|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
9-261 |
1.25e-45 |
|
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: 166.11 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 9 KLEWDLW--FQSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPFFlnalsgveDLQERREiyiLKRDIDRSI 86
Cdd:COG2200 328 ALESELReaLEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFI--------PAAERSG---LIVELDRWV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 87 RKKALLHLLKNQNRFPEAKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYK 166
Cdd:COG2200 397 LERALRQLARWPERGLDLRLSVNLSAR----SLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 167 EEGFLVAIDDLGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTY 246
Cdd:COG2200 473 ALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALREL 552
|
250
....*....|....*
gi 446501596 247 SARFLQGFYFAEALP 261
Cdd:COG2200 553 GCDYAQGYLFGRPLP 567
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
17-261 |
1.18e-43 |
|
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: 152.70 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 17 QSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPFFLNAlsgvedlqerrEIYILKRDIDRSIRKKALLHLLK 96
Cdd:cd01948 8 ERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLA-----------EETGLIVELGRWVLEEACRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 97 NQNRFPEAKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAIDD 176
Cdd:cd01948 77 WQAGGPDLRLSVNLSAR----QLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 177 LGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQGFYF 256
Cdd:cd01948 153 FGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLF 232
|
....*
gi 446501596 257 AEALP 261
Cdd:cd01948 233 SRPLP 237
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
16-259 |
8.77e-37 |
|
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: 134.37 E-value: 8.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 16 FQSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPFFlnalSGVEDLQerreiyiLKRDIDRSIRKKALLhLL 95
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFL----PLAEELG-------LIAELDRWVLEQALA-DL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 96 KNQNRFPEAKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAID 175
Cdd:pfam00563 76 AQLQLGPDIKLSINLSPA----SLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 176 DLGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQGFY 255
Cdd:pfam00563 152 DFGTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYY 231
|
....
gi 446501596 256 FAEA 259
Cdd:pfam00563 232 FSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
19-261 |
9.07e-26 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 104.61 E-value: 9.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 19 GEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIhsLGP-FFLNALSGVEdlqerreiyiLKRDIDRSIRKKALLHLLKN 97
Cdd:smart00052 11 GQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGI--ISPdEFIPLAEETG----------LIVPLGRWVLEQACQQLAEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 98 QNRFPEAKLF-VNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAIDD 176
Cdd:smart00052 79 QAQGPPPLLIsINLSAR----QLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 177 LGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQGFYF 256
Cdd:smart00052 155 FGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLF 234
|
....*
gi 446501596 257 AEALP 261
Cdd:smart00052 235 SRPLP 239
|
|
| YkuI_C |
pfam10388 |
EAL-domain associated signalling protein domain; In Bacillus species this highly conserved ... |
280-418 |
1.48e-12 |
|
EAL-domain associated signalling protein domain; In Bacillus species this highly conserved region of the YkuI protein lies immediately downstream of the EAL (diguanylate cyclase/phosphodiesterase domain 2) pfam00563 domain so that together they form a monomer which dimerizes for its enzymatic action. The region contains three alpha helices and five beta strands and is the C-terminal half of the structure.
Pssm-ID: 402144 Cd Length: 166 Bit Score: 65.46 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 280 FLNHKRNQLVKRIQLEKELEEKLdlsGIIVNAEEELCSIQ--IQNPNL-LSNFVFRIYATNLIGSQVSPNYMKIGNSSId 356
Cdd:pfam10388 18 FIQHEKKKLEAQYELSEQFQQRI---HQLLTKLKKTQDYDelILNLAKeLDDCAFRIYICDEDGFQQSGNAFKKEGEWI- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446501596 357 IDSSFVGRNWSWRPYFLEQLYKSMKDTRAewIISNPYYDISYGILLVTYSKKISEQNVLFVD 418
Cdd:pfam10388 94 LQPEYYMKNWSWRPYFLENIMRMRLEKKG--ILSDLYTDIETGERIRTYSYPLDDKLYLFID 153
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
17-261 |
3.15e-09 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 58.80 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 17 QSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPF--FLNALSGVEDLQErreiYILKrdidrsirkKALLHL 94
Cdd:PRK11829 415 ENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFvhFAEEEGMMVPLGN----WVLE---------EACRIL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 95 LKNQNRFPEAKLFVNISPAYMRDhieeEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAI 174
Cdd:PRK11829 482 ADWKARGVSLPLSVNISGLQVQN----KQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIAL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 175 DDLGSRSSNLDRIGifHPDILKVDLQMLRHSVIsRNFQE---ILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFL 251
