|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
282-698 |
5.12e-73 |
|
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: 249.69 E-value: 5.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 282 RAMAERQVDELTWKDGLTGAYSRSAFHR------DYDCGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREV 355
Cdd:COG5001 240 RKRAEERLRHLAYHDPLTGLPNRRLFLDrleqalARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRAC 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 356 FGEG--VYRIGDDEFCAVALPLEYEE-----FDRMTRSLTARFAEAGLP----ASVGLA-WSERCEDATVLLNTAgDR-M 422
Cdd:COG5001 320 LREGdtVARLGGDEFAVLLPDLDDPEdaeavAERILAALAEPFELDGHElyvsASIGIAlYPDDGADAEELLRNA-DLaM 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 423 RRVK-IGRHR----ATDLGIDLAQDGAV-NDLirpggaRDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeV 496
Cdd:COG5001 399 YRAKaAGRNRyrffDPEMDERARERLELeADL------RRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGL-V 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 497 QPASFVPALEDMGEIADVDFFALTRACETVARWQREGRAAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVT 576
Cdd:COG5001 472 SPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEIT 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 577 ESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSI 656
Cdd:COG5001 552 ESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGL 631
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 496663371 657 ESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDEFERRF 698
Cdd:COG5001 632 EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALL 673
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
455-693 |
6.11e-69 |
|
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: 225.50 E-value: 6.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 455 RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQReGR 534
Cdd:cd01948 4 RRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGL-ISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA-GG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 535 AAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVS 614
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663371 615 LFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDE 693
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
455-693 |
4.49e-58 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 196.67 E-value: 4.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 455 RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQREGR 534
Cdd:smart00052 5 RQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGI-ISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 535 AAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVS 614
Cdd:smart00052 84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663371 615 LFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDE 693
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
455-688 |
3.00e-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: 194.07 E-value: 3.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 455 RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQreGR 534
Cdd:pfam00563 5 RRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGL-ISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ--LG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 535 AAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVS 614
Cdd:pfam00563 82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663371 615 LFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRP 688
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
279-688 |
3.57e-43 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 167.25 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 279 SMKRAMAERQVDELTWKDGLTGAYSRSAFHRDYD--CGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVF 356
Cdd:PRK11359 362 ALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDdlVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 357 GEGVY--RIGDDEFCAVALPLEYEEFDRMTRSLTARFAEA--------GLPASVGLAWsERCEDATVLLNTAGDRMRRV- 425
Cdd:PRK11359 442 KPDQYlcRIEGTQFVLVSLENDVSNITQIADELRNVVSKPimiddkpfPLTLSIGISY-DVGKNRDYLLSTAHNAMDYIr 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 426 KIGRHRATDLGIDLAQdgAVNDLIRPGGA-RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGiEVQPASFVPA 504
Cdd:PRK11359 521 KNGGNGWQFFSPAMNE--MVKERLVLGAAlKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHG-HVPPSRFIPL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 505 LEDMGEIADVDFFALTRACETVARWQREGRAAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGG 584
Cdd:PRK11359 598 AEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHD 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 585 DLLRCVADDLRGRGFSVAVDDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIE 664
Cdd:PRK11359 678 TEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVE 757
|
410 420
....*....|....*....|....
