|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
3-523 |
0e+00 |
|
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: 525.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 3 KMLKKGVSIYIAALLLSFAFFYIVAQVAYYAFIQEKVEDYAESILARSDNIILQVREinALREEFSV-YTPCSDPYLHAL 81
Cdd:COG4943 7 RLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARS--ALDELNALpGDPCSPAHLAAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 82 RKRLWPYPLIKDIGYVEDGRIICSAlWGKYAAPLSLNVFKNKVSRGSYTWVF-DALIENNITADVVYNNNFSVTVSPFAF 160
Cdd:COG4943 85 RRLVFSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNvDNPLDPGRPMLIVGRGNYVVVIDPAAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 161 TRFREDStrWGFNAVVGDYNHKQHFFRVGNNTSLLENIEHGKVHEFF----FITEKSCDAQHDICVVAGVRHSFVFNNNG 236
Cdd:COG4943 164 IDVLSPQ--PGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFiqgdRLYASACSPQYPICVVAAAPLAGLLALWR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 237 YILLFLFCVASLVGLFVGALISKNQHENQSLLTRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDI 316
Cdd:COG4943 242 QLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 317 FIPLAEENGLINKISLYVVEHAIKECGAALRE-KDITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQSG 395
Cdd:COG4943 322 FIPLAEQSGLISPLTRQVIEQVFRDLGDLLAAdPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 396 RIEDIMQSICLYKEHGVLFALDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEG 475
Cdd:COG4943 402 DPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 516026079 476 VENEAQHLFLQGNLPEsCAQGWYFSKALAFSEIENLLAQVKQIDEGDD 523
Cdd:COG4943 482 VETEEQADYLRARGVQ-YGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-507 |
5.44e-73 |
|
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: 232.05 E-value: 5.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 269 TRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALR- 347
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 348 EKDITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQsgRIEDIMQSICL---YKEHGVLFALDDFGTGYS 424
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESA--LIDDLEEALATlrrLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 425 NLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWYFSKALA 504
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLR-ELGCDYVQGYLFSRPLP 237
|
...
gi 516026079 505 FSE 507
Cdd:cd01948 238 AEE 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
270-502 |
5.91e-63 |
|
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: 206.01 E-value: 5.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 270 RLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALREK 349
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 350 DITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQ-SGRIEDIMQSICLYKEHGVLFALDDFGTGYSNLKW 428
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516026079 429 LSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWYFSKA 502
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALR-ELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
269-503 |
1.75e-54 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 183.96 E-value: 1.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 269 TRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALRE 348
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 349 K--DITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQ-SGRIEDIMQSICLYKEHGVLFALDDFGTGYSN 425
Cdd:smart00052 82 GppPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVlLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 426 LKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQGNlpeSC--AQGWYFSKAL 503
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSL---GCdyGQGYLFSRPL 238
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
260-512 |
1.48e-39 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 153.77 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 260 NQHENQSLL--TRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEH 337
Cdd:PRK11359 535 NEMVKERLVlgAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAE 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 338 AIKECgAALREKDI---TLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITErqSGRIE---DIMQSICLYKEHG 411
Cdd:PRK11359 615 ACRQL-AEWRSQNIhipALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITE--SMMMEhdtEIFKRIQILRDMG 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 412 VLFALDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPE 491
Cdd:PRK11359 692 VGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLR-KIHC 770
|
250 260
....*....|....*....|.
gi 516026079 492 SCAQGWYFSKALAFSEIENLL 512
Cdd:PRK11359 771 RVIQGYFFSRPLPAEEIPGWM 791
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
3-523 |
0e+00 |
|
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: 525.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 3 KMLKKGVSIYIAALLLSFAFFYIVAQVAYYAFIQEKVEDYAESILARSDNIILQVREinALREEFSV-YTPCSDPYLHAL 81
Cdd:COG4943 7 RLLSLATLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARS--ALDELNALpGDPCSPAHLAAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 82 RKRLWPYPLIKDIGYVEDGRIICSAlWGKYAAPLSLNVFKNKVSRGSYTWVF-DALIENNITADVVYNNNFSVTVSPFAF 160
Cdd:COG4943 85 RRLVFSSRYVRDIGYVRDGRLLCSS-LGKLSKPVPLPPPDYVTADGYRLWLNvDNPLDPGRPMLIVGRGNYVVVIDPAAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 161 TRFREDStrWGFNAVVGDYNHKQHFFRVGNNTSLLENIEHGKVHEFF----FITEKSCDAQHDICVVAGVRHSFVFNNNG 236
Cdd:COG4943 164 IDVLSPQ--PGISLALLATNGGHLFASSGNPDPALLSRLLRGPSSWFiqgdRLYASACSPQYPICVVAAAPLAGLLALWR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 237 YILLFLFCVASLVGLFVGALISKNQHENQSLLTRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDI 316
Cdd:COG4943 242 QLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 317 FIPLAEENGLINKISLYVVEHAIKECGAALRE-KDITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQSG 395
Cdd:COG4943 322 FIPLAEQSGLISPLTRQVIEQVFRDLGDLLAAdPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 396 RIEDIMQSICLYKEHGVLFALDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEG 475
Cdd:COG4943 402 DPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 516026079 476 VENEAQHLFLQGNLPEsCAQGWYFSKALAFSEIENLLAQVKQIDEGDD 523
Cdd:COG4943 482 VETEEQADYLRARGVQ-YGQGWLFAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-507 |
5.44e-73 |
|
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: 232.05 E-value: 5.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 269 TRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALR- 347
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 348 EKDITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQsgRIEDIMQSICL---YKEHGVLFALDDFGTGYS 424
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESA--LIDDLEEALATlrrLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 425 NLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWYFSKALA 504
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLR-ELGCDYVQGYLFSRPLP 237
|
...
