| 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 |
9e-57 |
216.69 |
100.00 |
2,510,0,114,625,114,43 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 511 TDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARYGGE 590
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGGD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927375 591 EFVVILPETDADGAAHTAERLRQAVRGTPFHVEQmDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGRDAWR 668
cd01949 81 EFAILLPGTDLEEAEELAERLRKAIEEPFFIDGE-EIRVTASIGIAEYPEDGEDLEELLRRADKALYQAKRSGRNRVV 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... |
0 |
| 100122 |
cd06225 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
true |
false |
true |
48 |
2e-09 |
59.96 |
100.00 |
1,283,0,48 |
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 117927375 284 ISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRR 331
cd06225 1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
|
|
cl01054 |
141075 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
2 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
5e-49 |
191.30 |
99.38 |
2,508,0,108,616,110,49 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 509 SLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARYG 588
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSPLALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117927375 589 GEEFVVILPETDADGAAHTAERLRQAVR--GTPFHVEQMDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGRD 665
pfam00990 81 GDEFAILLPDTSLEGAQELAERIRRLLAalKIPHTLSGLPLYVTISIGIAAYPNDGEDAEDLLKRADQALYQAKNQGRN 159
|
|
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-48 |
189.38 |
100.00 |
2,506,0,110,617,110,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 507 RLSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVAR 586
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 587 YGGEEFVVILPETDADGAAHTAERLRQAVRgTPFHVEQMDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGRDA 666
smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 117927375 667 WRFA 670
smart00267 160 VAVY 163
|
|
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-46 |
181.38 |
100.00 |
2,507,0,119,626,120,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 508 LSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARY 587
TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 588 GGEEFVVILPETDADGAAHTAERLRQAVRGTPFHVEQMD-IPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGRDA 666
TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 117927375 667 WRFAR 671
TIGR00254 161 VVVAD 165
|
|
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 |
7e-44 |
174.15 |
98.90 |
3,491,2,125,617,127,26,643,154,27 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 492 ASVAIENVLLHQEAERLSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELA 571
COG2199 3 LRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 572 RRLHTTVREVDTVARYGGEEFVVILPETDADGAAHTAERLRQAVRgTPFHVEQMDIPVTASIGIAVFPRHGS-SAAILLR 650
COG2199 83 RRLRSNLREGDLVARLGGDEFAVLLPGTSLEEAARLAERIRAALE-EPFFLGGEELRVTVSIGVALYPEDGSdDAELLLR 161
|
170 180
....*....|....*....|
gi 117927375 651 AADEALYVAKHSGRDAWRFA 670
COG2199 162 RADLALYRAKRAGRNRVVVF 181
|
|
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 |
| 128599 |
smart00304 |
HAMP |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain |
false |
false |
false |
53 |
6e-10 |
61.50 |
100.00 |
1,281,0,53 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117927375 282 RLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRRYIG 334
smart00304 1 RRILRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
|
|
cl01054 |
141075 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
| 128379 |
smart00065 |
GAF |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
Domain present in phytochromes and cGMP-specific phosphodiesterases. |
true |
false |
false |
149 |
1e-09 |
60.47 |
98.66 |
5,358,0,35,393,37,33,428,70,6,434,81,33,471,114,33 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 359 NLPGILAVIVDTAMASVRASAGLVALFESDGVLHV--KVSRGLPELAPDAVVPLGAGIIGRVAERGTPVHgvVGDGPG-- 434
smart00065 1 DLEELLQTILEELRQLLGADRVLIYLVDEDDRGELvlVAADGLTLPLLGLRYPLGEGLAGRVAETGRPLN--IPDVEAdp 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117927375 435 ---LRPIPEEPRRRTVLAVPLRQAGRISGVLAVYDQeetgDGGAAFTENDVRTLGTFAGQASVAIENVLLHQE 504
smart00065 79 vfaLDLLGRYQGVRSFLAVPLVADGELVGVLALHNK----DSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 109717 |
pfam00672 |
HAMP |
HAMP domain |
HAMP domain |
false |
false |
false |
70 |
1e-09 |
60.32 |
77.14 |
1,277,16,54 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRR 331
pfam00672 17 WLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
|
|
cl01054 |
141075 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
| 32385 |
COG2203 |
FhlA |
FOG: GAF domain [Signal transduction mechanisms] |
FOG: GAF domain [Signal transduction mechanisms] |
false |
false |
false |
175 |
3e-06 |
49.24 |
96.00 |
6,346,5,49,395,59,12,407,73,18,427,91,4,431,101,41,476,142,31 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 347 LERLGAALAQTHNLPGILAVIVDTAMASVRASAGLVALFESDGVLHVKV-----SRGLPELAPDAV--VPLGAGIIGRVA 419
COG2203 6 LNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGLLDGALvaeaaEAGLEQLIDELFglVILPACLIGIAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 420 ERGTPVhgVVGD------GPGLRPIPEEPRRRTVLAVPLRQAGRISGVLAVYDQEETGDggaaFTENDVRTLGTFAGQAS 493
COG2203 86 REGRPV--VVEDilqdprFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRQ----WSEEELELLEELAEQVA 159
|
170
....*....|....
