|
Name |
Accession |
Description |
Interval |
E-value |
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
6-371 |
0e+00 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 760.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 6 MNDENFFKKAAAHGEEPPLTPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLVLVGWAFVWPHLAW 85
Cdd:PRK10245 1 MNDENFYKKAAAHGEEPPLTPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLLLVGWAFVWPHLAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 86 QIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITV 165
Cdd:PRK10245 81 QIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 166 SFNSAPLEWWLSLPIIVIYPLLFGWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLL 245
Cdd:PRK10245 161 SFNSAPLEWWLSLPVIVIYPLLFAWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 246 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTP 325
Cdd:PRK10245 241 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 16128370 326 QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNRTEVAA 371
Cdd:PRK10245 321 QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNRTEVAA 366
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
209-371 |
1.92e-89 |
|
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: 266.13 E-value: 1.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 209 MSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRF 288
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 289 GGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNT--PQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAgsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 16128370 367 TEVAA 371
Cdd:TIGR00254 161 VVVAD 165
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
210-366 |
4.61e-65 |
|
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: 203.64 E-value: 4.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 210 STRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFG 289
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 290 GDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP---NTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
211-366 |
3.20e-63 |
|
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: 198.93 E-value: 3.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 211 TRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGG 290
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128370 291 DEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
108-370 |
7.06e-63 |
|
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: 202.52 E-value: 7.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 108 LAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITVSFNSAPLEWWLSLPI---IVIY 184
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLellLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 185 PLLFGWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVG 264
Cdd:COG2199 89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 265 DEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP-NTPQVTLRISVGVAPLNPQMS 343
Cdd:COG2199 169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElEGKELRVTVSIGVALYPEDGD 248
|
250 260
....*....|....*....|....*..
gi 16128370 344 HYREWLKSADLALYKAKKAGRNRTEVA 370
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
209-370 |
4.09e-61 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 193.62 E-value: 4.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 209 MSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRF 288
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 289 GGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNRTE 368
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 16128370 369 VA 370
Cdd:smart00267 162 VY 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
205-366 |
5.95e-49 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 165.54 E-value: 5.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 205 RLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDV 284
Cdd:NF038266 89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 285 IGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP-NTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAG 363
Cdd:NF038266 169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAG 248
|
...
gi 16128370 364 RNR 366
Cdd:NF038266 249 RDR 251
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
174-364 |
3.32e-21 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 94.64 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 174 WWLSLPIIVIYPLLFGWVSYqtatklaeHKRRLQVMSTR---DGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDID 250
Cdd:NF040885 310 WKLFLFYLLSTALLLHLVRM--------HFRLYHNVSREnisDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 251 HFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLrlpnTPQVTLR 330
Cdd:NF040885 382 KLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHLRTI----DPDKRVS 457
|
170 180 190
....*....|....*....|....*....|....
gi 16128370 331 ISVGVAPLNPQMShYREWLKSADLALYKAKKAGR 364
Cdd:NF040885 458 FSWGAYQMQPGDT-LDDAYKAADERLYLNKKQKH 490
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
6-371 |
0e+00 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 760.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 6 MNDENFFKKAAAHGEEPPLTPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLVLVGWAFVWPHLAW 85
Cdd:PRK10245 1 MNDENFYKKAAAHGEEPPLTPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLLLVGWAFVWPHLAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 86 QIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITV 165
Cdd:PRK10245 81 QIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 166 SFNSAPLEWWLSLPIIVIYPLLFGWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLL 245
Cdd:PRK10245 161 SFNSAPLEWWLSLPVIVIYPLLFAWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 246 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTP 325
Cdd:PRK10245 241 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 16128370 326 QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNRTEVAA 371
Cdd:PRK10245 321 QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNRTEVAA 366
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
209-371 |
1.92e-89 |
|
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: 266.13 E-value: 1.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 209 MSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRF 288
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 289 GGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNT--PQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAgsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 16128370 367 TEVAA 371
Cdd:TIGR00254 161 VVVAD 165
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
210-366 |
4.61e-65 |
|
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: 203.64 E-value: 4.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 210 STRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFG 289
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 290 GDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP---NTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
211-366 |
3.20e-63 |
|
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: 198.93 E-value: 3.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 211 TRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGG 290
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128370 291 DEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNR 366
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
108-370 |
7.06e-63 |
|
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: 202.52 E-value: 7.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 108 LAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITVSFNSAPLEWWLSLPI---IVIY 184
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLellLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 185 PLLFGWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVG 264
Cdd:COG2199 89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 265 DEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP-NTPQVTLRISVGVAPLNPQMS 343
Cdd:COG2199 169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElEGKELRVTVSIGVALYPEDGD 248
|
250 260
....*....|....*....|....*..
