| 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 |
3e-37 |
151.20 |
98.73 |
3,194,0,104,298,114,21,319,136,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 195 YDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLARTGGD 274
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117928140 275 EFLLVLPSTTADQAAQVIERMRAA----------APDITFTAGIATWDGREPDYR-LVHRADAALYAAKAERRGT 338
cd01949 81 EFAILLPGTDLEEAEELAERLRKAieepffidgeEIRVTASIGIAEYPEDGEDLEeLLRRADKALYQAKRSGRNR 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-34 |
140.84 |
100.00 |
3,192,0,106,298,119,20,318,140,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 193 AWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLARTG 272
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 273 GDEFLLVLPSTTADQAAQVIERMRAA-------------APDITFTAGIATWDGREPDY-RLVHRADAALYAAKAERRGT 338
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 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
7e-33 |
136.22 |
97.55 |
3,191,1,107,298,118,20,318,139,21 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 192 QAWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLART 271
smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117928140 272 GGDEFLLVLPSTTADQAAQVIERMRAA----------APDITFTAGIATWDGREPDY-RLVHRADAALYAAKAERRGTT 339
smart00267 82 GGDEFALLLPETSLEEAIALAERILQQlrepiiihgiPLYLTISIGVAAYPNPGEDAeDLLKRADTALYQAKKAGRNQV 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-30 |
127.93 |
91.16 |
3,184,11,114,298,135,13,311,150,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 185 LIDRLSVQAWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRA 264
COG2199 12 AEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVARRLRSNLRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 265 GDLLARTGGDEFLLVLPSTTADQAAQVIERMRAA----------APDITFTAGIATW--DGREPDYRLVHRADAALYAAK 332
COG2199 92 GDLVARLGGDEFAVLLPGTSLEEAARLAERIRAAleepfflggeELRVTVSIGVALYpeDGSDDAELLLRRADLALYRAK 171
|
....*
gi 117928140 333 AERRG 337
COG2199 172 RAGRN 176
|
|
cl00291 |
140583 |
GGDEF |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as domain of unknown function 1 (DUF1). It is widely present in bacteria and often links to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain has been suggested to be homologous to the adenylyl cyclase catalytic domain. This prediction correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesiveness in bacteria. |
Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue... |
-1 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
4e-26 |
113.97 |
97.58 |
4,191,0,108,299,118,7,306,127,13,319,141,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 192 QAWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLART 271
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 272 GGDEFLLVLPSTTADQAAQVIERMRAAA----------PDITFTA--GIATWDGREPDYR-LVHRADAALYAAKAERRGT 338
TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAInskpievagsETLTVTVsiGVACYPGHGLTLEeLLKRADEALYQAKKAGRNR 160
|
.
gi 117928140 339 T 339
TIGR00254 161 V 161
|
|
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 |
| 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 |
6e-26 |
113.48 |
37.93 |
3,185,262,116,301,391,16,317,408,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 186 IDRLSVQAWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAG 265
COG3706 263 LERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 266 DLLARTGGDEFLLVLPSTTADQAAQVIERMRAAAPD-------------ITFTAGIATWDGREPD-YRLVHRADAALYAA 331
COG3706 343 DLVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINElpfvhelsrepleVTISIGVAEGKPGEDSiEELLKRADKALYKA 422
|
....*
gi 117928140 332 KAERR 336
COG3706 423 KASGR 427
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
9e-25 |
109.62 |
33.92 |
4,195,294,103,298,400,2,300,412,13,313,426,23 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 196 DALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLARTGGDE 275
PRK09581 295 DGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117928140 276 FLLVLPSTTADQAAQVIERMRAA---AP----------DITFTAGIATWDG-REPDYRLVHRADAALYAAKAERR 336
PRK09581 375 FVVVMPDTDIEVAIAVAERIRRKiaeEPfaisdgkerlNVTVSIGVAELRPsGESIEALIKRADKALYEAKNTGR 449
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
1e-22 |
102.48 |
50.17 |
3,194,131,23,219,154,82,301,247,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 195 YDALTGLPNRRLADFLLAAEMAAagRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLARTGGD 274
PRK09894 132 MDVLTGLPGRRVLDESFDHQLRN--REPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGE 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117928140 275 EFLLVLPSTTADQAAQVIERMRAAAPD-----------ITFTAGIATWDGREPDYRLVHRADAALYAAK 332
PRK09894 210 EFIIILKAATDEEACRAGERIRQLIANqaithsegrinITATFGVTRAFPEEPLDEVIGRADRAMYEGK 278
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
7e-21 |
96.31 |
14.43 |
3,188,683,116,309,799,9,318,825,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 189 LSVQAWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLL 268
PRK09776 684 LSYSASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 269 ARTGGDEFLLVLPSTTADQAAQVIERMRAAAPDITFtagiaTWDGREPDY-----------------RLVHRADAALYAA 331
PRK09776 764 ARLGGDEFGLLLPDCNVESARFIATRIISAINDYRF-----PWEGRVYRVgasagitaiddnnhqasEVMSQADIACYAA 838
|
....*.
