|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
497-735 |
1.96e-90 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 282.95 E-value: 1.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 497 MNRLQQALEHNHFFLMAQPITGMRG--DVYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRA 574
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTgrLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 575 KMPAH-RFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYA 653
Cdd:smart00052 81 QGPPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 654 SYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPL 733
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 16130428 734 ID 735
Cdd:smart00052 241 DD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
498-733 |
3.96e-85 |
|
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: 269.03 E-value: 3.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 498 NRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAK 575
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGriVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 576 MPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASY 655
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130428 656 ARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPL 733
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
246-735 |
1.96e-83 |
|
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: 276.28 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 246 TLSLLLPLMMWGAMRYGYKLISLLWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNYMAVLATRQRAVVRR 325
Cdd:COG2200 75 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 326 IQRLAYVDPVVHLPNVRALNRALRDAPWSALCYLRIPGMEMLVKNYGIMLRIQYK-----QKLSHWLSPLLEPGEDVYQL 400
Cdd:COG2200 155 LLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLlllllLALLLLLLLARLLLALLGGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 401 SGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSYCYVRSPVNHIYLLLgELNTVAELSIVTNAPENMQR 480
Cdd:COG2200 235 GGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAAL-LLAAAAAAAAAAAGGGRGRV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 481 RGAMYLQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSID 558
Cdd:COG2200 314 VFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGrvVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELD 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 559 MWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQE 638
Cdd:COG2200 394 RWVLERALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 639 LGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLG 718
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
490
....*....|....*..
gi 16130428 719 IDYMQGYLIGKPQPLID 735
Cdd:COG2200 554 CDYAQGYLFGRPLPLEE 570
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
497-730 |
1.04e-77 |
|
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: 249.54 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 497 MNRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAEnRA 574
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGrvVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 575 KMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYAS 654
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130428 655 YARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKP 730
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
486-732 |
2.93e-70 |
|
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: 243.14 E-value: 2.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 486 LQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMR-GDVYH-EILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIE 563
Cdd:COG5001 416 MDERARERLELEADLRRALERGELELHYQPQVDLAtGRIVGaEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLR 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 564 HTLQFMAE-NRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQ 642
Cdd:COG5001 496 EACRQLAAwQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVR 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 643 IAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYM 722
Cdd:COG5001 576 IALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYA 655
|
250
....*....|
gi 16130428 723 QGYLIGKPQP 732
Cdd:COG5001 656 QGYLFSRPLP 665
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
15-320 |
3.73e-54 |
|
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins. This entry also includes members of the 8 transmembrane UhpB type (8TMR-UT) domain family.
Pssm-ID: 428383 [Multi-domain] Cd Length: 299 Bit Score: 188.78 E-value: 3.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 15 WGLPLFLPSLILPIFAHINTFAHISSGeVFLFYLPLALMISMMMFFSWAALPGIALGIFVRK-----YAELGFYETLSLT 89
Cdd:pfam05231 1 LLLLLLLLYALLAAVSLSLALALVSSG-SAPIWLPTGLALAALLLFGRRGWPGILLGAVLASlmaglLSGLNLLLALAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 90 ANFIIIIILCWGGYRVFTPRRNNVSHGdtrlisqrIFWQIVFPATLFLILFQFAAFVGLLASRENLVGVMPFNLGTLINY 169
Cdd:pfam05231 80 AVNALEALLGAALLRRLLPGRNRLQRL--------RFWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 170 QALLVGNLIGVPLCYFIIRVVRNPFYLRSYYSQLKQQVDAKVTKKEFALWLLALGALLLLLCMPlNEKSTIFstnytlSL 249
Cdd:pfam05231 152 LGSATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMP-EINYPLG------YL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130428 250 LLPLMMWGAMRYGYKLISL---LWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNY-MAVLATRQR 320
Cdd:pfam05231 225 LLPPLLWAAFRFGVRGGSLaalLLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALlVSAAISEQR 299
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
317-739 |
1.76e-40 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 160.22 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 317 TRQRAVVRRIQRLAYVDPVVHLPNvRA-----LNRALRDA----PWSALCYLRIPGMEMLVKNYG-----IMLRiqykqK 382
Cdd:PRK09776 652 TESRKMLRQLSYSASHDALTHLAN-RAsfekqLRRLLQTVnsthQRHALVFIDLDRFKAVNDSAGhaagdALLR-----E 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 383 LSHWLSPLLEPGEDVYQLSGNDLALRL---NTESHQERITALDSHLKQFRFFWDGMPMQpqIGVSYcyvrspvnHIYLLL 459
