|
Name |
Accession |
Description |
Interval |
E-value |
| YkuI_C |
pfam10388 |
EAL-domain associated signalling protein domain; In Bacillus species this highly conserved ... |
264-431 |
6.46e-94 |
|
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: 280.02 E-value: 6.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 264 FLERDVLKQRLKTEFHQFITHEKKKLETVYEHSEQFYKRVHQAVTSLRKNnlSSDDDFIKKLAEELTDCSFRIYMCDEEG 343
Cdd:pfam10388 1 FVERDSLKDKLQKEFHQFIQHEKKKLEAQYELSEQFQQRIHQLLTKLKKT--QDYDELILNLAKELDDCAFRIYICDEDG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 344 DQLTGNVFKQDGEWIYQPEYAEKNWSWRPYFLENIMRMRNLRKGFFSDLYSDLETGEMIRTFSYPMDDQMYLFIDLPYSY 423
Cdd:pfam10388 79 FQQSGNAFKKEGEWILQPEYYMKNWSWRPYFLENIMRMRLEKKGILSDLYTDIETGERIRTYSYPLDDKLYLFIDIPYSY 158
|
....*...
2W27_A 424 LYEQDGLI 431
Cdd:pfam10388 159 LFEQDGLI 166
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
25-260 |
4.73e-61 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 198.21 E-value: 4.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 25 MLDPLDILTNiDDVLPYYQAIFSAEEQKVVGYEVLGRILADsEIQSLGP-FFLDAGIPEEYKLEVDNRIIRQALDRFLEA 103
Cdd:smart00052 1 ERELRQALEN-GQFLLYYQPIVSLRTGRLVGVEALIRWQHP-EGGIISPdEFIPLAEETGLIVPLGRWVLEQACQQLAEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 104 DS----DLLIFMNQDANLLM-LDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNI 178
Cdd:smart00052 79 QAqgppPLLISINLSARQLIsPDLVPRVLELLEET---GLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 179 GKESSNLDRIALLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLV 258
Cdd:smart00052 156 GTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFS 235
|
..
2W27_A 259 SP 260
Cdd:smart00052 236 RP 237
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
36-257 |
1.68e-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: 152.31 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 36 DDVLPYYQAIFSAEEQKVVGYEVLGRIL-ADSEIQSLGPFFldaGIPEEYKL--EVDNRIIRQALD---RFLEADSDLLI 109
Cdd:cd01948 10 GEFELYYQPIVDLRTGRIVGYEALLRWRhPEGGLISPAEFI---PLAEETGLivELGRWVLEEACRqlaRWQAGGPDLRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 110 FMNQDANLLM-LDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRI 188
Cdd:cd01948 87 SVNLSARQLRdPDFLDRLLELLAET---GLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W27_A 189 ALLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYL 257
Cdd:cd01948 164 KRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLF 232
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
36-257 |
1.87e-35 |
|
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: 137.99 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 36 DDVLPYYQAIFSAEEQKVVGYEVLGRIL-ADSEIQSLGPFFldaGIPEEYKL--EVDNRIIRQALD---RFLEADSDLLI 109
Cdd:COG2200 340 GELRLYYQPIVDLRTGRVVGYEALLRWRhPDGGLISPAEFI---PAAERSGLivELDRWVLERALRqlaRWPERGLDLRL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 110 FMNQDANLLM-LDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRI 188
Cdd:COG2200 417 SVNLSARSLLdPDFLERLLELLAEY---GLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W27_A 189 ALLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYL 257
Cdd:COG2200 494 KRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
36-257 |
1.59e-29 |
|
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: 114.72 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 36 DDVLPYYQAIFSAEEQKVVGYEVLGRI-LADSEIQSLGPFFLDAgipEEYKL--EVDNRIIRQALDRFLE--ADSDLLIF 110
Cdd:pfam00563 11 GEFVLYYQPIVDLRTGRVVGYEALLRWqHPDGGLISPARFLPLA---EELGLiaELDRWVLEQALADLAQlqLGPDIKLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 111 MNQDANLLmldHGESFLELLKEYEAKGIELH-RFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRIA 189
Cdd:pfam00563 88 INLSPASL---ADPGFLELLRALLKQAGPPPsRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2W27_A 190 LLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYL 257
Cdd:pfam00563 165 RLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYF 232
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
56-266 |
1.65e-07 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 53.91 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 56 YEVLGRIL-ADSEIQSLGPFfldagIP--EEYKL--EVDNRIIRQALDRFLE--ADSDLLIFMNQDANLLmldhGESFL- 127
Cdd:PRK09776 873 WLISLRLWdPEGEIIDEGAF-----RPaaEDPALmhALDRRVIHEFFRQAAKavASKGLSIALPLSVAGL----SSPTLl 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 128 -ELLKEYEAKGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGkesSNLDRIALLSP---DLLKIDLQAL 203
Cdd:PRK09776 944 pFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFG---RGLSSFNYLKAfmaDYLKLDGELV 1020
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
2W27_A 204 KVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLVSPS--ETFLE 266
Cdd:PRK09776 1021 ANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQplDLLLN 1085
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YkuI_C |
pfam10388 |
EAL-domain associated signalling protein domain; In Bacillus species this highly conserved ... |
264-431 |
6.46e-94 |
|
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: 280.02 E-value: 6.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 264 FLERDVLKQRLKTEFHQFITHEKKKLETVYEHSEQFYKRVHQAVTSLRKNnlSSDDDFIKKLAEELTDCSFRIYMCDEEG 343
Cdd:pfam10388 1 FVERDSLKDKLQKEFHQFIQHEKKKLEAQYELSEQFQQRIHQLLTKLKKT--QDYDELILNLAKELDDCAFRIYICDEDG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 344 DQLTGNVFKQDGEWIYQPEYAEKNWSWRPYFLENIMRMRNLRKGFFSDLYSDLETGEMIRTFSYPMDDQMYLFIDLPYSY 423
Cdd:pfam10388 79 FQQSGNAFKKEGEWILQPEYYMKNWSWRPYFLENIMRMRLEKKGILSDLYTDIETGERIRTYSYPLDDKLYLFIDIPYSY 158
|
....*...