gi 117927375 494 VAIENVLLHQEAER 507
COG2203 160 IAIERARLYEELQE 173
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 32631 |
COG2770 |
ResE |
FOG: HAMP domain [Signal transduction mechanisms] |
FOG: HAMP domain [Signal transduction mechanisms] |
false |
false |
false |
83 |
7e-06 |
47.71 |
72.29 |
1,277,23,60 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRRYIGQLE 337
COG2770 24 LAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALSALE 83
|
|
cl01054 |
141075 |
HAMP |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established. |
Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain... |
-1 |
| 110584 |
pfam01590 |
GAF |
GAF domain |
GAF domain |
false |
false |
false |
153 |
3e-04 |
42.62 |
100.00 |
5,358,0,39,397,40,10,407,51,18,425,87,45,475,132,21 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 359 NLPGILAVIVDTAMASVRASAGLVALFESDGVLHVKVSR-GLPELAPDAV-VPLGAGIIGRVAERGTPV----------- 425
pfam01590 1 DLEELLQTILEELRELLGADRCAILLADADGLLLYLVAGdGLSDIPLAARgLPLGGGVVGEVIAGGNPIvvpdvqddprf 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117927375 426 -------HGVVGDGPGLRPIPEEPRRRTVLAVPLRQAGRISGVLAVYDQEETgdggaAFTENDVRTLGTFAGQASVAI 496
pfam01590 81 rdltalaEELPAPVGCHEHYLRGLGIRSCLAVPLLGGGKLIGVLVLHSTSPR-----AFTEEELELLQALADQVAIAL 153
|
|
cl00853 |
140972 |
GAF |
GAF domain |
GAF domain |
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
4e-51 |
198.22 |
34.79 |
2,507,290,119,626,411,38 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 508 LSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARY 587
PRK09581 291 MAVTDGLTGLHNRRYFDMHLKQLIERANERGKPLSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDLIARY 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117927375 588 GGEEFVVILPETDADGAAHTAERLRQAVRGTPFHVEQMD--IPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGR 664
PRK09581 371 GGEEFVVVMPDTDIEVAIAVAERIRRKIAEEPFAISDGKerLNVTVSIGVAELRPSGESIEALIKRADKALYEAKNTGR 449
|
|
|
|
|
|
|
-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 |
9e-46 |
180.50 |
39.54 |
2,502,263,126,628,391,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 503 QEAERLSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVD 582
COG3706 264 ERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTVRGLD 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 583 TVARYGGEEFVVILPETDADGAAHTAERLRQAVRGTPFHVEQMDIP--VTASIGIAVFPRHGSSAAILLRAADEALYVAK 660
COG3706 344 LVARYGGEEFAVVLPDTDLEAAIAIAERIRQKINELPFVHELSREPleVTISIGVAEGKPGEDSIEELLKRADKALYKAK 423
|
170
....*....|..
