| 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-54 |
208.98 |
99.36 |
2,348,0,105,453,109,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 349 TDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVARYGGE 428
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927828 429 EFVVVLPDTDLAGAATAAENLRRRI----FGLDAEPRVTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGRNRV 500
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIeepfFIDGEEIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRV 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 |
1e-47 |
186.29 |
100.00 |
3,346,0,107,453,113,8,461,122,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 347 AATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVARYG 426
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 427 GEEFVVVLPDTDLAGAATAAENLRRRI------FGLDAEPR-VTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGRNR 499
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 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
1e-47 |
186.00 |
99.39 |
2,345,0,114,459,120,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 346 LAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVARY 425
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 426 GGEEFVVVLPDTDLAGAATAAENLRRRIFGLDAE------PRVTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGRNR 499
TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvagsetLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....
gi 117927828 500 VTLA 503
TIGR00254 161 VVVA 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 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
1e-46 |
182.83 |
98.16 |
2,344,0,108,452,112,48 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 345 LLAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVAR 424
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 425 YGGEEFVVVLPDTDLAGAATAAENLRRR----IFGLDAEPRVTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGRNRV 500
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQlrepIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 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 |
2e-42 |
168.37 |
97.24 |
3,329,2,124,453,130,23,476,154,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 330 TALALANSWLLEQITLLAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVA 409
COG2199 3 LRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 410 RALQQGCRSSDLVARYGGEEFVVVLPDTDLAGAATAAENLRRRI----FGLDAEPRVTVSLGVATFPLHGG-SPDHILSA 484
COG2199 83 RRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALeepfFLGGEELRVTVSIGVALYPEDGSdDAELLLRR 162
|
170
....*....|....*.
gi 117927828 485 ADAALYQSKSAGRNRV 500
COG2199 163 ADLALYRAKRAGRNRV 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 |
| 128379 |
smart00065 |
GAF |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
true |
false |
false |
149 |
6e-05 |
44.29 |
100.00 |
6,196,0,7,209,7,45,254,58,23,277,83,30,307,115,16,326,131,18 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 197 RLEEALHpadvgrVLVEAVHDDFLAPRAAIVVKSGPGDVILASVKTTPNRLSPAEDRS------IQSVRRERRTWRLGHI 270
smart00065 1 DLEELLQ------TILEELRQLLGADRVLIYLVDEDDRGELVLVAADGLTLPLLGLRYplgeglAGRVAETGRPLNIPDV 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927828 271 DRHRDRW--LAASFPGAQRLLLVPMSAGNNVDGVLVAEH--NARFGSRVDRRVVAMLeryASQTALALANSWLLEQIT 344
smart00065 75 EADPVFAldLLGRYQGVRSFLAVPLVADGELVGVLALHNkdSPRPFTEEDEELLQAL---ANQLAIALANAQLYEELR 149
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 32385 |
COG2203 |
FhlA |
FOG: GAF domain [Signal transduction mechanisms] |
FOG: GAF domain [Signal transduction mechanisms] |
false |
false |
false |
175 |
7e-04 |
40.77 |
96.57 |
4,186,1,57,243,69,30,273,102,45,319,147,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 187 DLLGLARLSQRLEEALHPADVGRVLVEAVHDDFLAPRAAIVVKSGPGDVILASVKTT-----------PNRLSPAEDRSI 255
COG2203 2 EEALLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGLLDGALVAEAaeagleqlideLFGLVILPACLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 256 QSVRRERRTWRLGHIDRH---RDRWLAASFPGAQRLLLVPMSAGNNVDGVLVAEHNARFGSRVDRRvVAMLERYASQTAL 332
COG2203 82 GIALREGRPVVVEDILQDprfRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEE-LELLEELAEQVAI 160
|
170
....*....|
gi 117927828 333 ALANSWLLEQ 342
COG2203 161 AIERARLYEE 170
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
7e-48 |
187.05 |
36.76 |
3,339,284,114,453,402,8,461,413,39 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 340 LEQITLLAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSS 419
PRK09581 285 LEQSIEMAVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGT 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 420 DLVARYGGEEFVVVLPDTDLAGAATAAENLRRRI----FGLDAEPR---VTVSLGVATFPLHGGSPDHILSAADAALYQS 492
PRK09581 365 DLIARYGGEEFVVVMPDTDIEVAIAVAERIRRKIaeepFAISDGKErlnVTVSIGVAELRPSGESIEALIKRADKALYEA 444
|
....*...
