| 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 |
8e-33 |
136.18 |
98.09 |
6,187,1,23,210,28,58,268,87,16,285,103,9,297,112,15,312,128,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 188 DPLTGLKNRRRMERAVAERMGRE----QPFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWGGDE 263
cd01949 2 DPLTGLPNRRAFEERLERLLARArrsgRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGDE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116623715 264 FVVLL-DCGPEDVGRHLERVRQwVFGDYVVQDqgvPHRLPIIASVGTAVW-QGGESMAELFARADRDMYQEKNAVRQR 339
cd01949 82 FAILLpGTDLEEAEELAERLRK-AIEEPFFID---GEEIRVTASIGIAEYpEDGEDLEELLRRADKALYQAKRSGRNR 155
|
|
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 |
3e-29 |
124.28 |
100.00 |
6,184,0,27,211,31,57,268,89,16,290,105,14,304,124,8,312,133,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 185 ASLDPLTGLKNRRRMERAVAERMGREQ----PFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWG 260
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQrrqsPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 261 GDEFVVLL-DCGPEDVGRHLERVRQwvfgdyVVQDQGVPHRLPII-----ASVGTAVW-QGGESMAELFARADRDMYQEK 333
pfam00990 81 GDEFAILLpDTSLEGAQELAERIRR------LLAALKIPHTLSGLplyvtISIGIAAYpNDGEDAEDLLKRADQALYQAK 154
|
....*.
gi 116623715 334 NAVRQR 339
pfam00990 155 NQGRNR 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-27 |
118.30 |
97.24 |
5,166,1,45,211,50,57,268,108,26,298,134,14,312,150,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 167 MRGELRHYQARLEEAERLASLDPLTGLKNRRRMERAVAERMGREQ----PFSVVLLDLNGFKQVNDSYGHAAGDDVLKQF 242
COG2199 2 LLRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARrhgePLALLLLDLDHFKQINDTYGHAAGDEVLREV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 243 ATELRSAFRAADDVGRWGGDEFVVLL-DCGPEDVGRHLERVRQWVFGDYVVQDqgvpHRLPIIASVGTAVW--QGGESMA 319
COG2199 82 ARRLRSNLREGDLVARLGGDEFAVLLpGTSLEEAARLAERIRAALEEPFFLGG----EELRVTVSIGVALYpeDGSDDAE 157
|
170 180
....*....|....*....|
gi 116623715 320 ELFARADRDMYQEKNAVRQR 339
COG2199 158 LLLRRADLALYRAKRAGRNR 177
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
2e-27 |
118.12 |
96.32 |
6,182,0,29,211,33,57,268,91,16,290,107,14,304,123,9,313,133,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 183 RLASLDPLTGLKNRRRMERAVAERMGREQ----PFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGR 258
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 259 WGGDEFVVLL-DCGPEDVGRHLERVRQwvfgdyVVQDQGVPHRLPII--ASVGTAVWQ-GGESMAELFARADRDMYQEKN 334
smart00267 81 LGGDEFALLLpETSLEEAIALAERILQ------QLREPIIIHGIPLYltISIGVAAYPnPGEDAEDLLKRADTALYQAKK 154
|
...
gi 116623715 335 AVR 337
smart00267 155 AGR 157
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
2e-24 |
108.19 |
96.97 |
6,183,0,28,211,32,61,272,94,20,296,114,4,300,120,14,314,135,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 184 LASLDPLTGLKNRRRMERAVAERMGREQ----PFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRW 259
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 260 GGDEFVVLLDCGP-EDVGRHLERVRQWVFGDYVVqdqgVPHR--LPIIASVGTAVWQG-GESMAELFARADRDMYQEKNA 335
TIGR00254 81 GGEEFVVILPGTPlEDALSKAERLRDAINSKPIE----VAGSetLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKA 156
|
....