gi 117927375 661 HSGRDAWRFARA 672
COG3706 424 ASGRNRVVVKRA 435
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
9e-31 |
130.60 |
51.54 |
3,511,132,19,532,151,106,639,257,26 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 512 DALTGLWNYRYLTMTLGHEieRATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARYGGEE 591
PRK09894 133 DVLTGLPGRRVLDESFDHQ--LRNREPLNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRPYETVYRYGGEE 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117927375 592 FVVILPETDADGAAHTAERLRQAVRGTPFHVEQMDIPVTASIGIAVFpRHGSSAAILLRAADEALYVAKHSGRD 665
PRK09894 211 FIIILKAATDEEACRAGERIRQLIANQAITHSEGRINITATFGVTRA-FPEEPLDEVIGRADRAMYEGKQAGRN 283
|
|
|
|
|
|
|
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
2e-25 |
112.90 |
24.59 |
4,505,230,5,510,238,21,533,259,83,617,342,51 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 506 ERLSL---TDALTGLWNYRYLTMTLGHEIerATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVD 582
PRK10060 231 ERLRIlanTDSITGLPNRNAIQELIDHAI--AQADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 583 TVARYGGEEFVVILPETDADGAAHTAERLRQAVRgTPFHVEQMDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHS 662
PRK10060 309 TLARLGGDEFLVLASHTSQAALEAMASRILTRLR-LPFRIGLIEVYTGCSIGIALSPEHGDDSESLIRSADTAMYTAKEG 387
|
....*.
gi 117927375 663 GRDAWR 668
PRK10060 388 GRGQFC 393
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
2e-25 |
112.49 |
13.71 |
1,511,690,153 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 512 DALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARYGGEE 591
PRK09776 691 DALTGLANRASFEKQLREALQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 770
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117927375 592 FVVILPETDADGAAHTAERLRQAVRGTPFHVEQMDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGR 664
PRK09776 771 FGLLLPDCNVESARFIATRIISAINDYRFPWEGRVYRVGASAGITAIDDNNHQASEVMSQADIACYAAKNAGR 843
|
|
|
|
|
|
|
-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 |
8e-25 |
110.89 |
27.45 |
4,494,213,103,597,318,8,606,326,11,618,337,58 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 495 AIENVLLHQEAERLSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRL 574
COG5001 214 AEETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHATGDRLLIEVGRRL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 575 HTTVREVDTVARYGGEEFVVILP--ETDADGAAhTAERLRQAVRGtPFHVEQMDIPVTASIGIAVFPRHGSSAAILLRAA 652
COG5001 294 KAFDGAPILAARLGGDEFALIIPalEDDALRVA-GARALCESLQA-PYDLRGVRVQVGASIGIAPFPSGADTSEQLFERA 371
|
170 180
....*....|....*....|....
gi 117927375 653 DEALYVAKHSGRDAWRFARAGGET 676
COG5001 372 DYALYHAKQNGKGAAVLFDARHEA 395
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
2e-21 |
99.59 |
42.86 |
3,505,206,111,616,322,3,625,325,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 506 ERLSLTDALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVA 585
PRK10245 207 QVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 586 RYGGEEFVVILPETDADGAAHTAERLRQAVR-----GTPfhveqmDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAK 660
PRK10245 287 RFGGDEFAVIMSGTPAESAITAMLRVHEGLNtlrlpNAP------QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAK 360
|
....*
gi 117927375 661 HSGRD 665
PRK10245 361 KAGRN 365
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
5e-21 |
97.99 |
27.53 |
8,438,309,17,455,327,12,469,339,10,482,349,37,519,390,18,545,408,66,612,474,25,639,499,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 439 PEEPRRRTVLAVPLRQA-GRISGVLAVYDQeeTGDGGAAFTEndvRTLGTFAGQASVAIENVLLHQEAERLSLTDALTGL 517
PRK11359 310 GAEVQNAQSWSATIRQRdGAPAGILQIKTS--SGAETSAFIE---RVADISQHMAALALEQEKSRQHIEQLIQFDPMTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 518 WN----YRYLTMTLGHEIERATRFrrplallmIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVARYGGEEFV 593
PRK11359 385 PNrnnlHNYLDDLVDKAVSPVVYL--------IGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927375 594 VILPETDADGAAHTAERLrQAVRGTPFHVEQMDIPVTASIGIAVfpRHGSSAAILLRAADEALYVAKHSGRDAWRF 669
PRK11359 457 LVSLENDVSNITQIADEL-RNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNGWQF 529
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
3e-12 |
69.28 |
37.84 |
