| 30163 |
cd01948 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
true |
false |
true |
240 |
1e-81 |
299.44 |
100.00 |
2,538,0,79,620,79,161 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 539 HELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQRl 618
cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 619 ypHDPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTGY 698
cd01948 80 --GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 699 SSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPALD 778
cd01948 158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 15805493 779 VHA 781
cd01948 238 AEE 240
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-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 |
7e-47 |
184.33 |
100.00 |
4,352,0,30,383,30,59,443,89,24,477,113,44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 353 HDSLTGLPNRALFSDRLSQAIARSKLPGGPqYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVARLGG 432
cd01949 1 TDPLTGLPNRRAFEERLERLLARARRSGRP-LALLLIDLDHFKQINDTYGHAAGDEVLKEVARRLRSSLRESDLVARLGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 433 DEFTILLEPLqSTEQAAQVAARIQDALRRPMQMPAagpgglpggwHQVTMSASLGIVHSQPDYDSAMAVLRDADIAMYRA 512
cd01949 80 DEFAILLPGT-DLEEAEELAERLRKAIEEPFFIDG----------EEIRVTASIGIAEYPEDGEDLEELLRRADKALYQA 148
|
....*....
gi 15805493 513 KDGGRAKYR 521
cd01949 149 KRSGRNRVV 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 |
| 128367 |
smart00052 |
EAL |
Putative diguanylate phosphodiesterase |
Putative diguanylate phosphodiesterase |
false |
false |
false |
241 |
5e-81 |
297.59 |
98.34 |
2,537,0,80,620,80,157 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 538 EHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQR 617
smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 618 lypHDPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTG 697
smart00052 81 ---QGPPLRISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 698 YSSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPAL 777
smart00052 158 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 237
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 32382 |
COG2200 |
Rtn |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms] |
false |
false |
false |
256 |
2e-77 |
286.07 |
99.61 |
2,534,1,81,619,82,174 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 535 NRMEHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQ 614
COG2200 2 LQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 615 WqrlyPHDPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDF 694
COG2200 82 W----PRAGPLRLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 695 GTGYSSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFS 774
COG2200 158 GTGYSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFS 237
|
250
....*....|....*....
gi 15805493 775 PALDVHAARTLVAEGQHHR 793
COG2200 238 RPLPADALDALLSSSQSRV 256
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 109613 |
pfam00563 |
EAL |
EAL domain |
EAL domain |
false |
false |
false |
236 |
5e-68 |
254.65 |
100.00 |
4,537,0,110,648,110,24,673,134,49,723,183,53 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 538 EHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQR 617
pfam00563 1 EQALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLIPPDEFLPLAERLGLIAELDRWVLEKALAQLAEWRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 618 LYPHDPPLHLSVNFCSQHLAAPDVHERVKElLQRTGFDPGRLNLEITESSLLSQTgDVQRNMERLRQLGVRLHLDDFGTG 697
pfam00563 81 NALLPPDLPLSVNLSPASLLDPSFLEALLA-LKQGGLPPSRLVLEITESDLDEDL-RLLEALARLRSLGFRLALDDFGTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15805493 698 YSSLSYLQLYPIDVLKIDRSFVQGMlDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPA 776
pfam00563 159 YSSLSYLSRLPPDYIKIDRSFIKDL-SDPESRALLRALIALARELGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 236
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 128563 |
smart00267 |
GGDEF |
diguanylate cyclase |
diguanylate cyclase |
false |
false |
false |
163 |
1e-41 |
166.65 |
100.00 |
4,348,0,34,383,34,56,440,90,27,477,117,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 349 HDALHDSLTGLPNRALFSDRLSQAIARSKLPGGPqYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVA 428
smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSP-FALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 429 RLGGDEFTILLePLQSTEQAAQVAARIQDALRRPMQMPAagpgglpggwHQVTMSASLGIVHSQPDYDSAMAVLRDADIA 508
smart00267 80 RLGGDEFALLL-PETSLEEAIALAERILQQLREPIIIHG----------IPLYLTISIGVAAYPNPGEDAEDLLKRADTA 148
|
170
....*....|....*
gi 15805493 509 MYRAKDGGRAKYRVF 523
smart00267 149 LYQAKKAGRNQVAVY 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 |
| 110022 |
pfam00990 |
GGDEF |
GGDEF domain |
GGDEF domain |
false |
false |
false |
160 |
3e-41 |
165.88 |
98.75 |
4,350,0,32,383,32,57,440,91,27,477,118,40 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 351 ALHDSLTGLPNRALFSDRLSQAIARSKLPGGPqYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVARL 430
pfam00990 1 AAHDPLTGLPNRRYFEEELEQELQRAQRRQSP-LALLLLDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 431 GGDEFTILLE--PLQSTEQAAQVAARIQDALRRPMQMPAagpgglpggwHQVTMSASLGIVHSQPDYDSAMAVLRDADIA 508
pfam00990 80 GGDEFAILLPdtSLEGAQELAERIRRLLAALKIPHTLSG----------LPLYVTISIGIAAYPNDGEDAEDLLKRADQA 149
|
....*....