gi 116623715 336 VRQR 339
TIGR00254 157 GRNR 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 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
1e-29 |
125.80 |
46.39 |
10,139,239,13,153,252,5,158,259,14,172,275,6,178,285,32,210,321,58,268,380,20,288,401,15,305,416,3,308,420,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 140 DSLVLRARELQDRvDQMAR--DGQQMLAQMRGELR--HYQARL----EEAERLASLDPLTGLKNRRRMERAVAERMGRE- 210
PRK09581 240 DPRLVKALELGVN-DYLMRpiDKNELLARVRTQIRrkRYQDALrqnlEQSIEMAVTDGLTGLHNRRYFDMHLKQLIERAn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 211 ---QPFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWGGDEFVVLL-DCGPEDVGRHLERVRQWV 286
PRK09581 319 ergKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYGGEEFVVVMpDTDIEVAIAVAERIRRKI 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116623715 287 FG-DYVVQDQGVPHRLPIiaSVG-TAVWQGGESMAELFARADRDMYQEKNAVRQR 339
PRK09581 399 AEePFAISDGKERLNVTV--SIGvAELRPSGESIEALIKRADKALYEAKNTGRNR 451
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
6e-27 |
116.73 |
72.01 |
7,132,73,21,153,104,16,170,120,8,183,128,27,210,157,58,268,216,28,299,244,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 133 DDLGRIRDSLVLRARELQDRV----------DQMARDGQQMLAQMRGeLRHYQARLeeaerLASLDPLTGLKNRRRMERA 202
PRK09894 74 RLLDSAHQHMHNCARELLLAIaeghwqdadfDAFQEGLLSFTAALTD-YKIYLLTI-----RSNMDVLTGLPGRRVLDES 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 203 VAERMGRE--QPFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWGGDEFVVLL-DCGPEDVGRHL 279
PRK09894 148 FDHQLRNRepLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEEFIIILkAATDEEACRAG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 280 ERVRQWVFGDYVVQDQGvphRLPIIASVGTAVWQGGESMAELFARADRDMYQEKNAVRQR 339
PRK09894 228 ERIRQLIANQAITHSEG---RINITATFGVTRAFPEEPLDEVIGRADRAMYEGKQAGRNR 284
|
|
|
|
|
|
|
-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 |
1e-23 |
105.77 |
43.68 |
6,146,239,16,170,255,40,210,299,58,268,358,30,299,388,17,316,406,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 147 RELQDRVDQMARDGQQmlaqmrgeLRHYQARLEEAERLASLDPLTGLKNRRRMERAVAERMGRE----QPFSVVLLDLNG 222
COG3706 240 GELRARLRRQLRRKRY--------ERQLRESLERLQELALVDGLTGLFNRRYFDEHLADLWKRAlregRPLSLLMLDIDD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 223 FKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWGGDEFVVLL-DCGPEDVGRHLERVRQWVFGDYVVQDQGVPhRL 301
COG3706 312 FKEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVLpDTDLEAAIAIAERIRQKINELPFVHELSRE-PL 390
|
170 180 190
....*....|....*....|....*....|....*....
gi 116623715 302 PIIASVGTAVWQGGE-SMAELFARADRDMYQEKNAVRQR 339
COG3706 391 EVTISIGVAEGKPGEdSIEELLKRADKALYKAKASGRNR 429
|
|
|
|
|
|
|
-1 |
| 34606 |
COG5001 |
COG5001 |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms] |
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF... |
false |
true |
false |
663 |
3e-16 |
81.22 |
28.05 |
7,157,197,7,164,205,18,182,225,30,212,259,68,287,327,15,302,347,10,312,358,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 158 RDGQQML-AQMRGELRHYQARLEEAE--RLASLDPLTGLKNRRRMERAVAERMGREQP----FSVVLLDLNGFKQVNDSY 230
COG5001 198 REFSDMVqSQVTLTQRAEETRRLSDEndRLANLDSLTGLPNRRRFFAELDARLAAARQsgrrLVLGVIDLDGFKPVNDAF 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 231 GHAAGDDVLKQFATELRSAFRAADDVGRWGGDEFVVLLDCGPEDVGRHLErvrqwvfGDYVVQDQGVPHRLP-----IIA 305
COG5001 278 GHATGDRLLIEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAG-------ARALCESLQAPYDLRgvrvqVGA 350
|
170 180 190
....*....|....*....|....*....|...