gi 496663371 665 TEQQLEALKTTGCTRAQGYLIGRP 688
Cdd:PRK11359 758 TKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
139-261 |
2.79e-08 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 53.54 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 139 DLDAALNAVLGMVGEFLQADRTYIFNIvshrmwnaYEWCAQGVSPEIQNLSDLPLSLIDHWIER------FTRGEAVIIN 212
Cdd:smart00065 1 DLEELLQTILEELRQLLGADRVLIYLV--------DENDRGELVLVAADGLTLPTLGIRFPLDEglagrvAETGRPLNIP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 496663371 213 --SVDDLQDGERADEYealsvQGIQSLVVVPLEVDGRLVGYMGADDPKKGR 261
Cdd:smart00065 73 dvEADPLFAEDLLGRY-----QGVRSFLAVPLVADGELVGVLALHNKKSPR 118
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
139-280 |
2.03e-07 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 50.56 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 139 DLDAALNAVLGMVGEFLQADRTYIFNIVshrmWNAYEWCAQGVSPEIQNLSDLPlslIDHWIERFTRGEAVIINsvDDLQ 218
Cdd:pfam01590 1 DLEEILQTILEELRELLGADRCALYLPD----ADGLEYLPPGARWLKAAGLEIP---PGTGVTVLRTGRPLVVP--DAAG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496663371 219 DGERADEYEALSVQGIQSLVVVPLEVDGRLVGYMGADDPKKG----RLEIIEkplvSLASFISASM 280
Cdd:pfam01590 72 DPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPPfteeELELLE----VLADQVAIAL 133
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
292-371 |
2.50e-05 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 45.02 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 292 LTWKDGLTGAYSRSAFHRDYD-----CGTFE-SIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMRE-VFGEGVY-RI 363
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDselkrARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsVRGSDVVgRY 80
|
....*...
gi 496663371 364 GDDEFCAV 371
Cdd:TIGR00254 81 GGEEFVVI 88
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
282-698 |
5.12e-73 |
|
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: 249.69 E-value: 5.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 282 RAMAERQVDELTWKDGLTGAYSRSAFHR------DYDCGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREV 355
Cdd:COG5001 240 RKRAEERLRHLAYHDPLTGLPNRRLFLDrleqalARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRAC 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 356 FGEG--VYRIGDDEFCAVALPLEYEE-----FDRMTRSLTARFAEAGLP----ASVGLA-WSERCEDATVLLNTAgDR-M 422
Cdd:COG5001 320 LREGdtVARLGGDEFAVLLPDLDDPEdaeavAERILAALAEPFELDGHElyvsASIGIAlYPDDGADAEELLRNA-DLaM 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 423 RRVK-IGRHR----ATDLGIDLAQDGAV-NDLirpggaRDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeV 496
Cdd:COG5001 399 YRAKaAGRNRyrffDPEMDERARERLELeADL------RRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGL-V 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 497 QPASFVPALEDMGEIADVDFFALTRACETVARWQREGRAAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVT 576
Cdd:COG5001 472 SPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEIT 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 577 ESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSI 656
Cdd:COG5001 552 ESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGL 631
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 496663371 657 ESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDEFERRF 698
Cdd:COG5001 632 EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALL 673
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
455-693 |
6.11e-69 |
|
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: 225.50 E-value: 6.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 455 RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQReGR 534
Cdd:cd01948 4 RRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGL-ISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA-GG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 535 AAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVS 614
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663371 615 LFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDE 693
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
140-698 |
1.28e-65 |
|
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: 227.36 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 140 LDAALNAVLGMVGEFLQADRTYIFNIVSHRMWNAYEWCAQGVSPEIQNLSDLPLSLIDHWIERFTRGEAVIINSVDDLQD 219
Cdd:COG2200 5 LALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 220 GERADEYEALSVQGIQSLVVVPLEVDGRLVGYMGADDPKKGRLEIIEKPLVSLASFISASMKRAMAERQVDELTWKDGLT 299
Cdd:COG2200 85 LLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 300 G---AYSRSAFHRDYDCGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVFGEGVYRIGDDEFCAVALPLE 376
Cdd:COG2200 165 RrllLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 377 YEEFDRMTRSLTARFAEAGLP-----------ASVGLAWSERCEDATVLLNTAGDRMRRVKIGRHRATDLGIDLAQDGAV 445
Cdd:COG2200 245 LAAAAAAAAALRLLLLLLLEPlllggglvvvaSSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 446 NDLIRPGGARDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACET 525
Cdd:COG2200 325 RRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGL-ISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 526 VARWQREGRAaVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDD 605
Cdd:COG2200 404 LARWPERGLD-LRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 606 FGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLI 685
Cdd:COG2200 483 FGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562
|
570
....*....|...