gi 516026079 505 FSE 507
Cdd:cd01948 238 AEE 240
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
262-514 |
6.33e-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: 245.07 E-value: 6.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 262 HENQSLLTRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKE 341
Cdd:COG5001 421 RERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQ 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 342 CgAALREK---DITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITE----RQSGRIEDIMQSIclyKEHGVLF 414
Cdd:COG5001 501 L-AAWQDAglpDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITEsallEDPEEALETLRAL---RALGVRI 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 415 ALDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQGNlpeSC- 493
Cdd:COG5001 577 ALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLREL---GCd 653
|
250 260
....*....|....*....|..
gi 516026079 494 -AQGWYFSKALAFSEIENLLAQ 514
Cdd:COG5001 654 yAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
262-513 |
9.95e-72 |
|
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: 239.69 E-value: 9.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 262 HENQSLLTRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKE 341
Cdd:COG2200 324 RRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 342 CgAALRE--KDITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQS-GRIEDIMQSICLYKEHGVLFALDD 418
Cdd:COG2200 404 L-ARWPErgLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALlEDLEAAIELLARLRALGVRIALDD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 419 FGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWY 498
Cdd:COG2200 483 FGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALR-ELGCDYAQGYL 561
|
250
....*....|....*
gi 516026079 499 FSKALAFSEIENLLA 513
Cdd:COG2200 562 FGRPLPLEELEALLR 576
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
270-502 |
5.91e-63 |
|
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: 206.01 E-value: 5.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 270 RLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALREK 349
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 350 DITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQ-SGRIEDIMQSICLYKEHGVLFALDDFGTGYSNLKW 428
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516026079 429 LSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWYFSKA 502
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALR-ELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
269-503 |
1.75e-54 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 183.96 E-value: 1.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 269 TRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALRE 348
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 349 K--DITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITERQ-SGRIEDIMQSICLYKEHGVLFALDDFGTGYSN 425
Cdd:smart00052 82 GppPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVlLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 426 LKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQGNlpeSC--AQGWYFSKAL 503
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSL---GCdyGQGYLFSRPL 238
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
260-512 |
1.48e-39 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 153.77 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 260 NQHENQSLL--TRLENAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEH 337
Cdd:PRK11359 535 NEMVKERLVlgAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAE 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 338 AIKECgAALREKDI---TLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITErqSGRIE---DIMQSICLYKEHG 411
Cdd:PRK11359 615 ACRQL-AEWRSQNIhipALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITE--SMMMEhdtEIFKRIQILRDMG 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 412 VLFALDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPE 491
Cdd:PRK11359 692 VGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLR-KIHC 770
|
250 260
....*....|....*....|.
gi 516026079 492 SCAQGWYFSKALAFSEIENLL 512
Cdd:PRK11359 771 RVIQGYFFSRPLPAEEIPGWM 791
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
273-509 |
3.79e-33 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 133.91 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 273 NAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIK-ECGAALREKDI 351
Cdd:PRK11829 412 QAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRiLADWKARGVSL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 352 TLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITErqSGRIEDIMQSICLYKE---HGVLFALDDFGTGYSNLKW 428
Cdd:PRK11829 492 PLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITE--TAQIQDLDEALRLLRElqgLGLLIALDDFGIGYSSLRY 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 429 L---SMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKdmpRTIVFEGVENEAQHLFLQGNLPEsCAQGWYFSKALAF 505
Cdd:PRK11829 570 LnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLK---VRVMAEGVETEEQRQWLLEHGIQ-CGQGFLFSPPLPR 645
|
....