4,506,245,13,520,258,104,624,363,17,642,380,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 507 RLSLTDALTGLWNyRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVAR 586
PRK09966 246 RTALHDPLTGLAN-RAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYR 324
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927375 587 YGGEEFVVILPETDADGAAHTAERLRQAVRGTPFHVEQ-MDIPVTASIGIAVFPRHgSSAAILLRAADEALYVAKH 661
PRK09966 325 LGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNgHQTTMTLSIGYAMTIEH-ASAEKLQELADHNMYQAKH 399
|
|
|
|
|
|
|
-1 |
| 34605 |
COG5000 |
NtrY |
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms] |
Signal transduction histidine kinase involved in nitrogen fixation and metabolism... |
false |
true |
false |
712 |
3e-11 |
65.75 |
10.81 |
2,279,300,35,314,336,41 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117927375 280 LARLISQPVAELSEAASRVAGGDLDITLPVRSRDE-VGRLAAAFNHMTAELRRYIGQLERSHAELRENLERLGAALA 355
COG5000 301 FARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQEALERAKDALEQRRRFLEAVLS 377
|
|
|
|
|
|
|
-1 |
| 31182 |
COG0840 |
Tar |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms] |
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction... |
false |
true |
false |
408 |
2e-08 |
56.15 |
24.02 |
1,277,77,98 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRRYIGQLERSHAELRENLERLGAALAQT 357
COG0840 78 ILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATEL 157
|
90
....*....|....*...
gi 117927375 358 HNLPGILAVIVDTAMASV 375
COG0840 158 SARADQQAESLEEVASAI 175
|
|
|
|
|
|
|
-1 |
| 33640 |
COG3850 |
NarQ |
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] |
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction... |
false |
true |
false |
574 |
1e-07 |
53.36 |
35.02 |
7,277,168,52,336,220,23,362,243,9,372,252,14,388,266,7,405,273,59,473,332,37 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELrryigqlERSHAELRENLERLGAALAQT 357
COG3850 169 YWLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGEL-------KKLYADLEQRVEEKTRDLEQK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 358 HNlpgILAVIVDTAmASVRASAGLVALFEsdGVLHVKVsrglpelapdAVVPLGAGIIGRVAERGTPVHGVVGDGPGLRP 437
COG3850 242 NQ---RLSFLYQSS-RRLHTSQIDDERLR--HVLNRLQ----------NLTGLAAVRLELYGGDDERNHQEHAEQWDISE 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117927375 438 IPEEPRRRTVLAVPLRQAGRISGVLAVydqeetgdgGAAFTENDVRTLGTFAGQASVAIENVLLHQEAERLSL 510
COG3850 306 GDQPSGLKWPQEDPLTQQGHLLGTLPW---------QRSLPEDDQQLLDTLVQQLGRTLALNKQQEQQQQLLL 369
|
|
|
|
|
|
|
-1 |
| 138290 |
PRK10935 |
PRK10935 |
nitrate/nitrite sensor protein NarQ; Provisional |
nitrate/nitrite sensor protein NarQ; Provisional |
false |
true |
false |
568 |
5e-07 |
51.42 |
11.44 |
1,277,169,65 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRRYIGQLERSHAE 342
PRK10935 170 RFTRRQVVAPLNQLVTASQQIQKGQFDIPLDTTLPNELGLLAKAFNQMASELHKLYRSLESQVEE 234
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
2e-05 |
46.62 |
21.70 |
2,506,297,33,540,330,125 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 507 RLSLTDALTGLWNYRYLTMTLGHEIERATRFRRpLALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREVDTVAR 586
PRK11829 298 RISHRFPVTELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQ 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117927375 587 YGGEEFVVILPETDADGAAHTAERLRQAVRGTPFHVEQMDIPVTASIGIAVFPRHGSSAAILLRAADEALYVAKHSGRD 665
PRK11829 377 LSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRN 455
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
2e-05 |
46.03 |
29.28 |
10,491,198,10,501,213,7,508,225,3,511,230,67,578,298,6,584,305,13,597,321,8,607,329,22,631,351,7,639,358,28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 492 ASVAIENVLL-----HQEAERL-----SLT--DALTGLWNYRYLTMTLGHEIERATRFRRPLALLMIDLDRFKDINDRHG 559
PRK11059 199 ASRALDHLLEelqdaRKERSRFdtfirSNAflDAKTGLGNRLFFDNQLDTLLEDQEKVGAHGVVMLIRLPDFDLLQEELG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 560 HQAGDAVLVELARRLHTTV-REVDTV-ARYGGEEFVVILP---ETDADGAAhtAERLRQAVRGTPFHVEQMDIPVtaSIG 634
PRK11059 279 ESQVDELLFELINLLSTFVqRYPGALlARYSRSDFAVLLPhrsLKEADSLA--SQLLKAVDSLPPPKMLDRDDFL--HIG 354
|
170 180 190
....*....|....*....|....*....|...