Cdd:PRK09776 726 LASLMLSMLRSSDVLARLGGDEFGLLLpdcNVESARFIATRIISAINDYHFPWEGRVYR--VGASA--------GITLID 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 460 GELNTVAEL----SIVTNAPENMQR-RGAMYLQRE--LKDKVAMMNRLQQ---ALEHNHFFLMAQPIT--GMRGDVYHEI 527
Cdd:PRK09776 796 ANNHQASEVmsqaDIACYAAKNAGRgRVTVYEPQQaaAHSEHRALSLAEQwrmIKENQLMMLAHGVASprIPEARNHWLI 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 528 LLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKmPAHRFAINLSPTSVCQARFPVEVSQLLAKYQ 607
Cdd:PRK09776 876 SLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS-KGLSIALPLSVAGLSSPTLLPFLLEQLENSP 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 608 IEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVA 687
Cdd:PRK09776 955 LPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLIS 1034
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16130428 688 SICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPLIDTLNE 739
Cdd:PRK09776 1035 IIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNS 1086
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
328-480 |
9.05e-24 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 98.47 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 328 RLAYVDPVVHLPNVRALNRAL--------RDAPWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSHWLSPLLEPGEDVYQ 399
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELeqelqraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 400 LSGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSY--CYVRSPVNHIYLLLGELNTVAELSIVTNAPEN 477
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIgvAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 16130428 478 MQR 480
Cdd:smart00267 161 AVY 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
497-735 |
1.96e-90 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 282.95 E-value: 1.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 497 MNRLQQALEHNHFFLMAQPITGMRG--DVYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRA 574
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTgrLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 575 KMPAH-RFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYA 653
Cdd:smart00052 81 QGPPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 654 SYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPL 733
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 16130428 734 ID 735
Cdd:smart00052 241 DD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
498-733 |
3.96e-85 |
|
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: 269.03 E-value: 3.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 498 NRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAK 575
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGriVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 576 MPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASY 655
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130428 656 ARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPL 733
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
246-735 |
1.96e-83 |
|
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: 276.28 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 246 TLSLLLPLMMWGAMRYGYKLISLLWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNYMAVLATRQRAVVRR 325
Cdd:COG2200 75 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 326 IQRLAYVDPVVHLPNVRALNRALRDAPWSALCYLRIPGMEMLVKNYGIMLRIQYK-----QKLSHWLSPLLEPGEDVYQL 400
Cdd:COG2200 155 LLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLlllllLALLLLLLLARLLLALLGGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 401 SGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSYCYVRSPVNHIYLLLgELNTVAELSIVTNAPENMQR 480
Cdd:COG2200 235 GGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAAL-LLAAAAAAAAAAAGGGRGRV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 481 RGAMYLQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSID 558
Cdd:COG2200 314 VFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGrvVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELD 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 559 MWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQE 638
Cdd:COG2200 394 RWVLERALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 639 LGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLG 718
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
490
....*....|....*..
gi 16130428 719 IDYMQGYLIGKPQPLID 735
Cdd:COG2200 554 CDYAQGYLFGRPLPLEE 570
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
497-730 |
1.04e-77 |
|
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: 249.54 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 497 MNRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAEnRA 574
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGrvVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQ-LQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 575 KMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYAS 654
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130428 655 YARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKP 730
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
486-732 |
2.93e-70 |
|
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: 243.14 E-value: 2.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 486 LQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMR-GDVYH-EILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIE 563
Cdd:COG5001 416 MDERARERLELEADLRRALERGELELHYQPQVDLAtGRIVGaEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLR 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 564 HTLQFMAE-NRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQ 642
Cdd:COG5001 496 EACRQLAAwQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVR 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 643 IAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYM 722
Cdd:COG5001 576 IALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYA 655
|
250
....*....|
gi 16130428 723 QGYLIGKPQP 732
Cdd:COG5001 656 QGYLFSRPLP 665
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
15-320 |
3.73e-54 |
|
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins. This entry also includes members of the 8 transmembrane UhpB type (8TMR-UT) domain family.
