| 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 |
7e-30 |
128.09 |
64.97 |
1,349,0,102 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 350 TDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYGGE 429
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100
....*....|....*....|..
gi 111225771 430 EFALLALDVRGDALADIAERLR 451
cd01949 81 EFAILLPGTDLEEAEELAERLR 102
|
|
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 |
7e-28 |
121.20 |
65.00 |
1,347,0,104 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 348 AITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYG 427
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100
....*....|....*....|....
gi 111225771 428 GEEFALLALDVRGDALADIAERLR 451
pfam00990 81 GDEFAILLPDTSLEGAQELAERIR 104
|
|
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 |
5e-27 |
118.50 |
66.87 |
1,345,0,109 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 346 RVAITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVAR 425
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100
....*....|....*....|....*....
gi 111225771 426 YGGEEFALLALDVRGDALADIAERLRLGV 454
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQL 109
|
|
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-25 |
112.91 |
68.51 |
1,335,7,124 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 336 RMARLEADQRRVAITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLD 415
COG2199 8 RLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVARRLRS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 111225771 416 VTRPGDVVARYGGEEFALLALDVRGDALADIAERLRLGVGREPV 459
COG2199 88 NLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALEEPFF 131
|
|
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 |
6e-23 |
105.11 |
69.70 |
3,347,1,91,438,93,6,445,99,17 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 348 AITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYG 427
TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 111225771 428 GEEFALLALDV-RGDALAdIAERLRLGVGREPVRVA 462
TIGR00254 82 GEEFVVILPGTpLEDALS-KAERLRDAINSKPIEVA 116
|
|
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 |
| 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 |
4e-04 |
42.57 |
21.02 |
1,550,124,33 |
10 20 30
....*....|....*....|....*....|...
gi 111225771 551 AVLPDHAGDVYALVAVADQALYAAKEAGRDRVA 583
cd01949 125 AEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
0.003 |
39.54 |
20.86 |
1,550,128,34 |
10 20 30
....*....|....*....|....*....|....
gi 111225771 551 AVLPDHAGDVYALVAVADQALYAAKEAGRDRVAI 584
smart00267 129 AAYPNPGEDAEDLLKRADTALYQAKKAGRNQVAV 162
|
|
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 |
8e-25 |
111.16 |
25.16 |
1,347,291,115 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 348 AITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYG 427
PRK09581 292 AVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARYG 371
|
90 100 110
....*....|....*....|....*....|....*
gi 111225771 428 GEEFALLALDVRGDALADIAERLRLGVGREPVRVA 462
PRK09581 372 GEEFVVVMPDTDIEVAIAVAERIRRKIAEEPFAIS 406
|
|
|
|
|
|
|
-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 |
8e-25 |
111.17 |
26.44 |
1,344,266,115 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 345 RRVAITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVA 424
COG3706 267 QELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLDLVA 346
|
90 100 110
....*....|....*....|....*....|....*
gi 111225771 425 RYGGEEFALLALDVRGDALADIAERLRLGVGREPV 459
COG3706 347 RYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPF 381
|
|
|
|
|
|
|
-1 |
| 32388 |
COG2206 |
COG2206 |
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms] |
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms] |
true |
true |
false |
344 |
1e-17 |
87.12 |
35.76 |
2,790,185,42,832,228,80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 791 VGKILLPPHVLARPGPLDAEEWRLIRLHPVMGATLLAQVPDL-RVEAEIIAQQREWFGGGGYPSGIAGSRIRMESRALAV 869
COG2206 186 IGKIGIPDSILNKPGKLTEEEFEIIKKHPIYGYDILKDLPEFlESVRAVALRHHERWDGTGYPRGLKGEEIPLEARIIAV 265
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 111225771 870 CTAWAAMRGGRGGRDPLSGPAAREQLRAGRATQFDPTVVDVFL 912
COG2206 266 ADVYDALTSDRPYKKAKSPEEALEELRKNSGGKFDPKVVDAFL 308
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
8e-17 |
84.76 |
36.52 |
2,350,132,25,377,157,82 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 351 DGLTGLRTRRYLEAEMRVAARRARQigSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYGGEE 430
PRK09894 133 DVLTGLPGRRVLDESFDHQLRNREP--LNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEE 210
|
90 100
....*....|....*....|....*....