gi 117927828 493 KSAGRNRV 500
PRK09581 445 KNTGRNRV 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 |
7e-46 |
180.12 |
46.21 |
5,298,229,20,322,249,14,340,263,113,453,382,7,460,390,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 299 VDGVLVAEHNARFGSRVDRRvvamLERYASQTALALANswllEQITLLAATDMLTGVANRRTLEENLDRMFAQASRAAQP 378
COG3706 230 NDYITKPIEEGELRARLRRQ----LRRKRYERQLRESL----ERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 379 ISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVARYGGEEFVVVLPDTDLAGAATAAENLRRRI----- 453
COG3706 302 LSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKInelpf 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 117927828 454 -FGLDAEP-RVTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGRNRV 500
COG3706 382 vHELSREPlEVTISIGVAEGKPGEDSIEELLKRADKALYKAKASGRNRV 430
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
4e-34 |
141.38 |
55.63 |
4,343,126,28,373,154,83,456,242,17,474,259,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 344 TLLAATDMLTGVANRRTLEENLDRMFAQasRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVA 423
PRK09894 127 TIRSNMDVLTGLPGRRVLDESFDHQLRN--REPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVY 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 424 RYGGEEFVVVLPDTDLAGAATAAENLRRRIFGL-----DAEPRVTVSLGVATFPLhGGSPDHILSAADAALYQSKSAGRN 498
PRK09894 205 RYGGEEFIIILKAATDEEACRAGERIRQLIANQaithsEGRINITATFGVTRAFP-EEPLDEVIGRADRAMYEGKQAGRN 283
|
....*.
gi 117927828 499 RVTLAG 504
PRK09894 284 RVMFID 289
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-27 |
118.46 |
47.71 |
4,328,193,9,339,202,114,453,318,10,463,330,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 329 QTALALANSwlLEQITLLAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRV 408
PRK10245 194 QTATKLAEH--KRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVAL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 409 ARALQQGCRSSDLVARYGGEEFVVVLPDTDLAGAATAAENLRRRI--FGLDAEPRVT--VSLGVATFPLHGGSPDHILSA 484
PRK10245 272 TRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLntLRLPNAPQVTlrISVGVAPLNPQMSHYREWLKS 351
|
170
....*....|....*....
gi 117927828 485 ADAALYQSKSAGRNRVTLA 503
PRK10245 352 ADLALYKAKKAGRNRTEVA 370
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
3e-24 |
108.28 |
23.98 |
6,340,230,27,369,257,72,441,330,10,451,345,2,454,347,2,457,349,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 341 EQITLLAATDMLTGVANRRTLEENLDRmfAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSD 420
PRK10060 231 ERLRILANTDSITGLPNRNAIQELIDH--AIAQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 421 LVARYGGEEFVVVLPDTDLAG-AATAAENLRR-----RIfGLdAEPRVTVSLGVATFPLHGGSPDHILSAADAALYQSKS 494
PRK10060 309 TLARLGGDEFLVLASHTSQAAlEAMASRILTRlrlpfRI-GL-IEVYTGCSIGIALSPEHGDDSESLIRSADTAMYTAKE 386
|
...
gi 117927828 495 AGR 497
PRK10060 387 GGR 389
|
|
|
|
|
|
|
-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 |
5e-24 |
107.42 |
23.83 |
3,344,225,91,435,320,10,445,331,52 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 345 LLAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVAR 424
COG5001 226 RLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDGAPILAAR 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927828 425 YGGEEFVVVLP----DTDLAGAATA-AENLRRRIFGLDAEPRVTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGR 497
COG5001 306 LGGDEFALIIPaledDALRVAGARAlCESLQAPYDLRGVRVQVGASIGIAPFPSGADTSEQLFERADYALYHAKQNGK 383
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
8e-24 |
107.10 |
15.14 |
2,338,679,111,449,795,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 339 LLEQITLLAATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRS 418
PRK09776 680 MLRQLSYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRS 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 419 SDLVARYGGEEFVVVLPDTDLAGAATAAENL-----RRRIFGLDAEPRVTVSLGVATFPLHGGSPDHILSAADAALYQSK 493
PRK09776 760 SDVLARLGGDEFGLLLPDCNVESARFIATRIisainDYRFPWEGRVYRVGASAGITAIDDNNHQASEVMSQADIACYAAK 839
|
....*....