Pssm-ID: 428383 [Multi-domain] Cd Length: 299 Bit Score: 188.78 E-value: 3.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 15 WGLPLFLPSLILPIFAHINTFAHISSGeVFLFYLPLALMISMMMFFSWAALPGIALGIFVRK-----YAELGFYETLSLT 89
Cdd:pfam05231 1 LLLLLLLLYALLAAVSLSLALALVSSG-SAPIWLPTGLALAALLLFGRRGWPGILLGAVLASlmaglLSGLNLLLALAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 90 ANFIIIIILCWGGYRVFTPRRNNVSHGdtrlisqrIFWQIVFPATLFLILFQFAAFVGLLASRENLVGVMPFNLGTLINY 169
Cdd:pfam05231 80 AVNALEALLGAALLRRLLPGRNRLQRL--------RFWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 170 QALLVGNLIGVPLCYFIIRVVRNPFYLRSYYSQLKQQVDAKVTKKEFALWLLALGALLLLLCMPlNEKSTIFstnytlSL 249
Cdd:pfam05231 152 LGSATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMP-EINYPLG------YL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130428 250 LLPLMMWGAMRYGYKLISL---LWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNY-MAVLATRQR 320
Cdd:pfam05231 225 LLPPLLWAAFRFGVRGGSLaalLLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALlVSAAISEQR 299
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
498-732 |
9.10e-50 |
|
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: 182.81 E-value: 9.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 498 NRLQQALEHNHFFLMAQPI--------TGMrgdvyhEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFM 569
Cdd:COG4943 274 RRLRRAIKRREFYVHYQPIvdlktgrcVGA------EALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 570 AENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALtNVKQAQITLQHLQELGCQIAIDDFG 649
Cdd:COG4943 348 GDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFG 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 650 TGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGK 729
Cdd:COG4943 427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506
|
...
gi 16130428 730 PQP 732
Cdd:COG4943 507 PLP 509
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
317-739 |
1.76e-40 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 160.22 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 317 TRQRAVVRRIQRLAYVDPVVHLPNvRA-----LNRALRDA----PWSALCYLRIPGMEMLVKNYG-----IMLRiqykqK 382
Cdd:PRK09776 652 TESRKMLRQLSYSASHDALTHLAN-RAsfekqLRRLLQTVnsthQRHALVFIDLDRFKAVNDSAGhaagdALLR-----E 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 383 LSHWLSPLLEPGEDVYQLSGNDLALRL---NTESHQERITALDSHLKQFRFFWDGMPMQpqIGVSYcyvrspvnHIYLLL 459
Cdd:PRK09776 726 LASLMLSMLRSSDVLARLGGDEFGLLLpdcNVESARFIATRIISAINDYHFPWEGRVYR--VGASA--------GITLID 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 460 GELNTVAEL----SIVTNAPENMQR-RGAMYLQRE--LKDKVAMMNRLQQ---ALEHNHFFLMAQPIT--GMRGDVYHEI 527
Cdd:PRK09776 796 ANNHQASEVmsqaDIACYAAKNAGRgRVTVYEPQQaaAHSEHRALSLAEQwrmIKENQLMMLAHGVASprIPEARNHWLI 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 528 LLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKmPAHRFAINLSPTSVCQARFPVEVSQLLAKYQ 607
Cdd:PRK09776 876 SLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS-KGLSIALPLSVAGLSSPTLLPFLLEQLENSP 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 608 IEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVA 687
Cdd:PRK09776 955 LPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLIS 1034
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16130428 688 SICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPLIDTLNE 739
Cdd:PRK09776 1035 IIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNS 1086
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
317-732 |
1.35e-37 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 149.83 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 317 TRQRAVVRRIQRLAYVDPVVHLPNVRALNRALRDAPWSA------LCYLRIPGMEMLVKNYGIMLRIQYKQKLSHWLSPL 390
Cdd:PRK10060 224 TEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAAdnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSC 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 391 LEPGEDVYQLSGNDLaLRLNTESHQERITALDS----HLKQ-FRFFWD--------GMPMQPQIGVSY-CYVRSPVNHIY 456
Cdd:PRK10060 304 LEEDQTLARLGGDEF-LVLASHTSQAALEAMASriltRLRLpFRIGLIevytgcsiGIALAPEHGDDSeSLIRSADTAMY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 457 lllgelnTVAELSIVTN---APEnMQRRGAMYLQRElkdkvammNRLQQALEHNHFFLMAQPITGMRGDVYH-EILLRMK 532
