|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
196-465 |
2.73e-46 |
|
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: 162.07 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 196 LLPVMVLVLSIILGVAVGGAESITFPLPALIWCAIRYPLPLTCLLTFLTGIGEILLVANALIHLSPDAHLQPWQLFSTRL 275
Cdd:COG2199 6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 276 GIAAMLISpVIVASSVDAINNLVKQLALRADFDFQTRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWG 352
Cdd:COG2199 86 LLLALLLL-LLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARregRPLALLLIDLDHFKRINDTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 353 HECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGLECRP 432
Cdd:COG2199 165 HAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYP 244
|
250 260 270
....*....|....*....|....*....|...
gi 695773294 433 VGGGRITELFNQllmaADDYLINAKQAGRNRIC 465
Cdd:COG2199 245 EDGDSAEELLRR----ADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
311-465 |
2.44e-44 |
|
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: 152.71 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 311 TRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAV 387
Cdd:cd01949 6 TGLPNRRAFEERLERLLARARrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDEFAI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695773294 388 AMLSATPQEGQLLAEKIRQGVAAQTFVWGpHKIKLTLSMGLECRPVGGGRITELFNQllmaADDYLINAKQAGRNRIC 465
Cdd:cd01949 86 LLPGTDLEEAEALAERLREAIEEPFFIDG-QEIRVTASIGIATYPEDGEDAEELLRR----ADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
305-463 |
3.09e-41 |
|
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: 144.70 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 305 ADFDFQTRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIG 381
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALregSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 382 GEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVW--GPHKIKLTLSMGLECRPVGGgritELFNQLLMAADDYLINAKQA 459
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHtvSGLPLYVTISIGIAAYPNDG----EDPEDLLKRADTALYQAKQA 156
|
....
gi 695773294 460 GRNR 463
Cdd:pfam00990 157 GRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
303-465 |
1.23e-38 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 137.76 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 303 LRADFDFQTRVYSRSGLSEALKRQPQSATQQ---LTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVAR 379
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 380 IGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGpHKIKLTLSMGLECRPVGGGRItelfNQLLMAADDYLINAKQA 459
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHG-IPLYLTISIGVAAYPNPGEDA----EDLLKRADTALYQAKKA 155
|
....*.
gi 695773294 460 GRNRIC 465
Cdd:smart00267 156 GRNQVA 161
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
268-465 |
2.11e-31 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 127.05 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 268 WQLFStrlgiAAMLISPVIVASSVDaiNNLVKQLALR--ADFDFQTRVYSRSGLSE---ALKRQPQSATQQLTVMLLDID 342
Cdd:PRK15426 366 WALFT-----AMLLISWYVIRRMVS--NMFVLQSSLQwqAWHDPLTRLYNRGALFEkarALAKRCQRDQQPFSVIQLDLD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 343 GFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGPHK-IK 421
Cdd:PRK15426 439 HFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTtIR 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695773294 422 LTLSMGL-ECRPVGGGRitelFNQLLMAADDYLINAKQAGRNRIC 465
Cdd:PRK15426 519 ISASLGVsSAEEDGDYD----FEQLQSLADRRLYLAKQAGRNRVC 559
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
311-464 |
2.34e-31 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 120.86 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 311 TRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAV 387
Cdd:NF038266 100 TGLPNRRLLMERLREEVERARrsgRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLL 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695773294 388 AMLSATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGL-ECRPVGggritELFNQLLMAADDYLINAKQAGRNRI 464
Cdd:NF038266 180 LLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLaEHRPPE-----EGLSATLSRADQALYQAKRAGRDRV 252
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
311-464 |
8.89e-31 |
|