gi 15805493 509 MYRAKDGGR 517
pfam00990 150 LYQAKNQGR 158
|
|
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-40 |
162.60 |
98.34 |
5,334,3,48,383,51,56,440,107,25,475,132,29,504,162,19 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 335 ARTAELEALSRQLQHDALHDSLTGLPNRALFSDRLSQAIARSKLPGGPqYAVLFLDVDRFKGINDTLGHPTGDAMLVEMA 414
COG2199 4 RLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEP-LALLLLDLDHFKQINDTYGHAAGDEVLREVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 415 RRLRACLRATDTVARLGGDEFTILLePLQSTEQAAQVAARIQDALRRPMQMpaagpgglpgGWHQVTMSASLGIVHSQPD 494
COG2199 83 RRLRSNLREGDLVARLGGDEFAVLL-PGTSLEEAARLAERIRAALEEPFFL----------GGEELRVTVSIGVALYPED 151
|
170 180 190
....*....|....*....|....*....|
gi 15805493 495 YDSAMAVLRD-ADIAMYRAKDGGRAKYRVF 523
COG2199 152 GSDDAELLLRrADLALYRAKRAGRNRVVVF 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 |
| 129356 |
TIGR00254 |
GGDEF |
diguanylate cyclase (GGDEF) domain |
diguanylate cyclase (GGDEF) domain |
false |
false |
false |
165 |
1e-32 |
137.08 |
99.39 |
4,350,1,27,378,28,61,440,89,19,467,108,57 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 351 ALHDSLTGLPNRALFSDRLSQAIARSKlPGGPQYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVARL 430
TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRAR-RFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 431 GGDEFTILLePLQSTEQAAQVAARIQDALrrpmqmpaAGPGGLPGGWHQVTMSASLGIVHSQPDYDSAMAVLRDADIAMY 510
TIGR00254 81 GGEEFVVIL-PGTPLEDALSKAERLRDAI--------NSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALY 151
|
170
....*....|....
gi 15805493 511 RAKDGGRAKYRVFT 524
TIGR00254 152 QAKKAGRNRVVVAD 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 |
| 138661 |
PRK11596 |
PRK11596 |
EAL domain-containing protein; Provisional |
EAL domain-containing protein; Provisional |
false |
false |
false |
255 |
4e-06 |
48.94 |
83.14 |
8,548,28,13,562,41,16,578,59,8,586,68,11,603,79,20,624,99,30,658,129,22,685,151,89 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 549 ELRVRYQPVLDLDrGRIEGFEALVRWQHPE--RGLLGPDD-FTPIAEESGLLpdidrwVLARACRELVQWQRLYPHDPpL 625
PRK11596 29 ERAYTFQPIYRTC-GRLMAVELLTVVTHPSnpSQRLSPDRyFAEITVSHRLD------VVKEQLDLLAQKADFFVRHG-L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 626 HLSVNFCSQHLAAPDVHERVKELLQRTGFdpgrLNLEITESSLLSQTGDVQRNMErlrqlGVRLHLDDFGTGYSSLSYLQ 705
PRK11596 101 LASVNIDGPTLIALRQQPKILRLIERLPW----LRFELVEHIRLPKDSTFASMCE-----FGPLWLDDFGTGMANFSALS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15805493 706 LYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFS 774
PRK11596 172 EVRYDYIKVARELFVMLRQSPEGRTLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLS 240
|
|
cl00290 |
140582 |
EAL |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria. |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called... |
-1 |
| 128397 |
smart00086 |
PAC |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) |
true |
false |
false |
43 |
0.006 |
38.32 |
100.00 |
1,272,0,43 |
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15805493 273 QFEERMLRPDGEPVYQLRNYTPLFDENGELLLYLGHGVDVTEL 315
smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
smart00086 |
128397 |
PAC |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) |
-1 |
| 137662 |
PRK10060 |
PRK10060 |
RNase II stability modulator; Provisional |
RNase II stability modulator; Provisional |
false |
true |
false |
663 |
7e-101 |
363.67 |
66.67 |
9,308,219,17,334,236,3,353,239,23,379,262,61,442,323,8,450,332,18,478,350,82,561,432,56,620,488,173 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 309 GVDVTELRRTQEALRELnaqleerveARTaelealsrqlqhdalhDSLTGLPNRALFSDRLSQAIARSklpGGPQYAVLF 388
PRK10060 220 GTDITEERRAQERLRIL---------ANT----------------DSITGLPNRNAIQELIDHAIAQA---DNNQVGIVY 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 389 LDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVARLGGDEFTILLEplQSTEQAAQ-VAARIQDALRRPMQMPA 467
PRK10060 272 LDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAS--HTSQAALEaMASRILTRLRLPFRIGL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 468 AgpgglpggwhQVTMSASLGIVHSQPDYDSAMAVLRDADIAMYRAKDGGRAKYRVFTPEMREHILHVNRMEHELRRALAA 547
PRK10060 350 I----------EVYTGCSIGIALSPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALEN 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 548 DELRVRYQPVLDLdRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQRlypHDPPLHL 627
PRK10060 420 DQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVILDVVRQAAKWRD---KGINLRV 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 628 SVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTGYSSLSYLQLY 707
PRK10060 496 AVNVSARQLADQTIFTALKQVLQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 708 PIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPALDVHAARTLVA 787
PRK10060 576 PIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYK 655
|
....*.