gi 496663371 686 GRPSAIDEFERRF 698
Cdd:COG2200 563 GRPLPLEELEALL 575
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
455-693 |
4.49e-58 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 196.67 E-value: 4.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 455 RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQREGR 534
Cdd:smart00052 5 RQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGI-ISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 535 AAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVS 614
Cdd:smart00052 84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663371 615 LFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDE 693
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
455-688 |
3.00e-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: 194.07 E-value: 3.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 455 RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQreGR 534
Cdd:pfam00563 5 RRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGL-ISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ--LG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 535 AAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVS 614
Cdd:pfam00563 82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663371 615 LFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRP 688
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
279-688 |
3.57e-43 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 167.25 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 279 SMKRAMAERQVDELTWKDGLTGAYSRSAFHRDYD--CGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVF 356
Cdd:PRK11359 362 ALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDdlVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 357 GEGVY--RIGDDEFCAVALPLEYEEFDRMTRSLTARFAEA--------GLPASVGLAWsERCEDATVLLNTAGDRMRRV- 425
Cdd:PRK11359 442 KPDQYlcRIEGTQFVLVSLENDVSNITQIADELRNVVSKPimiddkpfPLTLSIGISY-DVGKNRDYLLSTAHNAMDYIr 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 426 KIGRHRATDLGIDLAQdgAVNDLIRPGGA-RDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGiEVQPASFVPA 504
Cdd:PRK11359 521 KNGGNGWQFFSPAMNE--MVKERLVLGAAlKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHG-HVPPSRFIPL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 505 LEDMGEIADVDFFALTRACETVARWQREGRAAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGG 584
Cdd:PRK11359 598 AEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHD 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 585 DLLRCVADDLRGRGFSVAVDDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIE 664
Cdd:PRK11359 678 TEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVE 757
|
410 420
....*....|....*....|....
gi 496663371 665 TEQQLEALKTTGCTRAQGYLIGRP 688
Cdd:PRK11359 758 TKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
465-700 |
2.23e-42 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 163.35 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 465 IFLMPQVATQTGALVGAEALIRYLDPERGIEVqPASFVPALEDMGEIADVDFFALTRACETVARWQREGrAAVPIAVNFS 544
Cdd:PRK13561 416 IWLQPQVEMRSGKLVSAEALLRMQQPDGSWDL-PEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERG-IMLPLSVNLS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 545 RMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGrgGDLLRCVA--DDLRGRGFSVAVDDFGVDNANVSLFVQ---L 619
Cdd:PRK13561 494 ALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRI--DDPHAAVAilRPLRNAGVRVALDDFGMGYAGLRQLQHmksL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 620 EFDVLKMDRSLIWGIdATDRTMrvVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDEFERRFM 699
Cdd:PRK13561 572 PIDVLKIDKMFVDGL-PEDDSM--VAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEERYL 648
|
.
gi 496663371 700 A 700
Cdd:PRK13561 649 E 649
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
285-696 |
1.70e-36 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 145.98 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 285 AERQVDELTWKDGLTGAYSRSAFHRDYDCG----TFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVFGEG- 359
Cdd:PRK10060 229 AQERLRILANTDSITGLPNRNAIQELIDHAinaaDNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDq 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 360 -VYRIGDDEFCAVALPLEYEEFDRMTRSLTARFAEA---GLP-----ASVGLA-WSERCEDATVLLNTAGDRMRRVK-IG 428
Cdd:PRK10060 309 tLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPfriGLIevytgCSIGIAlAPEHGDDSESLIRSADTAMYTAKeGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 429 RHRATDLGIDLAQDGAvNDLIRPGGARDAVEAGLLDIFLMPQVaTQTGALVGAEALIRYLDPERGIeVQPASFVPALEDM 508
Cdd:PRK10060 389 RGQFCVFSPEMNQRVF-EYLWLDTNLRKALENDQLVIHYQPKI-TWRGEVRSLEALVRWQSPERGL-IPPLEFISYAEES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 509 GEIADVDFFALTRACETVARWQREGrAAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLR 588
Cdd:PRK10060 466 GLIVPLGRWVMLDVVRQVAKWRDKG-INLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 589 CVADDLRGRGFSVAVDDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQ 668
Cdd:PRK10060 545 SVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKE 624
|
410 420
....*....|....*....|....*...