Cdd:PRK11829 558 DDFGIGYSSLRYLN--HLKSLPIHMIKLDKSFV-KNLPEddaIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCG 634
|
250
....*....|
gi 446501596 252 QGFYFAEALP 261
Cdd:PRK11829 635 QGFLFSPPLP 644
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
9-261 |
1.25e-45 |
|
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: 166.11 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 9 KLEWDLW--FQSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPFFlnalsgveDLQERREiyiLKRDIDRSI 86
Cdd:COG2200 328 ALESELReaLEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFI--------PAAERSG---LIVELDRWV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 87 RKKALLHLLKNQNRFPEAKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYK 166
Cdd:COG2200 397 LERALRQLARWPERGLDLRLSVNLSAR----SLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 167 EEGFLVAIDDLGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTY 246
Cdd:COG2200 473 ALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALREL 552
|
250
....*....|....*
gi 446501596 247 SARFLQGFYFAEALP 261
Cdd:COG2200 553 GCDYAQGYLFGRPLP 567
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
17-261 |
1.18e-43 |
|
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: 152.70 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 17 QSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPFFLNAlsgvedlqerrEIYILKRDIDRSIRKKALLHLLK 96
Cdd:cd01948 8 ERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLA-----------EETGLIVELGRWVLEEACRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 97 NQNRFPEAKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAIDD 176
Cdd:cd01948 77 WQAGGPDLRLSVNLSAR----QLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 177 LGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQGFYF 256
Cdd:cd01948 153 FGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLF 232
|
....*
gi 446501596 257 AEALP 261
Cdd:cd01948 233 SRPLP 237
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
16-259 |
8.77e-37 |
|
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: 134.37 E-value: 8.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 16 FQSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPFFlnalSGVEDLQerreiyiLKRDIDRSIRKKALLhLL 95
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFL----PLAEELG-------LIAELDRWVLEQALA-DL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 96 KNQNRFPEAKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAID 175
Cdd:pfam00563 76 AQLQLGPDIKLSINLSPA----SLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 176 DLGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQGFY 255
Cdd:pfam00563 152 DFGTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYY 231
|
....
gi 446501596 256 FAEA 259
Cdd:pfam00563 232 FSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
19-261 |
9.07e-26 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 104.61 E-value: 9.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 19 GEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIhsLGP-FFLNALSGVEdlqerreiyiLKRDIDRSIRKKALLHLLKN 97
Cdd:smart00052 11 GQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGI--ISPdEFIPLAEETG----------LIVPLGRWVLEQACQQLAEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 98 QNRFPEAKLF-VNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAIDD 176
Cdd:smart00052 79 QAQGPPPLLIsINLSAR----QLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 177 LGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQGFYF 256
Cdd:smart00052 155 FGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLF 234
|
....*
gi 446501596 257 AEALP 261
Cdd:smart00052 235 SRPLP 239
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
19-261 |
3.80e-18 |
|
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: 86.75 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 19 GEIVPFFQPILSVERDSIFGYETLGRFRD----------------QSGKIHSLGPFFLN-ALSGVEDLQERReiyilkrd 81
Cdd:COG5001 437 GELELHYQPQVDLATGRIVGAEALLRWQHperglvspaefiplaeETGLIVPLGEWVLReACRQLAAWQDAG-------- 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 82 idrsirkkallhllknqnrFPEAKLFVNISPAYMRDHIEEEEVDpytiRLVKEFGLDPSKIVIEIVE----EHFDGSIES 157
Cdd:COG5001 509 -------------------LPDLRVAVNLSARQLRDPDLVDRVR----RALAETGLPPSRLELEITEsallEDPEEALET 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 158 LRPLisryKEEGFLVAIDDLGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENE 237
Cdd:COG5001 566 LRAL----RALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETE 641
|
250 260
....*....|....*....|....
gi 446501596 238 TELFQSLTYSARFLQGFYFAEALP 261
Cdd:COG5001 642 EQLEFLRELGCDYAQGYLFSRPLP 665
|
|
| YkuI_C |
pfam10388 |
EAL-domain associated signalling protein domain; In Bacillus species this highly conserved ... |
280-418 |
1.48e-12 |
|
EAL-domain associated signalling protein domain; In Bacillus species this highly conserved region of the YkuI protein lies immediately downstream of the EAL (diguanylate cyclase/phosphodiesterase domain 2) pfam00563 domain so that together they form a monomer which dimerizes for its enzymatic action. The region contains three alpha helices and five beta strands and is the C-terminal half of the structure.
