAILADIDHLRIVNEHYGHTVGDQVLRAVSLT 222
PRK11059 213 ARKERSrfdTFIRSNAFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFELINL 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 94968987 223 LANAV-SEAD-ILGRWSVDEFLILVPSSSVDSLGDIAERCRALVER 266
PRK11059 293 LSTFVqRYPGaLLARYSRSDFAVLLPHRSLKEADSLASQLLKAVDS 338
|
|
|
|
|
|
|
-1 |
| 129332 |
TIGR00229 |
sensory_box |
PAS domain S-box |
PAS domain S-box |
false |
true |
false |
124 |
3e-06 |
47.66 |
37.90 |
1,21,0,47 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 94968987 22 SPTFFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHY 68
TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRN 47
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
6e-06 |
46.76 |
18.40 |
4,160,378,30,194,408,71,266,479,20,287,499,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 161 DPLTDIGNRRYLEIELFKALQEFRQHGLPFgailADIDHLRIVNEHYGHTVGDQVLRAVSLTLANAVSEADILGRWSVDE 240
PRK11359 379 DPMTGLPNRNNLHNYLDDLVDKAVSPVVYL----IGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94968987 241 FLILVPSSSVDSLGDIAERCRALVErANIQVGTEQLVATISAGASAvDPLDTMEMFIRRLENYLQRSKYSGRN 313
PRK11359 455 FVLVSLENDVSNITQIADELRNVVS-KPIMIDDKPFPLTLSIGISY-DVGKNRDYLLSTAHNAMDYIRKNGGN 525
|
|
|
|
|
|
|
-1 |
| 110021 |
pfam00989 |
PAS |
PAS fold |
PAS fold |
false |
true |
false |
112 |
1e-05 |
45.47 |
38.39 |
1,23,0,43 |
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 94968987 24 TFFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIG 66
pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIG 43
|
|
|
|
|
|
|
-1 |
| 33622 |
COG3829 |
RocR |
Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains [Transcription / Signal transduction mechanisms] |
Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains [... |
false |
true |
false |
560 |
1e-04 |
42.59 |
8.57 |
1,23,116,48 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 94968987 24 TFFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQD 71
COG3829 117 QRLEAILDSIDDGLLVVDEDGIIIYYNKAYAKLLGLSPEEVLGKHLLD 164
|
|
|
|
|
|
|
-1 |
| 117025 |
pfam08448 |
PAS_4 |
PAS fold |
PAS fold |
false |
true |
false |
110 |
1e-04 |
42.40 |
94.55 |
4,29,0,42,74,42,11,88,53,21,110,74,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 30 LEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQDnilNHVDDAGTQLCfgkCPLLTTIEHGVPHECEIYLHH 109
pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAE---LLPPEDAARLE---RALRRALEGEEPIDFLEELLL 74
|
90 100 110
....*....|....*....|....*....|.
gi 94968987 110 kNGHRVPVRVHVTPVRDANNQIIGAVEMFVE 140
pfam08448 75 -NGEERHYELRLTPLRDPDGEVIGVLVISRD 104
|
|
|
|
|
|
|
-1 |
| 32384 |
COG2202 |
AtoS |
FOG: PAS/PAC domain [Signal transduction mechanisms] |
FOG: PAS/PAC domain [Signal transduction mechanisms] |
false |
true |
false |
232 |
0.001 |
39.19 |
54.31 |
2,16,104,65,85,169,61 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 17 DAFVNSPTFFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQDNILNHVDDAGtqlcFGKCPLLTTIE 96
COG2202 105 EALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERR----ELELARALAEG 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 94968987 97 HGVPHECEIYLHHKNGHRVPVRVHVTPVRDANNQIIGAVEMFVEANSSKA 146
COG2202 181 RGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERKQ 230
|
|
|
|
|
|
|
-1 |
| 106506 |
PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
807 |
0.002 |
38.50 |
16.98 |
5,25,333,21,46,355,21,67,389,11,80,400,18,98,419,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94968987 26 FQRLLEELYEGVYFVDTHRRI-LYWNRAAHRISGYSAEEVIGH-------------YCQDNILNHVDdaGTQLCFGKCPL 91
PRK13560 334 LRAIIEAAPIAAIGLDADGNIcFVNNNAAERMLGWSAAEVMGKplpgmdpelneefWCGDFQEWYPD--GRPMAFDACPM 411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 94968987 92 LTTIEHG-VPHECEIYLHHKNGHRVPVRVHVTPVRDANNQIIGAVEMFVEANSSKARNQ 149
PRK13560 412 AKTIKGGkIFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEE 470
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
0.007 |
36.74 |
4.63 |
1,29,17,37 |
10 20 30
....*....|....*....|....*....|....*..
gi 94968987 30 LEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIG 66
PRK11359 18 LEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIG 54
|
|
|
|
|
|
|
-1 |
| 106506 |
PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
807 |
0.009 |
36.19 |
5.82 |
1,24,204,47 |
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 94968987 25 FFQRLLEELYEGVYFVDTHRRILYWNRAAHRISGYSAEEVIGHYCQD 71
PRK13560 205 FLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHD 251
|
|
|
|
|
|
|
-1 |
|