gi 111225771 431 FALLALDVRGDALADIAERLRLGVGREPV 459
PRK09894 211 FIIILKAATDEEACRAGERIRQLIANQAI 239
|
|
|
|
|
|
|
-1 |
| 33243 |
COG3437 |
COG3437 |
Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription / Signal transduction mechanisms] |
Response regulator containing a CheY-like receiver domain and an HD-GYP domain [... |
false |
true |
false |
360 |
1e-14 |
77.26 |
35.56 |
2,789,221,40,829,262,87 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 790 NVGKILLPPHVLARPGPLDAEEWRLIRLHPVMGATLLAQV-PDLRVEAEIIAQQREWFGGGGYPSGIAGSRIRMESRALA 868
COG3437 222 DIGKVAIPDSILLKPGKLTSEEFEIMKGHPILGAEILKSSeRLMQVAAEIARHHHERWDGSGYPDGLKGDEIPLSARIVA 301
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 111225771 869 VCTAWAAMRGGRGGRDPLSGPAAREQLRAGRATQFDPTVVDVFLALEA 916
COG3437 302 IADVFDALVSGRPYKEAMSTEEALEIIRAQSGRLFDPKLVEAFIQVED 349
|
|
|
|
|
|
|
-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 |
2e-14 |
76.99 |
15.84 |
1,338,218,105 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 339 RLEADQRRVAITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTR 418
COG5001 219 RLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRLKAFDG 298
|
90 100
....*....|....*....|....*
gi 111225771 419 PGDVVARYGGEEFALLALDVRGDAL 443
COG5001 299 APILAARLGGDEFALIIPALEDDAL 323
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
1e-13 |
73.97 |
9.23 |
1,347,687,103 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 348 AITDGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYG 427
PRK09776 688 ASHDALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 767
|
90 100
....*....|....*....|...
gi 111225771 428 GEEFALLALDVRGDALADIAERL 450
PRK09776 768 GDEFGLLLPDCNVESARFIATRI 790
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
5e-13 |
72.07 |
17.50 |
4,344,233,30,376,263,74,450,339,2,455,341,8 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 345 RRVAITDGLTGLRTRRYLEAEMRVAARRARqiGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVA 424
PRK10060 234 RILANTDSITGLPNRNAIQELIDHAIAQAD--NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLA 311
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 111225771 425 RYGGEEFALLALDVRGDALADIAERL--RLgvgREPVRVAL 463
PRK10060 312 RLGGDEFLVLASHTSQAALEAMASRIltRL---RLPFRIGL 349
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
3e-12 |
69.15 |
32.08 |
3,338,197,12,350,212,91,441,307,9 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 339 RLEADQRRVAIT---DGLTGLRTRRYLEAEMRVAARRARQIGSGMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLD 415
PRK10245 198 KLAEHKRRLQVMstrDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 277
|
90 100 110
....*....|....*....|....*....|....*....
gi 111225771 416 VTRPGDVVARYGGEEFALLALDVRGD----ALADIAERL 450
PRK10245 278 TLRGSDVIGRFGGDEFAVIMSGTPAEsaitAMLRVHEGL 316
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
8e-11 |
64.48 |
12.89 |
2,350,378,25,379,403,78 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 351 DGLTGLRTRRYLEAEMRVAARRARQigsgMGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLDVTRPGDVVARYGGEE 430
PRK11359 379 DPMTGLPNRNNLHNYLDDLVDKAVS----PVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
|
90 100
....*....|....*....|....*..
gi 111225771 431 FALLALDVRGDALADIAERLRLGVGRE 457
PRK11359 455 FVLVSLENDVSNITQIADELRNVVSKP 481
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
2e-09 |
60.03 |
25.80 |
2,335,235,44,380,279,61 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225771 336 RMARLEADQRRVAITDGLTGLRTRRYLEAEMRVAARRARQIGSGmGLLLVDVDHFKSVNDRFGHPTGDQVLAEVARRLLD 415
PRK09966 236 RLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAE 314
|
90 100
....*....|....*....|....*.
gi 111225771 416 VTRPGDVVARYGGEEFALLALDVRGD 441
PRK09966 315 FGGLRHKAYRLGGDEFAMVLYDVQSE 340
|
|
|
|
|
|
|
-1 |