gi 15805493 788 EGQHHR 793
PRK10060 656 RYQKLR 661
|
|
|
|
|
|
|
-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 |
1e-87 |
319.66 |
66.82 |
4,323,200,54,378,254,90,478,344,137,621,481,162 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 324 ELNAQLEERVEARTAELEALSRQLQHDALHDSLTGLPNRALFSDRLSQAIARSKlPGGPQYAVLFLDVDRFKGINDTLGH 403
COG5001 201 SDMVQSQVTLTQRAEETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAAR-QSGRRLVLGVIDLDGFKPVNDAFGH 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 404 PTGDAMLVEMARRLRACLRATDTVARLGGDEFTILLEPLQSTEQAAQVAARIQDALRRPMQMPAAgpgglpggwhQVTMS 483
COG5001 280 ATGDRLLIEVGRRLKAFDGAPILAARLGGDEFALIIPALEDDALRVAGARALCESLQAPYDLRGV----------RVQVG 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 484 ASLGIVHSQPDYDSAMAVLRDADIAMYRAKDGGRAKYRVFTPEMREHILHVNRMEHELRRALAADELRVRYQPVLDLDRG 563
COG5001 350 ASIGIAPFPSGADTSEQLFERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSG 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 564 RIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWqrlyphDPPLHLSVNFCSQHLAAPDVHE 643
COG5001 430 KTIALEALARWHSPEIGPVPPDVFIGIAERSGQIVELTRLLLAKALREARAW------PMDVRVSINLSARDLASMENVR 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 644 RVKELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTGYSSLSYLQLYPIDVLKIDRSFVQGML 723
COG5001 504 RLLAIVSESCIAPHRLDFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLE 583
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 724 DNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPALDVHAAR 783
COG5001 584 ENPTSEDIVRTVLQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMPAEERR 643
|
|
|
|
|
|
|
-1 |
| 138538 |
PRK11359 |
PRK11359 |
cAMP phosphodiesterase; Provisional |
cAMP phosphodiesterase; Provisional |
false |
true |
false |
799 |
4e-74 |
274.80 |
56.45 |
10,299,331,13,312,345,25,338,370,7,352,377,20,377,397,58,436,455,35,481,490,10,491,501,6,500,507,125,627,632,150 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 300 GELLLYLGHGVDV-TELRRTQEALRELNAQLEERVEARTaELEALSRqlqhdalHDSLTGLPNRALFSDRLSQAiarskL 378
PRK11359 332 GILQIKTSSGAETsAFIERVADISQHMAALALEQEKSRQ-HIEQLIQ-------FDPMTGLPNRNNLHNYLDDL-----V 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 379 PGGPQYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVARLGGDEFtILLEPLQSTEQAAQVAARIQDA 458
PRK11359 399 DKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQF-VLVSLENDVSNITQIADELRNV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 459 LRRPMQMPAAGPGglpggwhqvtMSASLGIVHS-QPDYDSamaVLRDADIAMYRAKDGGRAKYRVFTPEMREHILHVNRM 537
PRK11359 478 VSKPIMIDDKPFP----------LTLSIGISYDvGKNRDY---LLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 538 EHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQR 617
PRK11359 545 GAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRS 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 618 LYPHDPPLhlSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTG 697
PRK11359 625 QNIHIPAL--SVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTG 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 698 YSSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPAL 777
PRK11359 703 FSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
4e-68 |
255.01 |
37.72 |
8,338,675,42,381,717,58,440,775,20,467,795,13,482,808,56,538,866,33,571,900,33,608,933,163 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 339 ELEALSRQLQHDALHDSLTGLPNRALFSDRLSQAIARSKLPGgPQYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLR 418
PRK09776 676 ESRAMLRQLSYSASHDALTGLANRASFEKQLREALQTVNSTH-QRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 419 ACLRATDTVARLGGDEFTILLePLQSTEQAAQVAARIQDALRrpmqmpaAGPGGLPGGWHQVtmSASLGIVHSQPDYDSA 498
