|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
96-333 |
4.91e-63 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 210.41 E-value: 4.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 96 ELQMEHyDMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAI 170
Cdd:COG2200 326 RLALES-ELREALEEGELRLYYQPIVDlRTGRVVGYEALLR---WrhpdGGLISPAEFIPAAERSGLIVELDRWVLERAL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 171 ETSAEWLPIGVKR--FVNFLPSSIYDAQMcLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAM 248
Cdd:COG2200 402 RQLARWPERGLDLrlSVNLSARSLLDPDF-LERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 249 DDVGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGY 328
Cdd:COG2200 481 DDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
|
....*
gi 1288431380 329 LFGKP 333
Cdd:COG2200 561 LFGRP 565
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
103-333 |
1.51e-60 |
|
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.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 194.30 E-value: 1.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 103 DMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRPV--EWGASFqPYELFETARKTGLHAFLDRAARTSAIETSAEWLPI 179
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDlRTGRIVGYEALLRWRhpEGGLIS-PAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 180 G--VKRFVNFLPSSIYDAQmCLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYST 257
Cdd:cd01948 81 GpdLRLSVNLSARQLRDPD-FLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288431380 258 LEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
108-333 |
4.86e-57 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 185.21 E-value: 4.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 108 ILHKQFTSYMQPIVDS-SEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAIETSAEWLPIGVK 182
Cdd:pfam00563 8 LENGEFVLYYQPIVDLrTGRVVGYEALLR---WqhpdGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 183 RF-VNFLPSSIYDAQMClSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYSTLEQM 261
Cdd:pfam00563 85 KLsINLSPASLADPGFL-ELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288431380 262 IKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
103-333 |
8.47e-42 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 145.82 E-value: 8.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 103 DMVSIILHKQFTSYMQPIVDS-SEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAIETSAEWL 177
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLrTGRLVGVEALIR---WqhpeGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 178 PIGVKRF---VNFLPSSIYDA---QMCLshtfNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDV 251
Cdd:smart00052 80 AQGPPPLlisINLSARQLISPdlvPRVL----ELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 252 GAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFG 331
Cdd:smart00052 156 GTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFS 235
|
..
gi 1288431380 332 KP 333
Cdd:smart00052 236 RP 237
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
99-333 |
8.72e-27 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 111.34 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 99 MEHYDMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRPVEWGASFQ-PYELFETARKTGLHAFLDRAARTSAIETSAEW 176
Cdd:PRK13561 400 TEESDILNALENHQFAIWLQPQVEmRSGKLVSAEALLRMQQPDGSWDlPEGLIDRIESCGLMVTVGHWVLEESCRLLAAW 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 177 ------LPIGVkrfvNFLPSSIYDAQMcLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDD 250
Cdd:PRK13561 480 qergimLPLSV----NLSALQLMHPNM-VADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDD 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 251 VGAGYSTLEQMIKLKP---DYVKIDRSLIDHCdrnPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQG 327
Cdd:PRK13561 555 FGMGYAGLRQLQHMKSlpiDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQG 631
|
....*.
gi 1288431380 328 YLFGKP 333
Cdd:PRK13561 632 FLFARA 637
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
96-333 |
4.91e-63 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 210.41 E-value: 4.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 96 ELQMEHyDMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAI 170
Cdd:COG2200 326 RLALES-ELREALEEGELRLYYQPIVDlRTGRVVGYEALLR---WrhpdGGLISPAEFIPAAERSGLIVELDRWVLERAL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 171 ETSAEWLPIGVKR--FVNFLPSSIYDAQMcLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAM 248
Cdd:COG2200 402 RQLARWPERGLDLrlSVNLSARSLLDPDF-LERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 249 DDVGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGY 328
Cdd:COG2200 481 DDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
|
....*
gi 1288431380 329 LFGKP 333
Cdd:COG2200 561 LFGRP 565
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
103-333 |
1.51e-60 |
|
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.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 194.30 E-value: 1.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 103 DMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRPV--EWGASFqPYELFETARKTGLHAFLDRAARTSAIETSAEWLPI 179
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDlRTGRIVGYEALLRWRhpEGGLIS-PAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 180 G--VKRFVNFLPSSIYDAQmCLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYST 257
Cdd:cd01948 81 GpdLRLSVNLSARQLRDPD-FLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288431380 258 LEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
108-333 |
4.86e-57 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 185.21 E-value: 4.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 108 ILHKQFTSYMQPIVDS-SEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAIETSAEWLPIGVK 182
Cdd:pfam00563 8 LENGEFVLYYQPIVDLrTGRVVGYEALLR---WqhpdGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 183 RF-VNFLPSSIYDAQMClSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYSTLEQM 261
Cdd:pfam00563 85 KLsINLSPASLADPGFL-ELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288431380 262 IKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
103-333 |
8.47e-42 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 145.82 E-value: 8.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 103 DMVSIILHKQFTSYMQPIVDS-SEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAIETSAEWL 177
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLrTGRLVGVEALIR---WqhpeGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 178 PIGVKRF---VNFLPSSIYDA---QMCLshtfNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDV 251
Cdd:smart00052 80 AQGPPPLlisINLSARQLISPdlvPRVL----ELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 252 GAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFG 331
Cdd:smart00052 156 GTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFS 235
|
..