gi 117927375 635 IAVFpRHGSSAAILLRAADEALYVAKHSGRDAW 667
PRK11059 355 IAAY-RSGQSTEQVMEEAEMALRSAQLQGGNSW 386
|
|
|
|
|
|
|
-1 |
| 132001 |
TIGR02956 |
TMAO_torS |
TMAO reductase sytem sensor TorS |
TMAO reductase sytem sensor TorS |
false |
true |
false |
968 |
8e-05 |
44.38 |
8.16 |
3,277,349,42,319,394,24,343,421,7 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLA---AAFNHMTAELRRYIGQLERSHAEL---RENLERL 350
TIGR02956 350 RVVYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGraiEAFRDTAAHNLKLQADERQVAQELqehKESLEQL 428
|
|
|
|
|
|
|
-1 |
| 137977 |
PRK10549 |
PRK10549 |
signal transduction histidine-protein kinase BaeS; Provisional |
signal transduction histidine-protein kinase BaeS; Provisional |
false |
true |
false |
467 |
3e-04 |
42.40 |
11.13 |
1,279,184,52 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 117927375 280 LARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRR 331
PRK10549 185 LARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLEK 236
|
|
|
|
|
|
|
-1 |
| 34607 |
COG5002 |
VicK |
Signal transduction histidine kinase [Signal transduction mechanisms] |
Signal transduction histidine kinase [Signal transduction mechanisms] |
false |
true |
false |
459 |
3e-04 |
42.62 |
16.99 |
3,278,48,52,337,100,18,357,118,8 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 279 FLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRryigqleRSHAELRENLERLGAALAqtH 358
COG5002 49 LLARTITKPITDMRKQAVDMARGNYSRKVKVYGTDEIGELADSFNDLTKRVQ-------EAQANTEQERRKLDSVLA--Y 119
|
....*..
gi 117927375 359 NLPGILA 365
COG5002 120 MTDGVIA 126
|
|
|
|
|
|
|
-1 |
| 33404 |
COG3604 |
FhlA |
Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains [Transcription / Signal transduction mechanisms] |
Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains [... |
false |
true |
false |
550 |
3e-04 |
42.22 |
32.36 |
7,337,23,15,352,41,37,390,78,9,399,90,34,433,130,31,465,161,6,475,167,34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 338 RSHAELRENLERLGA---ALAQTHNLPGILAVIVDTAMASVRASAGLVALFESDGvLHVKVSRGL---PELAPDAVVPLG 411
COG3604 24 RVSLELLADIRILVEltnALLSPLRLERLLAEVAKELHSLFGCDASALLRLDSKN-LIPLATDGLskdHLGREQRFVVEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 412 AGIIGRVAERGTPVHGVVGDGP------GLRPIPEEPRRRTVLAVPLRQAGRISGVLAVyDQEETGdggaAFTENDVRTL 485
COG3604 103 HPLLEQILKAGRPLVFHPADSLfpdpydGLLPDTEGNKKHACIGVPLKSGDKLIGALTL-DHTEPD----QFDEDLDEEL 177
|
170 180
....*....|....*....|....