PRK09776 755 SMLRSSDVLARLGGDEFGLLL-PDCNVESARFIATRIISAIN-------DYRFPWEGRVYRV--GASAGITAIDDNNHQA 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 499 MAVLRDADIAMYRAKDGGRAKYRVFTPEMREHILHVNRME--HELRRALAADELRVRYQPVLDLDRGRIEGFEAL-VRWQ 575
PRK09776 825 SEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSERRELSlaEQWRSMLEENQLMLQAQEIASPRIPEARNLWLIsLRLW 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 576 HPERGLLGPDDFTPIAEESGLLPDIDRWVlaraCRELVQWQRLYPHDPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFD 655
PRK09776 905 DCEGEIIDEGAFRPAAEDPALMHALDRWV----IHELFQQGARAVASKGLSIAIPLSVASLSSATLLPFLLEQLENSPLP 980
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 656 PGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTGYSSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTI 735
PRK09776 981 PRLLHLEITETALLNHAEAASRLVQKLRLAGCRVVLDDFGRGLSSFNYLKAFMADYLKIDGELCANLQGNLMDEMLVSII 1060
|
410 420 430
....*....|....*....|....*....|....*.
gi 15805493 736 VAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGF 771
PRK09776 1061 NGIAQRLGMKTIAGPVELPLTLDTLSGIGVDLAQGY 1096
|
|
|
|
|
|
|
-1 |
| 139666 |
PRK13561 |
PRK13561 |
putative phosphodiesterase; Provisional |
putative phosphodiesterase; Provisional |
false |
true |
false |
651 |
6e-62 |
234.28 |
66.67 |
9,340,217,6,346,226,29,380,255,88,478,343,17,496,360,121,620,481,87,707,571,20,730,591,47,777,640,11 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 341 EALSRQ---LQHDALHDSLTGLPNRALFSDRLSQAIARsklpgGPQYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRL 417
PRK13561 218 QLLQRHyeeQNENAMRFPVSDLPNKALLMALLEQVVAR-----KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 418 RACLRATDTVARLGGDEFTILLEPLQSTEQAAQVAARIQDALRRPMQMPAAgpgglpggwhQVTMSASLGIVHSQPDYdS 497
PRK13561 293 KSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRI----------QLRPSCSIGIAMFYGDL-T 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 498 AMAVLRDADIAMYRAKDGGRAKYRVFTPEMREHILHVNRMEHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHP 577
PRK13561 362 AEQLYSRAVSAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 578 ERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQRlypHDPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPG 657
PRK13561 442 DGSWDLPDGLIDRIESCGLMVTVGHWVLEESCRLLAAWQE---RGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 658 RLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLDDFGTGYSSLSYLQLY---PIDVLKIDRSFVQGMLDNDSnaeLVRT 734
PRK13561 519 TLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPEDSS---MVAA 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15805493 735 IVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPAL--DVHAARTLVAE 788
PRK13561 596 IIMLAQSLNLQMIAEGVETEAQRDWLAKAGVGVAQGFLFARPLpiEIFEERYLSEK 651
|
|
|
|
|
|
|
-1 |
| 34551 |
COG4943 |
COG4943 |
Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms] |
Predicted signal transduction protein containing sensor and EAL domains [Signal... |
false |
true |
false |
524 |
8e-54 |
207.50 |
45.61 |
3,538,270,83,624,353,47,672,400,109 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 539 HELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQWQRL 618
COG4943 271 RRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVFRDLGDLLRQ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 619 YPHdppLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQtGDVQRNMERLRQLGVRLHLDDFGTGY 698
COG4943 351 HRD---LHVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFADP-KKMTPIILRLREAGHEIYIDDFGTGY 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 699 SSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSPALD 778
COG4943 427 SNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYGQGWLFSKALP 506
|
...