gi 16128370 344 HYREWLKSADLALYKAKKAGRNRTEVA 370
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
209-370 |
4.09e-61 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 193.62 E-value: 4.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 209 MSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRF 288
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 289 GGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNRTE 368
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 16128370 369 VA 370
Cdd:smart00267 162 VY 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
205-366 |
5.95e-49 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 165.54 E-value: 5.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 205 RLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDV 284
Cdd:NF038266 89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 285 IGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLP-NTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAG 363
Cdd:NF038266 169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAG 248
|
...
gi 16128370 364 RNR 366
Cdd:NF038266 249 RDR 251
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
172-366 |
1.68e-43 |
|
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: 159.94 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 172 LEWWLSLPIIVIYPLLFGWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDH 251
Cdd:COG5001 213 LLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 252 FKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAML-RVHEGLNT-LRLPNTpQVTL 329
Cdd:COG5001 293 FKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAeRILAALAEpFELDGH-ELYV 371
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128370 330 RISVGVApLNPQmsHYR---EWLKSADLALYKAKKAGRNR 366
Cdd:COG5001 372 SASIGIA-LYPD--DGAdaeELLRNADLAMYRAKAAGRNR 408
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
209-366 |
1.52e-40 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 148.51 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 209 MSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRF 288
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 289 GGDEFAVIMSGTPAESAITAM--LRVHEGLNTLRLPN-TPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRN 365
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAerIRRKIAEEPFIISDgKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRN 450
|
.
gi 16128370 366 R 366
Cdd:PRK09581 451 R 451
|
|
| MASE2 |
pfam05230 |
MASE2 domain; Predicted integral membrane sensory domain found in histidine kinases, ... |
40-128 |
1.65e-32 |
|
MASE2 domain; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins.
Pssm-ID: 428382 Cd Length: 89 Bit Score: 116.93 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 40 RVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLVLVGWAFVWPHLAWQIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVN 119
Cdd:pfam05230 1 RIYLPRVLGYGLGALCIAAGLYEQHFSVWVWLLLVLNALLWPHLAYLLSRRSRDPYRTEQRLLLIDALLGGFWIALMGFS 80
|
....*....
gi 16128370 120 VLPSTAMLM 128
Cdd:pfam05230 81 PLPSLVLLA 89
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
176-366 |
4.97e-32 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 126.67 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 176 LSLPIIVIYpLLFG---WVSYQTATKLAEH----KRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIID 248
Cdd:PRK15426 358 ISIALTLLW-ALFTamlLISWYVIRRMVSNmfvlQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLD 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 249 IDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVT 328
Cdd:PRK15426 437 LDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTT 516
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128370 329 LRI--SVGVAPLNPQMSHYREWLKS-ADLALYKAKKAGRNR 366
Cdd:PRK15426 517 IRIsaSLGVSSAEEDGDYDFEQLQSlADRRLYLAKQAGRNR 557
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
206-367 |
3.55e-27 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 109.00 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 206 LQVMSTRDGMTGVYNRRhweTMLRN-EFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDV 284
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRR---VLDESfDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYET 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 285 IGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLpNTPQVTLRI--SVGVAPLNPQMsHYREWLKSADLALYKAKKA 362
Cdd:PRK09894 202 VYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAI-THSDGRINItaTFGVSRAFPEE-TLDVVIGRADRAMYEGKQT 279
|
....*
gi 16128370 363 GRNRT 367
Cdd:PRK09894 280 GRNRV 284
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
193-369 |
2.02e-23 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 102.06 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 193 YQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALT 272
Cdd:PRK09776 648 IQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 273 RQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVtLRI--SVGVAPLNPQMSHYREWLK 350
Cdd:PRK09776 728 SLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRV-YRVgaSAGITLIDANNHQASEVMS 806
|
170
....*....|....*....