Cdd:PRK10060 383 -------TAKEGGRGQFcvfSPE-MNQRVFEYLWLD--------TNLRKALENDQLVIHYQPKITWRGEVRSlEALVRWQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 533 GENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQ 612
Cdd:PRK10060 447 SPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 613 LIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHL 692
Cdd:PRK10060 527 IDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAV 606
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16130428 693 ARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQP 732
Cdd:PRK10060 607 AQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMP 646
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
483-733 |
2.86e-35 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 142.55 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 483 AMYLQRELKDKV-----AMMNRLQ----------QALEHNHFFLMAQPITGMR-GDVYH-EILLRMKGENDELISPDSFL 545
Cdd:PRK13561 373 AFTARRKGKNQIqffdpQQMEAAQkrlteesdilNALENHQFAIWLQPQVEMRsGKLVSaEALLRMQQPDGSWDLPEGLI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 546 PVAHEFGLSSSIDMWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTN 625
Cdd:PRK13561 453 DRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDD 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 626 VKQAQITLQHLQELGCQIAIDDFGTGYASYARL---KNVNADLLKIDGSFIRNIvsnSLDYQIVASICHLARMKKMLVVA 702
Cdd:PRK13561 533 PHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIA 609
|
250 260 270
....*....|....*....|....*....|.
gi 16130428 703 EYVENEEIREAVLSLGIDYMQGYLIGKPQPL 733
Cdd:PRK13561 610 EGVETEAQRDWLLKAGVGIAQGFLFARALPI 640
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
486-737 |
9.14e-33 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 135.07 E-value: 9.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 486 LQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMRGD--VYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIE 563
Cdd:PRK11829 396 LIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQqvIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 564 HTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQI 643
Cdd:PRK11829 476 EACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLI 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 644 AIDDFGTGYAS--YAR-LKNVNADLLKIDGSFIRNIvsnSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGID 720
Cdd:PRK11829 556 ALDDFGIGYSSlrYLNhLKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQ 632
|
250
....*....|....*..
gi 16130428 721 YMQGYLIGKPQPLIDTL 737
Cdd:PRK11829 633 CGQGFLFSPPLPRAEFE 649
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
311-732 |
1.24e-31 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 132.20 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 311 YMAVLATRQRAVVRRIQRLAYVDPVVHLPNVRALNRALRD----APWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSHW 386
Cdd:PRK11359 357 HLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDlvdkAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 387 LSPLLEPGEDVYQLSGNDLALrLNTESHQERITALDSHLKQF---RFFWDGMPMQPQ--IGVSYcyvRSPVNHIYLLlge 461
Cdd:PRK11359 437 FREKLKPDQYLCRIEGTQFVL-VSLENDVSNITQIADELRNVvskPIMIDDKPFPLTlsIGISY---DVGKNRDYLL--- 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 462 lntvaelsivTNAPENMQRR----GAMY------LQRELKDKVAMMNRLQQALEHNHFFLMAQP-ITGMRGDVY-HEILL 529
Cdd:PRK11359 510 ----------STAHNAMDYIrkngGNGWqffspaMNEMVKERLVLGAALKEAISNNQLKLVYQPqIFAETGELYgIEALA 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 530 RMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAK---MPAhrFAINLSPTSVCQARFPVEVSQLLAKY 606
Cdd:PRK11359 580 RWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQnihIPA--LSVNLSALHFRSNQLPNQVSDAMQAW 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 607 QIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIV 686
Cdd:PRK11359 658 GIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALL 737
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 16130428 687 ASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQP 732
Cdd:PRK11359 738 EAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
502-733 |