gi 15805493 779 VHA 781
COG4943 507 AQA 509
|
|
|
|
|
|
|
-1 |
| 138768 |
PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
biofilm formation regulator HmsP; Provisional |
false |
true |
false |
728 |
7e-52 |
201.08 |
55.91 |
7,355,304,25,382,329,81,475,410,7,482,419,134,619,553,84,703,640,24,730,664,47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 356 LTGLPNRALFSDRLSQAIARSKLPGgpQYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDTVARLGGDEF 435
PRK11829 305 VTELPNRSLFISLLEKEIASSTRTD--HFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 436 TILLEPLQSTEQAAQVAARIQDALRRPMqmpaagpgglpgGWHQVTM--SASLGIVHSQPDYDSAMAVLRDADIAMYRAK 513
PRK11829 383 AVLARGTRRSFPAMQLARRIMSQVTQPL------------FFDEITLrpSASIGITRYQAQQDTAESMMRNASTAMMAAH 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 514 DGGRAKYRVFTPEMREHILHVNRMEHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEE 593
PRK11829 451 HEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 594 SGLLPDIDRWVLARACRELVQWQrlyPHDPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQTG 673
PRK11829 531 EGMMVPLGNWVLEEACRILADWK---ARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 674 DVQRNMERLRQLGVRLHLDDFGTGYSSLSY---LQLYPIDVLKIDRSFVQGMLDNDSnaeLVRTIVAMAKNLNLKVVAEG 750
PRK11829 608 EALRLLRELQGLGLLIALDDFGIGYSSLRYlnhLKSLPIHMIKLDKSFVKNLPEDDA---IARIISCVSDVLKVRVMAEG 684
|
410 420
....*....|....*....|....*..
gi 15805493 751 IEDPRQLAALRGLGCDAGQGFLFSPAL 777
PRK11829 685 VETEEQRQWLLEHGIQCGQGFLFSPPL 711
|
|
|
|
|
|
|
-1 |
| 137979 |
PRK10551 |
PRK10551 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
518 |
1e-39 |
160.60 |
46.91 |
3,535,262,85,622,347,49,672,396,109 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 536 RMEHELRRALAADELRVRYQPVLDLDRGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELVQW 615
PRK10551 263 RPGREILTAIKREQFYVVYQPVVDTQTLRVTGLEVLLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 616 QRLYPhdPPLHLSVNFCSQHLAAPDVHERVKELLQRTGFDPGRLNLEITESSLLSQtGDVQRNMERLRQLGVRLHLDDFG 695
PRK10551 343 QKVLP--VGAKLGINIAPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMLQE-EEALKLFAWLHSQGIEIAIDDFG 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 696 TGYSSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFSP 775
PRK10551 420 TGHSALIYLERFTLDYLKIDRGFINAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLREHGVNFLQGYWISR 499
|
....*.
gi 15805493 776 ALDVHA 781
PRK10551 500 PLPLDD 505
|
|
|
|
|
|
|
-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 |
2e-33 |
139.67 |
45.06 |
6,322,239,17,339,258,43,383,301,56,440,357,21,462,378,11,479,389,46 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 323 RELNAQLEERVEARTAE--LEALSRQLQHDALHDSLTGLPNRALFSDRLSQAIARSKLPGGPqYAVLFLDVDRFKGINDT 400
COG3706 240 GELRARLRRQLRRKRYErqLRESLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRP-LSLLMLDIDDFKEINDT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 401 LGHPTGDAMLVEMARRLRACLRATDTVARLGGDEFTILLePLQSTEQAAQVAARIQDALRRpMQMPAAGPGGLpggwhqV 480
COG3706 319 YGHDVGDEVLRQVARRLRQTVRGLDLVARYGGEEFAVVL-PDTDLEAAIAIAERIRQKINE-LPFVHELSREP------L 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15805493 481 TMSASLGIVHSQPDYDSAMAVLRDADIAMYRAKDGGRAKYRVFTP 525
COG3706 391 EVTISIGVAEGKPGEDSIEELLKRADKALYKAKASGRNRVVVKRA 435
|
|
|
|
|
|
|
-1 |
| 137400 |
PRK09581 |
pleD |
response regulator PleD; Reviewed |
response regulator PleD; Reviewed |
false |
true |
false |
457 |
3e-29 |
125.80 |
50.55 |
11,287,218,4,291,227,5,296,236,8,304,253,11,315,266,1,316,268,18,335,286,5,350,291,32,383,323,56,440,379,16,463,395,54 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 288 QLRN-----YTPLF----DENGELLL---------YLGHGVDVTEL--R-RTQEALRELNAQLEERVEaRTAELealsrq 346
PRK09581 219 QLRSkertrYVPILllvdEDEDPRLVkalelgvndYLMRPIDKNELlaRvRTQIRRKRYQDALRQNLE-QSIEM------ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 347 lqhdALHDSLTGLPNRALFSDRLSQAIARSKLPGGPqYAVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRACLRATDT 426
PRK09581 292 ----AVTDGLTGLHNRRYFDMHLKQLIERANERGKP-LSLMMLDIDHFKQVNDTYGHDAGDEVLREFAKRLRKNIRGTDL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 427 VARLGGDEFTILLePLQSTEQAAQVAARIQdalrrpmQMPAAGPGGLPGGWHQVTMSASLGIVHSQPDYDSAMAVLRDAD 506
PRK09581 367 IARYGGEEFVVVM-PDTDIEVAIAVAERIR-------RKIAEEPFAISDGKERLNVTVSIGVAELRPSGESIEALIKRAD 438
|
250
....*....|.