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: 116.67 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 311 TRVYSRSGLSEALKRQPQSA---TQQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAV 387
Cdd:TIGR00254 8 TGLYNRRYLEEMLDSELKRArrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEEFVV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695773294 388 aMLSATPQEGQL-LAEKIRQGVAAQTF-VWGPHKIKLTLSMGLECRPVGGgritELFNQLLMAADDYLINAKQAGRNRI 464
Cdd:TIGR00254 88 -ILPGTPLEDALsKAERLRDAINSKPIeVAGSETLTVTVSIGVACYPGHG----LTLEELLKRADEALYQAKKAGRNRV 161
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
18-288 |
1.14e-05 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 48.13 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 18 VRDALVLFTITLllhfFGAML-RLVQELSFFWPLNAVMVGIFARYVWLNRSYFYATCFVAMMVYDGLTSRW-GMGFASLL 95
Cdd:PRK09776 1 VSLGLVSFIFTL----FSLELsRFPTTLAPLWFPTAIMMVAFYRHAGRMWPGILLSCSLGNIAANILLFSTsSLNLTWTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 96 INFSNIVFIVSLAQLLL-WDkrrtdsmpGPINVLN-----LFCYCLLAAFLSaavGTLGSMDVERETFISLLADWFSEQF 169
Cdd:PRK09776 77 INLVEAVVGAVLLRKLLpWY--------NPLQNLAdwlrlALGSAIVPPLLG---GVLVVLLTPGDDPLRAFLIWVLSEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 170 STAVLILPFILTVTIPSTLSGFRWSQLLP-VMVLVLSIILGVA--VGGAESITFPLPALIWCAIRYPLPLTCLLTFLTgi 246
Cdd:PRK09776 146 IGMLALVPLGLLFKPHYLLRHRNPRLLFEsLLTLAITLTLSWLalLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTT-- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 695773294 247 geILLVAnALIHLSPDAHLQPWQLF---STRLGIAAMLISPVIVA 288
Cdd:PRK09776 224 --VMMVS-LMMAADPSLLATPRTYLmshMPWLPFLLILLPANIMT 265
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
196-465 |
2.73e-46 |
|
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: 162.07 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 196 LLPVMVLVLSIILGVAVGGAESITFPLPALIWCAIRYPLPLTCLLTFLTGIGEILLVANALIHLSPDAHLQPWQLFSTRL 275
Cdd:COG2199 6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 276 GIAAMLISpVIVASSVDAINNLVKQLALRADFDFQTRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWG 352
Cdd:COG2199 86 LLLALLLL-LLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARregRPLALLLIDLDHFKRINDTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 353 HECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGLECRP 432
Cdd:COG2199 165 HAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYP 244
|
250 260 270
....*....|....*....|....*....|...
gi 695773294 433 VGGGRITELFNQllmaADDYLINAKQAGRNRIC 465
Cdd:COG2199 245 EDGDSAEELLRR----ADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
311-465 |
2.44e-44 |
|
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: 152.71 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 311 TRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAV 387
Cdd:cd01949 6 TGLPNRRAFEERLERLLARARrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDEFAI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695773294 388 AMLSATPQEGQLLAEKIRQGVAAQTFVWGpHKIKLTLSMGLECRPVGGGRITELFNQllmaADDYLINAKQAGRNRIC 465
Cdd:cd01949 86 LLPGTDLEEAEALAERLREAIEEPFFIDG-QEIRVTASIGIATYPEDGEDAEELLRR----ADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
305-463 |
3.09e-41 |
|
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: 144.70 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 305 ADFDFQTRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIG 381
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALregSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 382 GEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVW--GPHKIKLTLSMGLECRPVGGgritELFNQLLMAADDYLINAKQA 459
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHtvSGLPLYVTISIGIAAYPNDG----EDPEDLLKRADTALYQAKQA 156
|
....
gi 695773294 460 GRNR 463
Cdd:pfam00990 157 GRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
303-465 |
1.23e-38 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 137.76 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 303 LRADFDFQTRVYSRSGLSEALKRQPQSATQQ---LTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVAR 379
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 380 IGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGpHKIKLTLSMGLECRPVGGGRItelfNQLLMAADDYLINAKQA 459
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHG-IPLYLTISIGVAAYPNPGEDA----EDLLKRADTALYQAKKA 155
|
....*.