8.25e-26 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 112.01 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 502 QALEHNHFFLMAQP--------ITGMrgdvyhEILLRMKGENDELISPDSFLPVAHEFGLSSSIdmwvIEHTLQFMAENR 573
Cdd:PRK10551 270 TGIKRGQFYVEYQPvvdtqtlrVTGL------EALLRWRHPTAGEIPPDAFINYAEAQKLIVPL----TQHLFELIARDA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 574 AKMPAH-----RFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQItLQHLQELGCQIAIDDF 648
Cdd:PRK10551 340 AELQKVlpvgaKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATKL-FAWLHSQGIEIAIDDF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 649 GTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIG 728
Cdd:PRK10551 419 GTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWIS 498
|
....*
gi 16130428 729 KPQPL 733
Cdd:PRK10551 499 RPLPL 503
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
328-480 |
9.05e-24 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 98.47 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 328 RLAYVDPVVHLPNVRALNRAL--------RDAPWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSHWLSPLLEPGEDVYQ 399
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELeqelqraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 400 LSGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSY--CYVRSPVNHIYLLLGELNTVAELSIVTNAPEN 477
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIgvAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 16130428 478 MQR 480
Cdd:smart00267 161 AVY 163
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
500-734 |
3.85e-17 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 85.68 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 500 LQQALEHNHFFLMAQPITGMRGDVYH-EILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENrakmPA 578
Cdd:PRK11059 408 LEQTLVRGGPRLYQQPAVTRDGKVHHrELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYW----PE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 579 HRFAINLSPTSVCQARFP-------VEVSQLLAKyqieawQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTG 651
Cdd:PRK11059 484 ENLSINLSVDSLLSRAFQrwlrdtlLQCPRSQRK------RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLT 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 652 YASYARLKNVNADLLKIDGSFIRNI---VSNSLdyqIVASI---CHLARMKkmlVVAEYVENEEIREAVLSLGIDYMQGY 725
Cdd:PRK11059 558 VVSTSYIKELNVELIKLHPSLVRNIhkrTENQL---FVRSLvgaCAGTETQ---VFATGVESREEWQTLQELGVSGGQGD 631
|
....*....
gi 16130428 726 LIGKPQPLI 734
Cdd:PRK11059 632 FFAESQPLD 640
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
508-733 |
2.40e-11 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 66.36 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 508 HFFLMAQPITGMRGDVY-HEILLRMKGENdelispdSFLPVAHEFGLSSsidmwVIEHTLQFMAENRAKMPAHRFaINLS 586
Cdd:COG3434 3 DVFVARQPILDRDQRVVgYELLFRSGLEN-------SAPDVDGDQATAR-----VLLNAFLEIGLDRLLGGKLAF-INFT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 587 PTSVCQ---ARFPVEvsqllakyqieawQLIFEVTESNALTnvkqAQI--TLQHLQELGCQIAIDDFgTGYASYARLKNV 661
Cdd:COG3434 70 EELLLSdlpELLPPE-------------RVVLEILEDVEPD----EELleALKELKEKGYRIALDDF-VLDPEWDPLLPL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130428 662 nADLLKIDgsfirniVSNSLDYQIVASICHLARMKKMLVvAEYVENEEIREAVLSLGIDYMQGYLIGKPQPL 733
Cdd:COG3434 132 -ADIIKID-------VLALDLEELAELVARLKRYGIKLL-AEKVETREEFELCKELGFDLFQGYFFSKPEIL 194
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
239-446 |
5.13e-04 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 42.66 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 239 TIFSTNYTLSLLLPLMMWGAMRYGYKLISLLWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNYMAVLA-- 316
Cdd:COG2199 18 LLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLal 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130428 317 ---TRQRAVVRRIQRLAYVDPVVHLPNVRALNRAL--------RDAPWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSH 385
Cdd:COG2199 98 ediTELRRLEERLRRLATHDPLTGLPNRRAFEERLerelararREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVAR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130428 386 WLSPLLEPGEDVYQLSGNDLAL---RLNTESHQERITALDSHLKQFRFFWDGMPMQPQ--IGVSYC 446
Cdd:COG2199 178 RLRASLRESDLVARLGGDEFAVllpGTDLEEAEALAERLREALEQLPFELEGKELRVTvsIGVALY 243
|
|
| |