gi 15805493 507 IAMYRAKDGGR 517
PRK09581 439 KALYEAKNTGR 449
|
|
|
|
|
|
|
-1 |
| 137576 |
PRK09894 |
PRK09894 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
293 |
8e-23 |
104.41 |
59.73 |
7,329,107,18,347,126,15,362,142,17,383,159,56,440,215,19,468,234,26,495,260,22 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 330 EERVEARTAELEALSRQL-QHDALHDSLTGLPNR-ALFSDRLSQAIARSKLPggpqYAVLFLDVDRFKGINDTLGHPTGD 407
PRK09894 108 QEGLLSFTAALTDYKIYLlTIRSNMDVLTGLPGRrVLDESFDHQLRNREPLN----LYLALLDIDRFKLVNDTYGHLIGD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 408 AMLVEMARRLRACLRATDTVARLGGDEFTILLePLQSTEQAAQVAARIQDALrrpmqmpaaGPGGLPGGWHQVTMSASLG 487
PRK09894 184 VVLRTLATYLASWTRPYETVYRYGGEEFIIIL-KAATDEEACRAGERIRQLI---------ANQAITHSEGRINITATFG 253
|
170 180 190
....*....|....*....|....*....|
gi 15805493 488 IVHSQPDyDSAMAVLRDADIAMYRAKDGGR 517
PRK09894 254 VTRAFPE-EPLDEVIGRADRAMYEGKQAGR 282
|
|
|
|
|
|
|
-1 |
| 138376 |
PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
regulatory protein CsrD; Provisional |
false |
true |
false |
642 |
2e-22 |
102.65 |
68.69 |
18,315,196,10,328,206,9,337,217,9,349,226,34,384,260,37,421,298,6,427,305,12,440,317,21,464,338,14,485,352,9,495,361,13,508,387,2,510,390,5,515,399,8,540,407,21,562,428,54,621,482,25,646,508,129 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 316 RRTQEALRELnaqLEERVEART--AELEALSRQlqhDALHDSLTGLPNRALFSDRLSQAIARSKLPGGPQyAVLFLDVDR 393
PRK11059 197 RLASRALDHL---LEELQDARKerSRFDTFIRS---NAFLDAKTGLGNRLFFDNQLDTLLEDQEKVGAHG-VVMLIRLPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 394 FKGINDTLGHPTGDAMLVEMARRLRACL-RATDTV-ARLGGDEFTILLePLQSTEQAAQVAARIQDALRRpmqMPAAGPG 471
PRK11059 270 FDLLQEELGESQVDELLFELINLLSTFVqRYPGALlARYSRSDFAVLL-PHRSLKEADSLASQLLKAVDS---LPPPKML 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 472 GLPGGWHqvtmsasLGIVHSQPDyDSAMAVLRDADIA-------------MY-RAKDG----GRAKYRVFtpemrehilh 533
PRK11059 346 DRDDFLH-------IGIAAYRSG-QSTEQVMEEAEMAlrsaqlqggnswfMYdKAQDPekgrGSVRWRTL---------- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 534 vnrmeheLRRALAADELRVRYQPVLDLDrGRIEGFEALVRWQHPERGLLGPDDFTPIAEESGLLPDIDRWVLARACRELV 613
PRK11059 408 -------LEQALVRGGPRLYQQPVVTRD-GQVHHRELMCRIRDGQGNEVRAAEFMPMVLQCGLSEQYDRQVIERVLPLLS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 614 QWQrlyphDPPLHLSVNFCSQHLAAPDVHERVK-ELLQRTGFDPGRLNLEITESSLLSQTGDVQRNMERLRQLGVRLHLD 692
PRK11059 480 YWP-----EESQNLSINLSVDSLLSRAFQRWLRdTLLQCERSQRKRLIFELAEADVVQHIDRLRPVLRMLRGLGCRLAVD 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 693 DFGTGYSSLSYLQLYPIDVLKIDRSFVQGMLDNDSNAELVRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFL 772
PRK11059 555 QAGLTVVSTSYIKELNVELIKLHPSLVRNIHQRTENQLFVRSLVGACAGTETQVFAEGVESREEWQTLQILGVSGGQGDF 634
|
...