2W27_A 424 LYEQDGLI 431
Cdd:pfam10388 159 LFEQDGLI 166
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
25-260 |
4.73e-61 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 198.21 E-value: 4.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 25 MLDPLDILTNiDDVLPYYQAIFSAEEQKVVGYEVLGRILADsEIQSLGP-FFLDAGIPEEYKLEVDNRIIRQALDRFLEA 103
Cdd:smart00052 1 ERELRQALEN-GQFLLYYQPIVSLRTGRLVGVEALIRWQHP-EGGIISPdEFIPLAEETGLIVPLGRWVLEQACQQLAEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 104 DS----DLLIFMNQDANLLM-LDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNI 178
Cdd:smart00052 79 QAqgppPLLISINLSARQLIsPDLVPRVLELLEET---GLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 179 GKESSNLDRIALLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLV 258
Cdd:smart00052 156 GTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFS 235
|
..
2W27_A 259 SP 260
Cdd:smart00052 236 RP 237
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
36-257 |
1.68e-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: 152.31 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 36 DDVLPYYQAIFSAEEQKVVGYEVLGRIL-ADSEIQSLGPFFldaGIPEEYKL--EVDNRIIRQALD---RFLEADSDLLI 109
Cdd:cd01948 10 GEFELYYQPIVDLRTGRIVGYEALLRWRhPEGGLISPAEFI---PLAEETGLivELGRWVLEEACRqlaRWQAGGPDLRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 110 FMNQDANLLM-LDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRI 188
Cdd:cd01948 87 SVNLSARQLRdPDFLDRLLELLAET---GLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W27_A 189 ALLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYL 257
Cdd:cd01948 164 KRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLF 232
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
36-257 |
1.87e-35 |
|
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: 137.99 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 36 DDVLPYYQAIFSAEEQKVVGYEVLGRIL-ADSEIQSLGPFFldaGIPEEYKL--EVDNRIIRQALD---RFLEADSDLLI 109
Cdd:COG2200 340 GELRLYYQPIVDLRTGRVVGYEALLRWRhPDGGLISPAEFI---PAAERSGLivELDRWVLERALRqlaRWPERGLDLRL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 110 FMNQDANLLM-LDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRI 188
Cdd:COG2200 417 SVNLSARSLLdPDFLERLLELLAEY---GLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W27_A 189 ALLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYL 257
Cdd:COG2200 494 KRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
36-257 |
1.59e-29 |
|
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: 114.72 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 36 DDVLPYYQAIFSAEEQKVVGYEVLGRI-LADSEIQSLGPFFLDAgipEEYKL--EVDNRIIRQALDRFLE--ADSDLLIF 110
Cdd:pfam00563 11 GEFVLYYQPIVDLRTGRVVGYEALLRWqHPDGGLISPARFLPLA---EELGLiaELDRWVLEQALADLAQlqLGPDIKLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 111 MNQDANLLmldHGESFLELLKEYEAKGIELH-RFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRIA 189
Cdd:pfam00563 88 INLSPASL---ADPGFLELLRALLKQAGPPPsRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2W27_A 190 LLSPDLLKIDLQALKVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYL 257
Cdd:pfam00563 165 RLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYF 232
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
56-266 |
1.65e-07 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 53.91 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 56 YEVLGRIL-ADSEIQSLGPFfldagIP--EEYKL--EVDNRIIRQALDRFLE--ADSDLLIFMNQDANLLmldhGESFL- 127
Cdd:PRK09776 873 WLISLRLWdPEGEIIDEGAF-----RPaaEDPALmhALDRRVIHEFFRQAAKavASKGLSIALPLSVAGL----SSPTLl 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 128 -ELLKEYEAKGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGkesSNLDRIALLSP---DLLKIDLQAL 203
Cdd:PRK09776 944 pFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFG---RGLSSFNYLKAfmaDYLKLDGELV 1020
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
2W27_A 204 KVSQPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLVSPS--ETFLE 266