gi 1288431380 332 KP 333
Cdd:smart00052 236 RP 237
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
97-333 |
2.02e-40 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 150.70 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 97 LQMEHyDMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLR---PvEWGAsFQPYELFETARKTGLHAFLDRAARTSAIET 172
Cdd:COG5001 424 LELEA-DLRRALERGELELHYQPQVDlATGRIVGAEALLRwqhP-ERGL-VSPAEFIPLAEETGLIVPLGEWVLREACRQ 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 173 SAEWLPIGVKRF---VNFLPSSIYDAQMcLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMD 249
Cdd:COG5001 501 LAAWQDAGLPDLrvaVNLSARQLRDPDL-VDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALD 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 250 DVGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYL 329
Cdd:COG5001 580 DFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYL 659
|
....
gi 1288431380 330 FGKP 333
Cdd:COG5001 660 FSRP 663
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
110-333 |
1.22e-28 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 116.17 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 110 HKQFTSYMQPIVD-SSEQIVAYEFLLRpveW----GASFQPyELF-ETARKTGLHAFLDRAARTSAIETSAEWLP----- 178
Cdd:COG4943 282 RREFYVHYQPIVDlKTGRCVGAEALVR---WrdpdGSVISP-DIFiPLAEQSGLISPLTRQVIEQVFRDLGDLLAadpdf 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 179 -IGVkrfvNFLPSSIydaqmcLSHTFntIDRLH-------LDPRDFVFEVVETEKIDDVEHLQSIfEVYRSHGISVAMDD 250
Cdd:COG4943 358 hISI----NLSASDL------LSPRF--LDDLErllartgVAPQQIVLEITERGFIDPAKARAVI-AALREAGHRIAIDD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 251 VGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLF 330
Cdd:COG4943 425 FGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLF 504
|
...
gi 1288431380 331 GKP 333
Cdd:COG4943 505 AKP 507
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
99-333 |
8.72e-27 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 111.34 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 99 MEHYDMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRPVEWGASFQ-PYELFETARKTGLHAFLDRAARTSAIETSAEW 176
Cdd:PRK13561 400 TEESDILNALENHQFAIWLQPQVEmRSGKLVSAEALLRMQQPDGSWDlPEGLIDRIESCGLMVTVGHWVLEESCRLLAAW 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 177 ------LPIGVkrfvNFLPSSIYDAQMcLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDD 250
Cdd:PRK13561 480 qergimLPLSV----NLSALQLMHPNM-VADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDD 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 251 VGAGYSTLEQMIKLKP---DYVKIDRSLIDHCdrnPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQG 327
Cdd:PRK13561 555 FGMGYAGLRQLQHMKSlpiDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQG 631
|
....*.