gi 496663371 669 LEALKTTGCTRAQGYLIGRPSAIDEFER 696
Cdd:PRK10060 625 DAFLTKNGVNERQGFLFAKPMPAVAFER 652
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
456-698 |
8.53e-36 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 143.93 E-value: 8.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 456 DAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIeVQPASFVPALEDMGEIADVDFFALTRACETVARWQREGrA 535
Cdd:PRK11829 412 QAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSY-VLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARG-V 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 536 AVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESAR----GRGGDLLRCvaddLRGRGFSVAVDDFGVDNA 611
Cdd:PRK11829 490 SLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQiqdlDEALRLLRE----LQGLGLLIALDDFGIGYS 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 612 NVSLF---VQLEFDVLKMDRSLIWGIDATDRTMRVVSglaSLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRP 688
Cdd:PRK11829 566 SLRYLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIIS---CVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
|
250
....*....|
gi 496663371 689 SAIDEFERRF 698
Cdd:PRK11829 643 LPRAEFEAQY 652
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
469-694 |
1.10e-21 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 99.30 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 469 PQVATQTGALVGAEALIRYLDPERGiEVQPASFVPALEDMGEIAdvdffALTRAC-ETVARWQREGRAAVP----IAVNF 543
Cdd:PRK10551 283 PVVDTQTLRVTGLEALLRWRHPTAG-EIPPDAFINYAEAQKLIV-----PLTQHLfELIARDAAELQKVLPvgakLGINI 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 544 SRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLRcVADDLRGRGFSVAVDDFGVDNanvSLFVQLE--- 620
Cdd:PRK10551 357 SPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATK-LFAWLHSQGIEIAIDDFGTGH---SALIYLErft 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663371 621 FDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDEF 694
Cdd:PRK10551 433 LDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
282-694 |
1.21e-18 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 90.89 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 282 RAMaERQVDELTWKDGLTGAYSRSAF--HRDYDCGTFESIG----FVLVDADRLAVVNRERSRDEGDEVLRRICSSMREV 355
Cdd:PRK09776 655 RKM-LRQLSYSASHDALTHLANRASFekQLRRLLQTVNSTHqrhaLVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 356 F--GEGVYRIGDDEFcAVALP---LEYEEF--DRMTRSLTA-RFAEAG----LPASVGLAwserCEDATVllNTAGDRMR 423
Cdd:PRK09776 734 LrsSDVLARLGGDEF-GLLLPdcnVESARFiaTRIISAINDyHFPWEGrvyrVGASAGIT----LIDANN--HQASEVMS 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 424 RVKI--------GRHRATDLGIDLAQ-DGAVNDLIRPGGARDAVEAGLLdiflmpQVATQTGALVGAEA------LIRYL 488
Cdd:PRK09776 807 QADIacyaaknaGRGRVTVYEPQQAAaHSEHRALSLAEQWRMIKENQLM------MLAHGVASPRIPEArnhwliSLRLW 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 489 DPErGIEVQPASFVPALEDMGEIADVDffalTRACETVARWQREGRAA--VPIAVNFSRMTVGEEGFVDRVAETVARFGV 566
Cdd:PRK09776 881 DPE-GEIIDEGAFRPAAEDPALMHALD----RRVIHEFFRQAAKAVASkgLSIALPLSVAGLSSPTLLPFLLEQLENSPL 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 567 DPSLIEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGvdnANVSLFVQLE---FDVLKMDRSLIWGID--ATDRTM 641
Cdd:PRK09776 956 PPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFG---RGLSSFNYLKafmADYLKLDGELVANLHgnLMDEML 1032
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 496663371 642 rvVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAIDEF 694
Cdd:PRK09776 1033 --ISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
185-431 |
1.83e-16 |
|
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: 80.02 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 185 IQNLSDLPLSLIDHWIERFTRGEAVIINSVDDLQDGERADEYEALSVQGIQSLVVVPLEVDGRLVGYMGADDPKKGRLEI 264
Cdd:COG2199 6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 265 IEKPLVSLASFISASMKRAMAERQVDELTWKDGLTGAYSRSAFHRDYD------CGTFESIGFVLVDADRLAVVNRERSR 338
Cdd:COG2199 86 LLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLErelaraRREGRPLALLLIDLDHFKRINDTYGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 339 DEGDEVLRRICSSMREVFGEG--VYRIGDDEFCAVALPLEYEEFDRMTRSLTARFAEAGLP---------ASVGLA-WSE 406
Cdd:COG2199 166 AAGDEVLKEVARRLRASLRESdlVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElegkelrvtVSIGVAlYPE 245
|
250 260
....*....|....*....|....*.