gi 117927375 486 GTFAGQASVAIENVLLHQEAERLS 509
COG3604 178 RFLAALAALAVANALLHRELSSLK 201
|
|
|
|
|
|
|
-1 |
| 137312 |
PRK09470 |
cpxA |
two-component sensor protein; Provisional |
two-component sensor protein; Provisional |
false |
true |
false |
461 |
4e-04 |
41.89 |
17.57 |
6,279,185,26,305,216,7,313,223,3,319,226,19,338,250,2,341,252,14 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 280 LARLISQPVAELSEAASRVAGGDLDI-----TLPVRSRdEVGrlaAAFNHMTAELRRYIGQLER-----SHaELRENLER 349
PRK09470 186 LAWSLAKPARKLKNAADEVAQGNFRQhpeleAGPQEFR-AAG---ASFNQMVTALERMMSSQQRllsdiSH-ELRTPLTR 260
|
....*.
gi 117927375 350 LGAALA 355
PRK09470 261 LQLATA 266
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
0.001 |
40.14 |
25.04 |
3,501,223,36,541,259,97,639,356,30 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 502 HQEAERLSLTDALTGLWNYRYLTMTLGHEIERATRFrrplALLMIDLDRFKDINDRHGHQAGDAVLVELARRLHTTVREV 581
PRK13561 224 YEEQNENAMRFPVSDLPNKALLMALLEQVVARKQTT----ALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 582 DTVARYGGEEFVVILPETDADGAAHTAERLRQAVRGTPFHVEQMDIPVTASIGIAVFpRHGSSAAILLRAADEALYVAKH 661
PRK13561 300 MVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAVSAAFTARR 378
|
....*...
gi 117927375 662 SGRDAWRF 669
PRK13561 379 KGKNQIQF 386
|
|
|
|
|
|
|
-1 |
| 33405 |
COG3605 |
PtsP |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms] |
Signal transduction protein containing GAF and PtsI domains [Signal transduction... |
false |
true |
false |
756 |
0.002 |
39.90 |
22.35 |
6,346,4,43,389,48,18,407,67,19,426,87,14,440,103,30,475,133,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 347 LERLGAALAQTHNLPGILAVIVDTAMASVRASAGLVALFESDG-VLHVKVSRGLPELAPDAV-VPLGAGIIGRVAERGTP 424
COG3605 5 LRRIVEKVASALELQEALDIIVRDIALAMVTEVCSVYLLRADRrVLELMATEGLNKPAVHLVqLAFGEGLVGLVGRSAEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 425 VH-GVVGDGPGLRPIPE--EPRRRTVLAVPLRQAGRISGVLAVYDQEETgdggaAFTENDVRTLGTFAGQASVAIENVLL 501
COG3605 85 LNlADAQSHPSFKYLPEtgEERYHSFLGVPIIRRGRLLGVLVVQQRELR-----QYDEDEVEFLVTLAMQLAEIVAQSQL 159
|
170
....*....|....
gi 117927375 502 HQEAERLSLTDALT 515
COG3605 160 TGATRGGYRELDLI 173
|
|
|
|
|
|
|
-1 |
| 138019 |
PRK10600 |
PRK10600 |
nitrate/nitrite sensor protein NarX; Provisional |
nitrate/nitrite sensor protein NarX; Provisional |
false |
true |
false |
569 |
0.004 |
38.94 |
12.30 |
1,278,143,70 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117927375 279 FLARLISQPVAELSEAASRVAGGDLDITLPVRSRDEVGRLAAAFNHMTAELRRYIGQLERSHAELRENLE 348
PRK10600 144 WLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLE 213
|
|
|
|
|
|
|
-1 |
| 138589 |
PRK11466 |
PRK11466 |
hybrid sensory histidine kinase TorS; Provisional |
hybrid sensory histidine kinase TorS; Provisional |
false |
true |
false |
912 |
0.007 |
37.70 |
8.33 |
3,277,349,31,308,384,24,332,412,13 |
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117927375 278 RFLARLISQPVAELSEAASRVAGGDLDITLP----VRSRDEVGRLAAAFNHMTAELRRY----IGQLERSHAELRE 345
PRK11466 350 RVVYRSVTRPLAEQTQALQRLLDGDIDSPFPetagVRELDTIGRLMDAFRSNVHALNRHreqlAAQVKARTAELQE 425
|
|
|
|
|
|
|
-1 |
|