gi 1288431380 328 YLFGKP 333
Cdd:PRK13561 632 FLFARA 637
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
118-347 |
6.31e-26 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 106.81 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 118 QPIVDSSEQIVAYEFLLRPVEwGASFQPYELFETARKTGLHAFLdraartsaiETSAEWLPIGVKRFVNFlpssiyDAQM 197
Cdd:COG3434 9 QPILDRDQRVVGYELLFRSGL-ENSAPDVDGDQATARVLLNAFL---------EIGLDRLLGGKLAFINF------TEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 198 CLSHTFntidrLHLDPRDFVFEVVETEKIDDvEHLQSIFEvYRSHGISVAMDDV--GAGYSTLEQMIklkpDYVKIDrsl 275
Cdd:COG3434 73 LLSDLP-----ELLPPERVVLEILEDVEPDE-ELLEALKE-LKEKGYRIALDDFvlDPEWDPLLPLA----DIIKID--- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1288431380 276 IDHCDRnpaqqKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKPSERPPRD-PHSQLIY 347
Cdd:COG3434 139 VLALDL-----EELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKlPPSQLTL 206
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
112-333 |
2.01e-23 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 101.30 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 112 QFTSYMQPIVDSSEQIVAYEFLLRpveWGAS----FQPYELFETARKTGLHAFLDRAARTSAIETSAEWLP--IGVKRFV 185
Cdd:PRK10060 421 QLVIHYQPKITWRGEVRSLEALVR---WQSPerglIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDkgINLRVAV 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 186 NFLPSSIYDaQMCLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYSTLEQMIKLK 265
Cdd:PRK10060 498 NVSARQLAD-QTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFP 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288431380 266 PDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:PRK10060 577 IDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
103-336 |
8.14e-20 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 90.39 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 103 DMVSIILHKQFTSYMQPIVD-SSEQIVAYEFLLRpveW----GASFQPYELFETARKTGLHAFLDRAARTSAIETSAEWL 177
Cdd:PRK11829 409 DLLQAIENHDFTLFLQPQWDmKRQQVIGAEALLR---WcqpdGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWK 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 178 PIGVK--RFVNFLPSSIYDAQMcLSHTFNTIDRLHLDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGY 255
Cdd:PRK11829 486 ARGVSlpLSVNISGLQVQNKQF-LPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGY 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 256 STLEQMIKLKP---DYVKIDRSLIDHCdrnPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGK 332
Cdd:PRK11829 565 SSLRYLNHLKSlpiHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSP 641
|
....
gi 1288431380 333 PSER 336
Cdd:PRK11829 642 PLPR 645
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
219-333 |
4.74e-17 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 82.51 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 219 EVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHD 298
Cdd:PRK11359 667 EITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQS 746
|
90 100 110
....*....|....*....|....*....|....*
gi 1288431380 299 FGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:PRK11359 747 LNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
108-333 |
9.94e-16 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 78.11 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 108 ILHKQFTSYMQPIVDS-SEQIVAYEFLLR---PVEWGAS---FQPYelfetARKTGL------HAFLDRAARTSAIETSa 174
Cdd:PRK10551 272 IKRGQFYVEYQPVVDTqTLRVTGLEALLRwrhPTAGEIPpdaFINY-----AEAQKLivpltqHLFELIARDAAELQKV- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 175 ewLPIGVKRFVNFLPSSIYDAQMClshtfNTIDRL--HLDPRDF--VFEVVETEKIDDVEHLQsIFEVYRSHGISVAMDD 250
Cdd:PRK10551 346 --LPVGAKLGINISPAHLHSDSFK-----ADVQRLlaSLPADHFqiVLEITERDMVQEEEATK-LFAWLHSQGIEIAIDD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 251 VGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLF 330
Cdd:PRK10551 418 FGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWI 497
|
...
gi 1288431380 331 GKP 333
Cdd:PRK10551 498 SRP 500
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
211-333 |
1.13e-12 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 69.32 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 211 LDPRDFVFEVVETEKIDDVEHLQSIFEVYRSHGISVAMDDVGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLE 290
Cdd:PRK09776 955 LPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLIS 1034
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1288431380 291 MITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:PRK09776 1035 IIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
210-335 |
7.05e-07 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 51.02 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 210 HLDPRdFVFEVVEtekiDDV----EHLQSIFEVYRSHGISVAMDDVGAGY-STleQMIK-LKPDYVKIDRSLIDHCDRNP 283
Cdd:PRK11059 514 SQRKR-LIFELAE----ADVcqhiSRLRPVLRMLRGLGCRLAVDQAGLTVvST--SYIKeLNVELIKLHPSLVRNIHKRT 586
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1288431380 284 AQQKQLEMITNMAHDFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKPSE 335
Cdd:PRK11059 587 ENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQP 638
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
218-333 |
2.96e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 38.83 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431380 218 FEVVETEKIDDVEHLQSIFEVYRshgisVAMDDVGAGYSTLEQMIKLKPDYVKIDRSLIDHCDRNPAQQKQLEMITNMAH 297
Cdd:PRK11596 132 FELVEHIRLPKDSPFASMCEFGP-----LWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMN 206
|
90 100 110
....*....|....*....|....*....|....*.
gi 1288431380 298 DFGAMVLAEGIERREEFHFCRDIGIELAQGYLFGKP 333
Cdd:PRK11596 207 RYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRP 242
|
|
| |