gi 496663371 407 RCEDATVLLNTAGDRMRRVK-IGRHR 431
Cdd:COG2199 246 DGDSAEELLRRADLALYRAKrAGRNR 271
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
291-431 |
1.17e-12 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 66.50 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 291 ELTWKDGLTGAYSRSAFHR------DYDCGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVFGEG--VYR 362
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEeleqelQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdlLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663371 363 IGDDEFCAVALPLEYEEFDRMTRSLTARFAEAGLP--------ASVGLA-WSERCEDATVLLNTAGDRMRRVK-IGRHR 431
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIhgiplyltISIGVAaYPNPGEDAEDLLKRADTALYQAKkAGRNQ 159
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
296-431 |
7.91e-12 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 63.73 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 296 DGLTGAYSRSAFHRDYD------CGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVFGEG--VYRIGDDE 367
Cdd:cd01949 3 DPLTGLPNRRAFEERLErllaraRRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESdlVARLGGDE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663371 368 FCAVALPLEYEEFDRMTRSLTARFAEAGLP--------ASVGLA-WSERCEDATVLLNTAGDRMRRVKI-GRHR 431
Cdd:cd01949 83 FAILLPGTDLEEAEALAERLREAIEEPFFIdgqeirvtASIGIAtYPEDGEDAEELLRRADEALYRAKRsGRNR 156
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
139-261 |
2.79e-08 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 53.54 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 139 DLDAALNAVLGMVGEFLQADRTYIFNIvshrmwnaYEWCAQGVSPEIQNLSDLPLSLIDHWIER------FTRGEAVIIN 212
Cdd:smart00065 1 DLEELLQTILEELRQLLGADRVLIYLV--------DENDRGELVLVAADGLTLPTLGIRFPLDEglagrvAETGRPLNIP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 496663371 213 --SVDDLQDGERADEYealsvQGIQSLVVVPLEVDGRLVGYMGADDPKKGR 261
Cdd:smart00065 73 dvEADPLFAEDLLGRY-----QGVRSFLAVPLVADGELVGVLALHNKKSPR 118
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
296-431 |
1.07e-07 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 51.87 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 296 DGLTGAYSRSAFHR------DYDCGTFESIGFVLVDADRLAVVNRERSRDEGDEVLR----RICSSMREvfGEGVYRIGD 365
Cdd:pfam00990 4 DPLTGLPNRRYFEEqleqelQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQevaqRLSSSLRR--SDLVARLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 366 DEFCAVaLP-------LEYEEF-DRMTRSLTARFAEAGLP----ASVGLA-WSERCEDATVLLNTAGDRMRRVK-IGRHR 431
Cdd:pfam00990 82 DEFAIL-LPetslegaQELAERiRRLLAKLKIPHTVSGLPlyvtISIGIAaYPNDGEDPEDLLKRADTALYQAKqAGRNR 160
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
139-280 |
2.03e-07 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 50.56 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 139 DLDAALNAVLGMVGEFLQADRTYIFNIVshrmWNAYEWCAQGVSPEIQNLSDLPlslIDHWIERFTRGEAVIINsvDDLQ 218
Cdd:pfam01590 1 DLEEILQTILEELRELLGADRCALYLPD----ADGLEYLPPGARWLKAAGLEIP---PGTGVTVLRTGRPLVVP--DAAG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496663371 219 DGERADEYEALSVQGIQSLVVVPLEVDGRLVGYMGADDPKKG----RLEIIEkplvSLASFISASM 280
Cdd:pfam01590 72 DPRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPPfteeELELLE----VLADQVAIAL 133
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
604-695 |
2.21e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 52.70 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 604 DDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASLCDDLSIESVAEGIETEQQLEALKTTGCTRAQGY 683
Cdd:PRK11596 158 DDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGY 237
|
90
....*....|..