Pssm-ID: 402144 Cd Length: 166 Bit Score: 65.46 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 280 FLNHKRNQLVKRIQLEKELEEKLdlsGIIVNAEEELCSIQ--IQNPNL-LSNFVFRIYATNLIGSQVSPNYMKIGNSSId 356
Cdd:pfam10388 18 FIQHEKKKLEAQYELSEQFQQRI---HQLLTKLKKTQDYDelILNLAKeLDDCAFRIYICDEDGFQQSGNAFKKEGEWI- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446501596 357 IDSSFVGRNWSWRPYFLEQLYKSMKDTRAewIISNPYYDISYGILLVTYSKKISEQNVLFVD 418
Cdd:pfam10388 94 LQPEYYMKNWSWRPYFLENIMRMRLEKKG--ILSDLYTDIETGERIRTYSYPLDDKLYLFID 153
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
17-261 |
3.15e-09 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 58.80 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 17 QSGEIVPFFQPILSVERDSIFGYETLGRFRDQSGKIHSLGPF--FLNALSGVEDLQErreiYILKrdidrsirkKALLHL 94
Cdd:PRK11829 415 ENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFvhFAEEEGMMVPLGN----WVLE---------EACRIL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 95 LKNQNRFPEAKLFVNISPAYMRDhieeEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAI 174
Cdd:PRK11829 482 ADWKARGVSLPLSVNISGLQVQN----KQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIAL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 175 DDLGSRSSNLDRIGifHPDILKVDLQMLRHSVIsRNFQE---ILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFL 251
Cdd:PRK11829 558 DDFGIGYSSLRYLN--HLKSLPIHMIKLDKSFV-KNLPEddaIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCG 634
|
250
....*....|
gi 446501596 252 QGFYFAEALP 261
Cdd:PRK11829 635 QGFLFSPPLP 644
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
24-261 |
9.51e-09 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 57.42 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 24 FFQPILSVERDSIFGYETLGRFRDQSGkihslgpfflnALSGVEDLQERREIYILKRDIDRSIRKKALLHLLKNQNRFPE 103
Cdd:PRK13561 417 WLQPQVEMRSGKLVSAEALLRMQQPDG-----------SWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIM 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 104 AKLFVNISPAYMRdhieEEEVDPYTIRLVKEFGLDPSKIVIEIVE----EHFDGSIESLRPLisryKEEGFLVAIDDLGS 179
Cdd:PRK13561 486 LPLSVNLSALQLM----HPNMVADMLELLTRYRIQPGTLILEVTEsrriDDPHAAVAILRPL----RNAGVRVALDDFGM 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 180 RSSNLDRIGIFHP---DILKVD---LQML--RHSVISrnfqeilfTISRLSESLGCSLLFEGIENETELFQSLTYSARFL 251
Cdd:PRK13561 558 GYAGLRQLQHMKSlpiDVLKIDkmfVDGLpeDDSMVA--------AIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIA 629
|
250
....*....|
gi 446501596 252 QGFYFAEALP 261
Cdd:PRK13561 630 QGFLFARALP 639
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
132-261 |
8.52e-07 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 51.22 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 132 VKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLVAIDDLGSRSSNLDRIGIFHPDILKVDLQMLRHsvISRN- 210
Cdd:PRK10060 517 LQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRD--IHKQp 594
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 211 -FQEILFTISRLSESLGCSLLFEGIENETElfqsltysARFL--------QGFYFAEALP 261
Cdd:PRK10060 595 vSQSLVRAIVAVAQALNLQVIAEGVETAKE--------DAFLtkngvnerQGFLFAKPMP 646
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
18-261 |
1.76e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 50.15 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 18 SGEIVPFFQPILSVERDSIFGYETLGRFRD-QSGKIhSLGPFflnaLSGVEDLQERREI-YILKRDIDRSI---RKKALl 92
Cdd:PRK11359 554 NNQLKLVYQPQIFAETGELYGIEALARWHDpLHGHV-PPSRF----IPLAEEIGEIENIgRWVIAEACRQLaewRSQNI- 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 93 hllknqnRFPeaKLFVNISPAymrdHIEEEEVDPYTIRLVKEFGLDPSKIVIEIVEEHFDGSIESLRPLISRYKEEGFLV 172
Cdd:PRK11359 628 -------HIP--ALSVNLSAL----HFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 173 AIDDLGSRSSNLDRIGIFHPDILKVDLQMLRHSVISRNFQEILFTISRLSESLGCSLLFEGIENETELFQSLTYSARFLQ 252
Cdd:PRK11359 695 SVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQ 774
|
....*....
gi 446501596 253 GFYFAEALP 261
Cdd:PRK11359 775 GYFFSRPLP 783
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
25-261 |
4.38e-05 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 45.75 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 25 FQPILSVERDSIFGYETLGRFRDQS-GKIhslgP--FFLNALSGvedlqeRREIYILKRDIDRSIRKKAllHLLknQNRF 101
Cdd:PRK10551 281 YQPVVDTQTLRVTGLEALLRWRHPTaGEI----PpdAFINYAEA------QKLIVPLTQHLFELIARDA--AEL--QKVL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 102 PE-AKLFVNISPAYMRDHIEEEEVdpytIRLVKEFGLDPSKIVIEIVEehfdgsieslRPLISRYK---------EEGFL 171
Cdd:PRK10551 347 PVgAKLGINISPAHLHSDSFKADV----QRLLASLPADHFQIVLEITE----------RDMVQEEEatklfawlhSQGIE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446501596 172 VAIDDLGSRSSNLDRIGIFHPDILKVDlqmlrhsvisRNF-QEI---------LFTISRLSESLGCSLLFEGIENETELF 241
Cdd:PRK10551 413 IAIDDFGTGHSALIYLERFTLDYLKID----------RGFiQAIgtetvtspvLDAVLTLAKRLNMLTVAEGVETPEQAR 482
|
250 260
....*....|....*....|
gi 446501596 242 QSLTYSARFLQGFYFAEALP 261
Cdd:PRK10551 483 WLRERGVNFLQGYWISRPLP 502
|
|
| |