gi 15805493 773 FSP 775
PRK11059 635 FAS 637
|
|
|
|
|
|
|
-1 |
| 137615 |
PRK09966 |
PRK09966 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
407 |
1e-21 |
100.86 |
43.73 |
5,322,220,9,332,229,45,379,274,89,477,363,15,493,378,20 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 323 RELNAQLEErVEARTAELEALSRQLQHDALHDSLTGLPNRALFSDRLSQAIARSKlpGGPQYAVLFLDVDRFKGINDTLG 402
PRK09966 221 LDFNSLLDE-MEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSD--ARKTSALLFLDGDNFKYINDTWG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 403 HPTGDAMLVEMARRLRACLRATDTVARLGGDEFTILLEPLQSTEQAAQVAARIQDALRRPMQMPAAgpgglpggwHQVTM 482
PRK09966 298 HATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNG---------HQTTM 368
|
170 180 190
....*....|....*....|....*....|.
gi 15805493 483 SASLGIVHSQpDYDSAMAVLRDADIAMYRAK 513
PRK09966 369 TLSIGYAMTI-EHASAEKLQELADHNMYQAK 398
|
|
|
|
|
|
|
-1 |
| 137770 |
PRK10245 |
adrA |
diguanylate cyclase AdrA; Provisional |
diguanylate cyclase AdrA; Provisional |
false |
true |
false |
371 |
2e-16 |
83.02 |
44.74 |
5,344,203,18,367,221,17,384,242,55,439,299,25,477,324,45 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 345 RQLQHDALHDSLTGLPNRalfsdRLSQAIARSKLPGGPQY----AVLFLDVDRFKGINDTLGHPTGDAMLVEMARRLRAC 420
PRK10245 204 RRLQVMSTRDGMTGVYNR-----RHWETMLRNEFDNCRRHnrdaTLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQIT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 421 LRATDTVARLGGDEFTILL--EPLQSTEQAAQVAARIQDALRRPMQmpaagpgglpggwHQVTMSASLGIVHSQPDYDSA 498
PRK10245 279 LRGSDVIGRFGGDEFAVIMsgTPAESAITAMLRVHEGLNTLRLPNA-------------PQVTLRISVGVAPLNPQMSHY 345
|
170 180
....*....|....*....|....
gi 15805493 499 MAVLRDADIAMYRAKDGGRAKYRV 522
PRK10245 346 REWLKSADLALYKAKKAGRNRTEV 369
|
|
|
|
|
|
|
-1 |
| 117025 |
pfam08448 |
PAS_4 |
PAS fold |
PAS fold |
true |
true |
false |
110 |
1e-11 |
67.05 |
91.82 |
4,211,9,22,233,32,11,249,43,32,282,75,35 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 212 VLGPDQRYRFCNPAAIGNPQIR-EWIMGHTDAEYvaergFPPELATERGRHMDEAARERKTVQFEERMLRPdGEPVYQLR 290
pfam08448 10 VLDPDGRVRYANAAAAELFGLPpEELLGKTLAEL-----LPPEDAARLERALRRALEGEEPIDFLEELLLN-GEERHYEL 83
|
90 100
....*....|....*....|....*..