gi 496663371 684 LIGRPSAIDEFE 695
Cdd:PRK11596 238 FLSRPAPFETLE 249
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
133-588 |
4.25e-06 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 50.19 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 133 RVLENDDLDAALNAVLGMVGEFLQADRTYIFniVSHRMWNAYEWCAqGVSPEIQNLSDLPLSlIDHWIERFTRGEAVIIN 212
Cdd:COG2203 201 ALRSALDLEELLQRILELAGELLGADRGAIL--LVDEDGGELELVA-APGLPEEELGRLPLG-EGLAGRALRTGEPVVVN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 213 SVDDlQDGERADEYEALSVQGIQSLVVVPLEVDGRLVGYMGADDPKKGRLEIIEKPLV-SLASFISASMKRAMAERQVDE 291
Cdd:COG2203 277 DAST-DPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLeALADQAAIAIERARLYEALEA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 292 LTWKDGLTGAYSRSAFHRDYDCGTFESIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMREVFGEGVYRIGDDEFCAV 371
Cdd:COG2203 356 ALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRR 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 372 ALPLEYEEFDRMTRSLTARFAEAGLPASVGLAWSERCEDATVLLNTAGDRMRRVKIGRHRATDLGIDLAQDGAVNDLIRP 451
Cdd:COG2203 436 ILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 452 GGARDAVEAGLLDIFLMPQVATQTGALVGAEALIRYLDPERGIEVQPASFVPALEDMGEIADVDFFALTRACETVARWQR 531
Cdd:COG2203 516 LLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLV 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 496663371 532 EGRAAVPIAVNFSRMTVGEEGFVDRVAETVARFGVDPSLIEIEVTESARGRGGDLLR 588
Cdd:COG2203 596 AVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALAS 652
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
573-691 |
1.21e-05 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 48.26 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 573 IEVTESARGRGGDLLRCvaDDLRGRGFSVAVDDFGVDNANVSLfvqLEF-DVLKmdrsliwgIDATDRTMRVVSGLASLC 651
Cdd:COG3434 88 LEILEDVEPDEELLEAL--KELKEKGYRIALDDFVLDPEWDPL---LPLaDIIK--------IDVLALDLEELAELVARL 154
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 496663371 652 DDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAI 691
Cdd:COG3434 155 KRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEIL 194
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
292-371 |
2.50e-05 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 45.02 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 292 LTWKDGLTGAYSRSAFHRDYD-----CGTFE-SIGFVLVDADRLAVVNRERSRDEGDEVLRRICSSMRE-VFGEGVY-RI 363
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDselkrARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsVRGSDVVgRY 80
|
....*...
gi 496663371 364 GDDEFCAV 371
Cdd:TIGR00254 81 GGEEFVVI 88
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
571-692 |
9.92e-03 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 39.08 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663371 571 IEIEVTESARGRGGDLLRCVADDLRGRGFSVAVDDFGVDNANVSLFVQLEFDVLKMDRSLIWGIDATDRTMRVVSGLASL 650
Cdd:PRK11059 519 LIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGA 598
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 496663371 651 CDDLSIESVAEGIETEQQLEALKTTGCTRAQGYLIGRPSAID 692
Cdd:PRK11059 599 CAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| |