gi 116623715 306 SVGTAVW-QGGESMAELFARADRDMYQEKNAVR 337
COG5001 351 SIGIAPFpSGADTSEQLFERADYALYHAKQNGK 383
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
2e-15 |
78.59 |
14.96 |
7,175,678,38,213,720,55,268,776,5,277,781,11,288,795,12,302,807,6,308,814,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 176 ARLEEAERLASLDPLTGLKNRRRMERAVAERMGREQPF----SVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFR 251
PRK09776 679 AMLRQLSYSASHDALTGLANRASFEKQLREALQTVNSThqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 252 AADDVGRWGGDEFVVLL-DCGPEdvgrHLERVRQWVFG---DYVVQDQGVPHRlpIIASVG-TAVWQGGESMAELFARAD 326
PRK09776 759 SSDVLARLGGDEFGLLLpDCNVE----SARFIATRIISainDYRFPWEGRVYR--VGASAGiTAIDDNNHQASEVMSQAD 832
|
170
....*....|...
gi 116623715 327 RDMYQEKNAVRQR 339
PRK09776 833 IACYAAKNAGRGR 845
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
2e-14 |
75.54 |
25.04 |
7,169,224,11,183,235,32,215,269,60,275,334,9,297,343,7,304,355,8,312,364,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 170 ELRHYQARLEEaerLASLDPLTGLKNRRRMERAVAERMGREQPFSV--VLLDLNGFKQVNDSYGHAAGDDVLKQFATELR 247
PRK10060 225 EERRAQERLRI---LANTDSITGLPNRNAIQELIDHAIAQADNNQVgiVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAIL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 248 SAFRAADDVGRWGGDEFVVLLDCGPEDV-----GRHLERVRQwvfgdyvvqdqgvPHRLPII-----ASVGTAVW-QGGE 316
PRK10060 302 SCLEEDQTLARLGGDEFLVLASHTSQAAleamaSRILTRLRL-------------PFRIGLIevytgCSIGIALSpEHGD 368
|
170 180
....*....|....*....|..
gi 116623715 317 SMAELFARADRDMYQEKNAVRQ 338
PRK10060 369 DSESLIRSADTAMYTAKEGGRG 390
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
2e-10 |
61.57 |
46.19 |
6,156,219,58,214,280,50,264,331,9,273,341,11,285,352,11,298,363,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 157 ARDGQQMLAQMRGELRHYQARLEEAERLASLDPLTGLKNRRRMERAVAERMGREQPFS---VVLLDLNGFKQVNDSYGHA 233
PRK09966 220 ALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKtsaLLFLDGDNFKYINDTWGHA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 234 AGDDVLKQFATELRSAFRAADDVGRWGGDEF-VVLLDCGPE-DVGRHLERVRQwVFGDYVVQDQGvpHRLPIIASVGTAV 311
PRK09966 300 TGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFaMVLYDVQSEsEVQQICSALTQ-IFNLPFDLHNG--HQTTMTLSIGYAM 376
|
170 180 190
....*....|....*....|....*....|.
gi 116623715 312 WQGGESMAELFARADRDMYQEKNAVRQREAK 342
PRK09966 377 TIEHASAEKLQELADHNMYQAKHQRAEKLVR 407
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-09 |
57.98 |
33.42 |
5,213,242,63,276,306,8,287,314,12,299,327,17,317,344,22 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 214 SVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWGGDEFVVLLDCGPEDVG-RHLERVRQwvfGDYVV 292
PRK10245 243 TLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAiTAMLRVHE---GLNTL 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 116623715 293 QDQGVPH-RLPIIASVGTAVWQGGEsMAELFARADRDMYQEKNAVRQR 339
PRK10245 320 RLPNAPQvTLRISVGVAPLNPQMSH-YREWLKSADLALYKAKKAGRNR 366
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
1e-08 |
56.00 |
15.39 |
2,181,372,84,265,457,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116623715 182 ERLASLDPLTGLKNRRRMERAVAERMGREQPFSVVLLDLNGFKQVNDSYGHAAGDDVLKQFATELRSAFRAADDVGRWGG 261
PRK11359 373 EQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 116623715 262 DEFV-VLLDCGPEDVGRHLERVRQWVFGDYVVQDQGVPHRLPI 303
PRK11359 453 TQFVlVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSI 495
|
|
|
|
|
|
|
-1 |
|