gi 695773294 460 GRNRIC 465
Cdd:smart00267 156 GRNQVA 161
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
59-465 |
6.84e-33 |
|
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: 132.21 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 59 ARYVWLNRSYFYATCFVAMMVYDGLTSRWGMGFASLLINFSNIVFIVSLAQLLLWDKRRTDSMPGPINVLNLFCYCLLAA 138
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 139 FLSAAVGTLGSMDVERETFISLLADWFSEQFSTAVLILPFILTVTIPSTLSGFRWSQLLPVMVLVLSIILGVAVGGAESI 218
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 219 TFPLPALIWCAIRYPLPLTCLLTFLTGIGEILLVANALIHLSPDAHLQPWQLFSTRLGIAAMLISPVIVASSVDAINNLV 298
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 299 K----QLALRADFDFQTRVYSRSGLSEALKR---QPQSATQQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLV 371
Cdd:COG5001 241 KraeeRLRHLAYHDPLTGLPNRRLFLDRLEQalaRARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 372 GEQGLVARIGGEEFAVAMLS-ATPQEGQLLAEKIRQgVAAQTFVWGPHKIKLTLSMGLECRPVGGGRITElfnqLLMAAD 450
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILA-ALAEPFELDGHELYVSASIGIALYPDDGADAEE----LLRNAD 395
|
410
....*....|....*
gi 695773294 451 DYLINAKQAGRNRIC 465
Cdd:COG5001 396 LAMYRAKAAGRNRYR 410
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
268-465 |
2.11e-31 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 127.05 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 268 WQLFStrlgiAAMLISPVIVASSVDaiNNLVKQLALR--ADFDFQTRVYSRSGLSE---ALKRQPQSATQQLTVMLLDID 342
Cdd:PRK15426 366 WALFT-----AMLLISWYVIRRMVS--NMFVLQSSLQwqAWHDPLTRLYNRGALFEkarALAKRCQRDQQPFSVIQLDLD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 343 GFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGPHK-IK 421
Cdd:PRK15426 439 HFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTtIR 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695773294 422 LTLSMGL-ECRPVGGGRitelFNQLLMAADDYLINAKQAGRNRIC 465
Cdd:PRK15426 519 ISASLGVsSAEEDGDYD----FEQLQSLADRRLYLAKQAGRNRVC 559
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
311-464 |
2.34e-31 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 120.86 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 311 TRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAV 387
Cdd:NF038266 100 TGLPNRRLLMERLREEVERARrsgRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLL 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695773294 388 AMLSATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGL-ECRPVGggritELFNQLLMAADDYLINAKQAGRNRI 464
Cdd:NF038266 180 LLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLaEHRPPE-----EGLSATLSRADQALYQAKRAGRDRV 252
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
311-464 |
8.89e-31 |
|
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: 116.67 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 311 TRVYSRSGLSEALKRQPQSA---TQQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAV 387
Cdd:TIGR00254 8 TGLYNRRYLEEMLDSELKRArrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEEFVV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695773294 388 aMLSATPQEGQL-LAEKIRQGVAAQTF-VWGPHKIKLTLSMGLECRPVGGgritELFNQLLMAADDYLINAKQAGRNRI 464
Cdd:TIGR00254 88 -ILPGTPLEDALsKAERLRDAINSKPIeVAGSETLTVTVSIGVACYPGHG----LTLEELLKRADEALYQAKKAGRNRV 161
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
301-464 |
4.18e-30 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 118.63 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 301 LALRADFDFQTRVYSRSGLSEALKRQPQSATQQ-LTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVAR 379
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQnLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 380 IGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGL-ECRPvgggriTELFNQLLMAADDYLINAKQ 458
Cdd:PRK09894 205 YGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVsRAFP------EETLDVVIGRADRAMYEGKQ 278
|
....*.