Cdd:PRK09776 1021 ANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQplDLLLN 1085
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
42-260 |
4.12e-07 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 51.92 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 42 YQAIFSAEEQKVVGYEVLGRILADSEiqslGPFFLDAGIP--EEYKLEVD------NRIIRQA--LDRFLEADSDLLIfm 111
Cdd:PRK10551 281 YQPVVDTQTLRVTGLEALLRWRHPTA----GEIPPDAFINyaEAQKLIVPltqhlfELIARDAaeLQKVLPVGAKLGI-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 112 NQDANLLmldHGESFLELLKEYEAKgIELHRF--VLEITEHNF--EGDIEQLYHMLayyRTYGIKIAVDNIGKESSNLDR 187
Cdd:PRK10551 355 NISPAHL---HSDSFKADVQRLLAS-LPADHFqiVLEITERDMvqEEEATKLFAWL---HSQGIEIAIDDFGTGHSALIY 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W27_A 188 IALLSPDLLKID---LQAL---KVSQPspsyehVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLVSP 260
Cdd:PRK10551 428 LERFTLDYLKIDrgfIQAIgteTVTSP------VLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
43-260 |
7.08e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 50.96 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 43 QAIFSAEeQKVVGYEVLGRiladseiQSLGPFFldagiPEEYKLEVDNRIIrqaLDRFLEADSDLLI-----FMNQDANL 117
Cdd:COG3434 9 QPILDRD-QRVVGYELLFR-------SGLENSA-----PDVDGDQATARVL---LNAFLEIGLDRLLggklaFINFTEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 118 LMLDhgesFLELLKEyeakgielHRFVLEITEhNFEGDiEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRIALLspDLLK 197
Cdd:COG3434 73 LLSD----LPELLPP--------ERVVLEILE-DVEPD-EELLEALKELKEKGYRIALDDFVLDPEWDPLLPLA--DIIK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
2W27_A 198 IDLQALKVSQPSPSYEHVL-YSISLLARKIgaallyEDIEanfQLQYAWRNGGRYFQGYYLVSP 260
Cdd:COG3434 137 IDVLALDLEELAELVARLKrYGIKLLAEKV------ETRE---EFELCKELGFDLFQGYFFSKP 191
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
117-267 |
9.10e-06 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 47.79 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 117 LLMLDHGESFLELLKEYeakGIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSN---LDRIALLSP 193
Cdd:PRK13561 497 LMHPNMVADMLELLTRY---RIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGlrqLQHMKSLPI 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W27_A 194 DLLKID---LQALkvsqpsPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLVS--PSETFLER 267
Cdd:PRK13561 574 DVLKIDkmfVDGL------PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARalPIEIFEER 646
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
27-272 |
2.68e-05 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 46.47 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 27 DPLDILTNIDDVLpYYQAIFSAEEQKVVGYEVLGRILAD----SEIQSLGPFFLDAG--IP-EEYKLEVDNRIIRQALDR 99
Cdd:PRK11829 409 DLLQAIENHDFTL-FLQPQWDMKRQQVIGAEALLRWCQPdgsyVLPSGFVHFAEEEGmmVPlGNWVLEEACRILADWKAR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 100 FLEADSDLLIFMNQDANLLMLDHGESfleLLKEYEakgIELHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIG 179
Cdd:PRK11829 488 GVSLPLSVNISGLQVQNKQFLPHLKT---LISHYH---IDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFG 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 180 KESSNLD---RIALLSPDLLKIDLQALKvsqPSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYY 256
Cdd:PRK11829 562 IGYSSLRylnHLKSLPIHMIKLDKSFVK---NLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFL 638
|
250
....*....|....*.
2W27_A 257 LvspSETFLERDVLKQ 272
Cdd:PRK11829 639 F---SPPLPRAEFEAQ 651
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
128-260 |
9.70e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 38.21 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W27_A 128 ELLKEYEAKGielHRFVLEITEHNFEGDIEQLYHMLAYYRTYGIKIAVDNIGKESSNLDRIALLSPDLLKIDLQALKVSQ 207
Cdd:PRK11359 652 DAMQAWGIDG---HQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCL 728
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
2W27_A 208 PSPSYEHVLYSISLLARKIGAALLYEDIEANFQLQYAWRNGGRYFQGYYLVSP 260
Cdd:PRK11359 729 TEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| |