gi 117928140 332 KAERRG 337
PRK09776 839 KNAGRG 844
|
|
|
|
|
|
|
-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-18 |
87.77 |
23.68 |
5,192,227,94,286,326,11,297,339,7,304,350,7,311,358,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 193 AWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLARTG 272
COG5001 228 ANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDGAPILAARLG 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117928140 273 GDEFLLVLPSTTAD-----QAAQVIERMRA--AAPDITF----TAGIATW-DGREPDYRLVHRADAALYAAKAERRG 337
COG5001 308 GDEFALIIPALEDDalrvaGARALCESLQApyDLRGVRVqvgaSIGIAPFpSGADTSEQLFERADYALYHAKQNGKG 384
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-17 |
84.56 |
45.01 |
5,187,204,101,288,309,9,297,322,7,304,331,15,319,347,24 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 188 RLSVQAWYDALTGLPNRRLADFLLAAEMAAAGRHGRPLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDL 267
PRK10245 205 RLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 268 LARTGGDEFLLVLPSTTADQA----AQVIERMRA----AAPDITF--TAGIATWDGREPDYR-LVHRADAALYAAKAERR 336
PRK10245 285 IGRFGGDEFAVIMSGTPAESAitamLRVHEGLNTlrlpNAPQVTLriSVGVAPLNPQMSHYReWLKSADLALYKAKKAGR 364
|
....*..
gi 117928140 337 GTTGIAS 343
PRK10245 365 NRTEVAA 371
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
2e-15 |
78.23 |
24.28 |
7,186,230,36,224,266,63,287,333,9,301,342,3,304,356,7,311,367,4,318,371,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 187 DRLSVQAWYDALTGLPNRRLADFLLAAEMAAAGRHGrpLTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGD 266
PRK10060 231 ERLRILANTDSITGLPNRNAIQELIDHAIAQADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 267 LLARTGGDEFLLVLPSTTADQ----AAQVIERMRaaapdITF-----------TAGIATW----DGREpdyRLVHRADAA 327
PRK10060 309 TLARLGGDEFLVLASHTSQAAleamASRILTRLR-----LPFriglievytgcSIGIALSpehgDDSE---SLIRSADTA 380
|
170
....*....|.
gi 117928140 328 LYAAKAERRGT 338
PRK10060 381 MYTAKEGGRGQ 391
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
6e-12 |
66.79 |
18.02 |
7,185,371,4,190,375,2,194,377,21,218,398,11,230,409,66,296,477,4,300,489,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 186 IDRLsVQawYDALTGLPNRRLADFLLAAEMaaaGRHGRPLTIAVcDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAG 265
PRK11359 372 IEQL-IQ--FDPMTGLPNRNNLHNYLDDLV---DKAVSPVVYLI-GVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPD 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117928140 266 DLLARTGGDEFLLVLPSTTADQAAQVIERMR--AAAP--------DITFTAGIATWDGREPDYRLVHRADA 326
PRK11359 445 QYLCRIEGTQFVLVSLENDVSNITQIADELRnvVSKPimiddkpfPLTLSIGISYDVGKNRDYLLSTAHNA 515
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
7e-05 |
43.47 |
37.84 |
5,192,247,32,225,279,67,292,358,17,309,376,8,318,384,17 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 193 AWYDALTGLPNRRLADFLLAAEMAAAGRHGRPlTIAVCDLDELKRINDTRGHRAGDQLLARAGRTWAATLRAGDLLARTG 272
PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117928140 273 GDEFLLVLPSTTADQAAQVI------------ERMRAAAPDITFTAGIA-TWDGREPDyRLVHRADAALYAAKAER 335
PRK09966 327 GDEFAMVLYDVQSESEVQQIcsaltqifnlpfDLHNGHQTTMTLSIGYAmTIEHASAE-KLQELADHNMYQAKHQR 401
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
9e-04 |
39.87 |
23.68 |
7,191,226,13,204,242,31,238,273,25,263,300,21,284,324,3,287,328,13,300,347,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117928140 192 QAWYDALTGLPNR---RLADFLLAAEMAAAGRHGRPLTIAVCDLDELkriNDTRGHRAGDQLLARAGRTWAATLR--AGD 266
PRK11059 227 NAFLDAKTGLGNRlffDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLL---QEELGESQVDELLFELINLLSTFVQryPGA 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117928140 267 LLARTGGDEFLLVLPSTT---ADQ-AAQVIERMRAAAP------DITFTAGIATWDGREPDYRLVHRADAALYAA 331
PRK11059 304 LLARYSRSDFAVLLPHRSlkeADSlASQLLKAVDSLPPpkmldrDDFLHIGIAAYRSGQSTEQVMEEAEMALRSA 378
|
|
|
|
|
|
|
-1 |
|