gi 117927828 494 SAGRNRVTL 502
PRK09776 840 NAGRGRVTV 848
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
1e-15 |
79.88 |
22.53 |
6,320,345,10,330,359,39,372,398,7,380,405,71,451,480,21,474,501,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 321 AMLERYASQT----ALALANSWLLEQITLLAATDMLTGVANRRTLEENLDRMFaqaSRAAQPIsVVMVDIDHFKHINDTF 396
PRK11359 346 AFIERVADISqhmaALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLV---DKAVSPV-VYLIGVDHIQDVIDSL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 397 GHQVGDQTLQRVARALQQGCRSSDLVARYGGEEFVVVLPDTDLAGAATAAENLRR----RIFGLDAEPRVTVSLGVATFP 472
PRK11359 422 GYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNvvskPIMIDDKPFPLTLSIGISYDV 501
|
170 180
....*....|....*....|....*.
gi 117927828 473 lhGGSPDHILSAADAALYQSKSAGRN 498
PRK11359 502 --GKNRDYLLSTAHNAMDYIRKNGGN 525
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
3e-11 |
65.43 |
48.65 |
6,307,200,21,328,223,13,341,242,32,374,274,60,434,338,35,469,374,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 308 NARFGSRVDRRVVAMLERYAS--QTALALANSWLLE------QITLLAATDMLTGVANRRTLEENLDRMFAQASrAAQPI 379
PRK09966 201 NRNFSRRVSEERIAEFHRFALdfNSLLDEMEEWQLRlqaknaQLLRTALHDPLTGLANRAAFRSGINTLMNNSD-ARKTS 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 380 SVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVARYGGEEFVVVL----PDTDLAGAATAAENLRRRIFG 455
PRK09966 280 ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLydvqSESEVQQICSALTQIFNLPFD 359
|
170 180 190
....*....|....*....|....*....|....*....
gi 117927828 456 LDAEPRVTVSLGVA-TFPLHGGSPDHILSAADAALYQSK 493
PRK09966 360 LHNGHQTTMTLSIGyAMTIEHASAEKLQELADHNMYQAK 398
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
1e-04 |
43.33 |
23.52 |
6,346,227,72,418,301,38,457,339,6,463,350,9,473,359,16,492,375,3 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 347 AATDMLTGVANRRTLEENLDRMFAQASRAAQPISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRS--SDLVAR 424
PRK11059 228 AFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELGESQVDELLFELINLLSTFVQRypGALLAR 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927828 425 YGGEEFVVVLPDTDLAGAATAAENLRRRIFGLdAEPRVT-----VSLGVATFPlHGGSPDHILSAADAALyqsKSA 495
PRK11059 308 YSRSDFAVLLPHRSLKEADSLASQLLKAVDSL-PPPKMLdrddfLHIGIAAYR-SGQSTEQVMEEAEMAL---RSA 378
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
0.004 |
38.14 |
21.29 |
4,351,304,26,378,330,60,441,390,19,460,417,42 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927828 352 LTGVANRRTLEENLDRMFAQASRAAQpISVVMVDIDHFKHINDTFGHQVGDQTLQRVARALQQGCRSSDLVARYGGEEFV 431
PRK11829 305 VTELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFA 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117927828 432 VVLPDTDlagAATAAENLRRRIFGLDAEP--------RVTVSLGVATFPLHGGSPDHILSAADAALYQSKSAGRNRVTL 502
PRK11829 384 VLARGTR---RSFPAMQLARRIMSQVTQPlffdeitlRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMV 459
|
|
|
|
|
|
|
-1 |
|