gi 695773294 459 AGRNRI 464
Cdd:PRK09894 279 TGRNRV 284
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
334-466 |
1.28e-28 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 117.69 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 334 LTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTF 413
Cdd:PRK09581 324 LSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPF 403
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 695773294 414 VW--GPHKIKLTLSMGL-ECRPVGggritELFNQLLMAADDYLINAKQAGRNRICT 466
Cdd:PRK09581 404 IIsdGKERLNVTVSIGVaELRPSG-----DTIEALIKRADKALYEAKNTGRNRVVA 454
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
17-464 |
3.48e-28 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 117.98 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 17 PVRDALVLFTITLLLHFFGAML-RLVQELSFFWPLNAVMVGIFARYVWLNRSYFYATCFVAMMVYDGLTSRWgmgFASLL 95
Cdd:COG3447 13 PLLRLLLLALLYFLLALLGLLLaRPPGGVSPIWPPAGVALAALLRFGRRAWPGILLGALLANLLAGLTGDPL---LLALL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 96 INFSNIVFIVSLAQLLLWDKRRTDSMPGPINVLNL-FCYCLLAAFLSAAVGTLG---SMDVERETFISLLADWFSEQFST 171
Cdd:COG3447 90 IALGNTLEALLAAWLLRRLLGFSPPLQRLRDVLRFlLAAALLAPLISALLGALAlalAGLLPGSPFLSSWLTWWLGDALG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 172 AVLILPFILTVTIPSTLSGFRWSQLLPVMVLVLSIILGVAV--GGAESITF-PLPALIWCAIRYPLPLTCLLTFLTGIGE 248
Cdd:COG3447 170 ILLVTPLLLAWRRPRLRRLRRRRLLEALALLALLLLVSWLVfgLLGYPLAFlLFPLLLWAALRFGLRGAALAVLLLALIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 249 ILLVANALIHLSPDAHLQpwQLFSTRLGIAAMLISPVIVA----------------SSVDAINNLVKQLALRADFDFQTR 312
Cdd:COG3447 250 ILATALGLGPFASLSPNQ--SLLLLQLFLAVLALTGLLLAaalaerrrqrlrerelALRAALELLALGLLLAALDDALLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 313 VYSRSGLSEALKRQPQ-SATQQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLS 391
Cdd:COG3447 328 LNARGLLLLALSLAALlLLRLALLLLLLALDALLLLLADDDRGELRGDLLRRRGATRLGAVVARLLRRSGGRGEEVVVLL 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695773294 392 ATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGLECRPVGGGRITELFNQLLMAADDYLINAKQAGRNRI 464
Cdd:COG3447 408 VIAQVEEALELALRERREERLLERLALALELLAITAALLAAALLLALADLLLLLLAEAAQLLARALLLGLDRL 480
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
333-436 |
5.70e-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: 68.54 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 333 QLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGE-QGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQ 411
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100
....*....|....*....|....*
gi 695773294 412 TFVWGPHkikLTLSMGLECRPVGGG 436
Cdd:cd07556 81 NQSEGNP---VRVRIGIHTGPVVVG 102
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
299-463 |
2.52e-13 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 71.01 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 299 KQLALRADFDFQTRVYSRSGLSEALKRQPQSATQ---QLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQG 375
Cdd:PRK10245 199 RRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRhhrDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 376 LVARIGGEEFAVAMlSATPQEGQLLA-EKIRQGVAAQTFVWGPhKIKLTLSMGLEcrPVGggriTEL--FNQLLMAADDY 452
Cdd:PRK10245 279 VIGRFGGDEFAVIM-SGTPAESAITAmSRVHEGLNTLRLPNAP-QVTLRISVGVA--PLN----PQMshYREWLKSADLA 350
|
170
....*....|.
gi 695773294 453 LINAKQAGRNR 463
Cdd:PRK10245 351 LYKAKNAGRNR 361
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
282-464 |
3.21e-13 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 72.01 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 282 ISPVIVASSVDAINNLVKQLALRADFDFQTRVYSRSGLSEALKRQPQSAT---QQLTVMLLDIDGFKRVNDSWGHECGDC 358
Cdd:PRK09776 642 IGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNsthQRHALVFIDLDRFKAVNDSAGHAAGDA 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 359 VLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMGLECRPVGGGRI 438
Cdd:PRK09776 722 LLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQA 801
|
170 180
....*....|....*....|....*.