gi 15805493 291 NYTPLFDENGELLLYLGHGVDVTELRR 317
pfam08448 84 RLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
|
|
|
|
|
-1 |
| 117025 |
pfam08448 |
PAS_4 |
PAS fold |
PAS fold |
true |
true |
false |
110 |
7e-05 |
44.71 |
88.18 |
6,86,12,11,97,24,9,106,34,16,123,50,22,146,72,22,169,94,15 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 87 RQGTVIHASEA-CGALGWSHD-LRGRPLAELLSSPLEDlRLSNLLKRVWQGERLHQVPLSLrHTEGRLQLAEASLLPLHA 164
pfam08448 13 PDGRVRYANAAaAELFGLPPEeLLGKTLAELLPPEDAA-RLERALRRALEGEEPIDFLEEL-LLNGEERHYELRLTPLRD 90
|
90 100
....*....|....*....|
gi 15805493 165 ASGEsTAAYVAMSITTTELH 184
pfam08448 91 PDGE-VIGVLVISRDITERR 109
|
|
|
|
|
|
|
-1 |
| 33240 |
COG3434 |
COG3434 |
Predicted signal transduction protein containing EAL and modified HD-GYP domains [Signal transduction mechanisms] |
Predicted signal transduction protein containing EAL and modified HD-GYP domains [... |
false |
true |
false |
407 |
3e-04 |
42.57 |
27.27 |
4,653,80,16,671,96,29,700,130,19,732,149,42 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 654 FDPGRLNLEITESSLLsqTGDVQRNMERLRQLGVRLHLDDFGTGYSS-----LSYLQLYPIDVLKIDRSFVqgmldndsn 728
COG3434 81 LPPDKVVIEILEDCPP--TEKLLSAIKELKQKGYLLALDDFIFSNVSewkplLPLSDIVKIDFKRVTFDKA--------- 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15805493 729 aelvRTIVAMAKNLNLKVVAEGIEDPRQLAALRGLGCDAGQGFLFS 774
COG3434 150 ----RLFDRDLGYINKKFLAEKVETEEEFEQAKKAGFDLFQGYFFS 191
|
|
|
|
|
|
|
-1 |
| 129332 |
TIGR00229 |
sensory_box |
PAS domain S-box |
PAS domain S-box |
false |
true |
false |
124 |
5e-04 |
41.88 |
68.55 |
3,232,39,14,250,53,46,297,99,25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 233 REWIMGHTDAEYVAergfPPELATERGRHMDEAARERKTVQFEERMLRPDGEPVYQLRNYTPLFdENGELLLYLGHGVDV 312
TIGR00229 40 AEELIGRNVLELIP----EEDREEVRERIERLLEGEREPYSEERRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDI 114
|
90
....*....|
gi 15805493 313 TELRRTQEAL 322
TIGR00229 115 TERKQAEEAL 124
|
|
|
|
|
|
|
-1 |
| 139664 |
PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
bacterio-opsin activator; Provisional |
false |
true |
false |
674 |
0.002 |
40.17 |
11.87 |
3,250,215,8,263,223,61,325,284,11 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 251 PPELATERgrhmdEAARERKTVQFEERMLRPDGEPVYQLRNYTPLFDENGELLLYLGHGVDVTELRRTQEALRElNAQLE 330
PRK13558 216 EDRVAEFW-----TAITEDHDTQVVLRNYRRDGSLFWNQVDISPIYDEDGTVSHYVGFQMDVSERMAAQQELQG-ERQSL 289
|
....*.
gi 15805493 331 ERVEAR 336
PRK13558 290 DRLLDR 295
|
|
|
|
|
|
|
-1 |
| 137515 |
PRK09776 |
PRK09776 |
putative sensor protein; Provisional |
putative sensor protein; Provisional |
false |
true |
false |
1116 |
0.002 |
39.69 |
5.82 |
3,259,490,25,285,515,7,292,523,32 |
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15805493 260 RHMDEAARERKTVQFEERMLRPDGEpVYQLRNY-TPLFDENGELLLYLGHGVDVTELRRTQEALRE 324
PRK09776 491 KEIRDALQGRSPFKLEFRIVVPDGE-IRHIRALaNRVLNKDGEVERLLGINMDMTEVRQLNEALFE 555
|
|
|
|
|
|
|
-1 |
| 33926 |
COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms] |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [... |
true |
true |
false |
603 |
0.004 |
39.10 |
9.45 |
3,314,321,36,350,358,13,365,371,7 |
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15805493 315 LRRTQEALRELNAQLEERVEARTAELEALSRQLQHD-ALHDSLTGLPNRAlfSDRLSQA 372
COG4191 322 ARLRLAELQEARAELERRVEERTADLTRANARLQAEiAEREQAEAALRRA--QDELVQA 378
|
|
|
|
|
|
|
-1 |
| 139665 |
PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
hypothetical protein; Provisional |
false |
true |
false |
363 |
0.005 |
38.65 |
29.48 |
7,265,113,7,273,120,44,330,164,8,340,172,10,350,187,13,363,204,7,370,214,6 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15805493 266 ARERKTVqFEERMLRPDGEPVYQLRNYTPLFDENGELLLYLGHGVDVTELRRtqealrelnaqleERVEARTAelEALSR 345
PRK13559 114 AAERVVV-VELLNYRKDGSPFWNALHLGPIYDEDGKLLYFFGSQWDVTDIRA-------------VRALEAHE--RRLAR 177
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15805493 346 QLQHD-----ALHDSLTGLPNRA----LFSDRLS---QAIARS 376
PRK13559 178 EVDHRsknvfAVVDSIVRLTGRAddasLYAAAIQervQALARA 220
|
|
|
|
|
|
|
-1 |
|