gi 16128370 351 SADLALYKAKKAGRNRTEV 369
Cdd:PRK09776 807 QADIACYAAKNAGRGRVTV 825
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
174-364 |
3.32e-21 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 94.64 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 174 WWLSLPIIVIYPLLFGWVSYqtatklaeHKRRLQVMSTR---DGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDID 250
Cdd:NF040885 310 WKLFLFYLLSTALLLHLVRM--------HFRLYHNVSREnisDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 251 HFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLrlpnTPQVTLR 330
Cdd:NF040885 382 KLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHLRTI----DPDKRVS 457
|
170 180 190
....*....|....*....|....*....|....
gi 16128370 331 ISVGVAPLNPQMShYREWLKSADLALYKAKKAGR 364
Cdd:NF040885 458 FSWGAYQMQPGDT-LDDAYKAADERLYLNKKQKH 490
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
197-364 |
1.42e-17 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 84.35 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 197 TKLAEHKR---RLQVMSTRDGMTGVYNRRHWETMLRNEFDNcrRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTR 273
Cdd:PRK10060 221 TDITEERRaqeRLRILANTDSITGLPNRNAIQELIDHAINA--ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 274 QLQITLRGSDVIGRFGGDEFAVIMSGTpAESAITAML-RVhegLNTLRLP---NTPQVTLRISVGVApLNPQMSHYREWL 349
Cdd:PRK10060 299 AILSCLEEDQTLARLGGDEFLVLASHT-SQAALEAMAsRI---LTRLRLPfriGLIEVYTGCSIGIA-LAPEHGDDSESL 373
|
170
....*....|....*.
gi 16128370 350 -KSADLALYKAKKAGR 364
Cdd:PRK10060 374 iRSADTAMYTAKEGGR 389
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
198-360 |
5.89e-13 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 69.65 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 198 KLAEHKRRLQVMSTR-------DGMTGVYNRRHWETMLrNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVA 270
Cdd:PRK09966 229 EMEEWQLRLQAKNAQllrtalhDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 271 LTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITamlRVHEGLNT-----LRLPNTPQVTLRISVGVApLNPQMSHY 345
Cdd:PRK09966 308 IAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQ---QICSALTQifnlpFDLHNGHQTTMTLSIGYA-MTIEHASA 383
|
170
....*....|....*
gi 16128370 346 REWLKSADLALYKAK 360
Cdd:PRK09966 384 EKLQELADHNMYQAK 398
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
242-360 |
1.67e-12 |
|
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: 63.91 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 242 ATLLIIDIDHFKSINDTWGHDVGDEA---IVALTRQLqiTLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNT 318
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELlneLAGRFDSL--IRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 16128370 319 LRLPNTPQVTLRISV-------GVAPLNPQMSHYREWLKSADLALYKAK 360
Cdd:cd07556 80 LNQSEGNPVRVRIGIhtgpvvvGVIGSRPQYDVWGALVNLASRMESQAK 128
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
283-360 |
8.09e-11 |
|
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: 60.31 E-value: 8.09e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128370 283 DVIGRFGGDEFAVIMSGTPAESAITAMLRVHEglnTLRLPNTPQVTlrISVGVAPLNpqmshyreWLKSADlALYKAK 360
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIRE---AVAELPSLRVT--VSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
201-311 |
1.23e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 62.86 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 201 EHKRRLQVMSTRDGMTGVYNRRHwetmLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLR 280
Cdd:PRK11359 367 KSRQHIEQLIQFDPLTGLPNRNN----LHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110
....*....|....*....|....*....|...
gi 16128370 281 GSDVIGRFGGDEFAVIMSGTPAESA--ITAMLR 311
Cdd:PRK11359 443 PDQYLCRIEGTQFVLVSLENDVSNItqIADELR 475
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
199-366 |
2.80e-03 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 39.54 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 199 LAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDAtLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQIT 278
Cdd:PRK11829 221 LADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFH-LLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQC 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128370 279 LRGSDVIGRFGGDEFAVIMSGTPAESaiTAMLRVHEGLNTLRLPNT-PQVTLR--ISVGVAPLNPQMSHYREWLKSADLA 355
Cdd:PRK11829 300 IDDSDLLAQLSKTEFAVLARGTRRSF--PAMQLARRIMSQVTQPLFfDEITLRpsASIGITRYQAQQDTAESMMRNASTA 377
|
170
....*....|.
gi 16128370 356 LYKAKKAGRNR 366
Cdd:PRK11829 378 MMAAHHEGRNQ 388
|
|
| |