gi 695773294 439 TELFNQllmaADDYLINAKQAGRNRI 464
Cdd:PRK09776 802 SEVMSQ----ADIACYAAKNAGRGRV 823
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
293-427 |
1.50e-11 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 65.80 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 293 AINNLVKQLALRADFdfqtrvysRSGLSEALKRQpqSATQQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVG 372
Cdd:PRK09966 248 ALHDPLTGLANRAAF--------RSGINTLMNNS--DARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGG 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 695773294 373 EQGLVARIGGEEFAVAMLSATPQ-EGQLLAEKIRQGVAAQTFVWGPHKIKLTLSMG 427
Cdd:PRK09966 318 LRHKAYRLGGDEFAMVLYDVQSEsEVQQICSALTQIFNLPFDLHNGHQTTMTLSIG 373
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
331-459 |
8.72e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 60.94 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 331 TQQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAA 410
Cdd:PRK11359 401 AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK 480
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 695773294 411 QTFVWGpHKIKLTLSMGLEcRPVGGGRitelfnqllmaaDDYLINAKQA 459
Cdd:PRK11359 481 PIMIDD-KPFPLTLSIGIS-YDVGKNR------------DYLLSTAHNA 515
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
305-473 |
1.27e-09 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 60.47 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 305 ADFDFQTRVYSRSGLSEALKRQPQSAT-QQLTVMLLDIDGFKRVNDSWGHECGDCVLAQFAQRVRDLVGEQGLVARIGGE 383
Cdd:PRK10060 237 ANTDSITGLPNRNAIQELIDHAINAADnNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGD 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 384 EFAV-------AMLSATpqeGQLLAEKIRqgvaaQTFVWGPHKIKLTLSMGLECRPVGGgritELFNQLLMAADDYLINA 456
Cdd:PRK10060 317 EFLVlashtsqAALEAM---ASRILTRLR-----LPFRIGLIEVYTGCSIGIALAPEHG----DDSESLIRSADTAMYTA 384
|
170
....*....|....*..
gi 695773294 457 KQAGRNRICTPTLAENQ 473
Cdd:PRK10060 385 KEGGRGQFCVFSPEMNQ 401
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
376-428 |
9.96e-07 |
|
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: 48.75 E-value: 9.96e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 695773294 376 LVARIGGEEFAVAMLSATPQEGQLLAEKIRQGVAAqtfvwgPHKIKLTLSMGL 428
Cdd:COG3706 117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVAE------LPSLRVTVSIGV 163
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
18-288 |
1.14e-05 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 48.13 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 18 VRDALVLFTITLllhfFGAML-RLVQELSFFWPLNAVMVGIFARYVWLNRSYFYATCFVAMMVYDGLTSRW-GMGFASLL 95
Cdd:PRK09776 1 VSLGLVSFIFTL----FSLELsRFPTTLAPLWFPTAIMMVAFYRHAGRMWPGILLSCSLGNIAANILLFSTsSLNLTWTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 96 INFSNIVFIVSLAQLLL-WDkrrtdsmpGPINVLN-----LFCYCLLAAFLSaavGTLGSMDVERETFISLLADWFSEQF 169
Cdd:PRK09776 77 INLVEAVVGAVLLRKLLpWY--------NPLQNLAdwlrlALGSAIVPPLLG---GVLVVLLTPGDDPLRAFLIWVLSEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773294 170 STAVLILPFILTVTIPSTLSGFRWSQLLP-VMVLVLSIILGVA--VGGAESITFPLPALIWCAIRYPLPLTCLLTFLTgi 246
Cdd:PRK09776 146 IGMLALVPLGLLFKPHYLLRHRNPRLLFEsLLTLAITLTLSWLalLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTT-- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 695773294 247 geILLVAnALIHLSPDAHLQPWQLF---STRLGIAAMLISPVIVA 288
Cdd:PRK09776 224 --VMMVS-LMMAADPSLLATPRTYLmshMPWLPFLLILLPANIMT 265
|
|
| |