gi 516026079 506 SEIE 509
Cdd:PRK11829 646 AEFE 649
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
233-508 |
1.26e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 128.19 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 233 NNNGYILLFLFCVASLVGLFVGALISKNQHENQSLLTrlenAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNI 312
Cdd:PRK10551 234 NDIWYALLLGLLSGILVGLLCYYLLSLRMRPGKEILT----GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 313 GPDIFIPLAEENGLINKISLYVVEHAIKEcGAALRE---KDITLSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEI 389
Cdd:PRK10551 310 PPDAFINYAEAQKLIVPLTQHLFELIARD-AAELQKvlpVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEI 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 390 TERQSGRIEDIMQSICLYKEHGVLFALDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPR 469
Cdd:PRK10551 389 TERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNM 468
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 516026079 470 TIVFEGVENEAQHLFL--QG-NLpescAQGWYFSKALAFSEI 508
Cdd:PRK10551 469 LTVAEGVETPEQARWLreRGvNF----LQGYWISRPLPLEDF 506
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
267-514 |
6.05e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 127.49 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 267 LLTRLENAIINKELHFVYQPLYRVKDKsIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECgAAL 346
Cdd:PRK10060 409 LDTNLRKALENDQLVIHYQPKITWRGE-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQV-AKW 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 347 REKDITL--SINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITErqSGRIEDIMQSICLYKEHGVLFA---LDDFGT 421
Cdd:PRK10060 487 RDKGINLrvAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE--SCLIENEELALSVIQQFSQLGAqvhLDDFGT 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 422 GYSNLKWLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQGNLPEScAQGWYFSK 501
Cdd:PRK10060 565 GYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNE-RQGFLFAK 643
|
250
....*....|...
gi 516026079 502 ALAFSEIENLLAQ 514
Cdd:PRK10060 644 PMPAVAFERWYKR 656
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
273-509 |
1.07e-29 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 123.67 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 273 NAIINKELHFVYQPLYRVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECgAALREKDIT 352
Cdd:PRK13561 407 NALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLL-AAWQERGIM 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 353 --LSINVSCSDICSKTFYQRLIDTLQQEGVAGKHIMLEITErqSGRIEDIMQSICLYK---EHGVLFALDDFGTGYSNLK 427
Cdd:PRK13561 486 lpLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTE--SRRIDDPHAAVAILRplrNAGVRVALDDFGMGYAGLR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 428 WLSM---LDVDEIKIDKSITDSIGTQSinrHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQGNLPEScAQGWYFSKALA 504
Cdd:PRK13561 564 QLQHmksLPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI-AQGFLFARALP 639
|
....*
gi 516026079 505 FSEIE 509
Cdd:PRK13561 640 IEIFE 644
|
|
| CSS-motif |
pfam12792 |
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ... |
36-234 |
2.61e-21 |
|
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS sequence motif is found N-terminal to the EAL, pfam00563, domain in many cyclic diguanylate phosphodiesterases.
Pssm-ID: 463709 Cd Length: 209 Bit Score: 92.20 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 36 QEKVEDYAESILARSDNIILQV----REINALREEfsvytPCSDPYLHALRKRLWPYPLIKDIGYVEDGRIICSALWGKY 111
Cdd:pfam12792 2 QEQLDAFAERALRRLESVLDQAdqalDRLLPLTGQ-----PCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 112 AAPLSLNVFKNKVSRGSYTWVF-DALIENNITADVVYNNNFSVTVSPFAFTRFREDStrwGFNAVVGDYNHKQHFFRVGN 190
Cdd:pfam12792 77 DTPLPLLPPDLTTPPGVRLWLLrGTPLVPGRPALVLRRGGYGVVIDPGVFIDVQYLP---GLLAAVSQPDGRLLALVVGD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516026079 191 N--------TSLLENIEHGKVHEFFFITEkSCDAQHDICVVAGVRHSFVFNN 234
Cdd:pfam12792 154 DallfdgrlHSLAEPAPGTARSGGALYAR-ARSTRYPLTVVVYAPRASLLAN 204
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
298-455 |
1.26e-12 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 70.86 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 298 VEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKECGAALREKDITLSINVSCSDICSKTFYQRLIDTLQQ 377
Cdd:PRK09776 873 WLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLEN 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 378 EGVAGKHIMLEITER-------QSGRIEDIMQsiclykEHGVLFALDDFGTGYSNLKWLSMLDVDEIKID--------KS 442
Cdd:PRK09776 953 SPLPPRLLHLEITETallnhaeSASRLVQKLR------LAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDgelvanlhGN 1026
|
170
....*....|...
gi 516026079 443 ITDSIGTQSINRH 455
Cdd:PRK09776 1027 LMDEMLISIIQGH 1039
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
369-511 |
7.66e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 62.71 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 369 QRLIDTLqqegvagKHIMLEITERQSGRIEDIMQSIClykEHGVLFaLDDFGTGYSNLKWLSMLDVDEIKIDKSITDSIG 448
Cdd:PRK11596 121 LRLIERL-------PWLRFELVEHIRLPKDSPFASMC---EFGPLW-LDDFGTGMANFSALSEVRYDYIKVARELFIMLR 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516026079 449 TQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWYFSKALAFSEIENL 511
Cdd:PRK11596 190 QSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQ-RSPAFAAQGYFLSRPAPFETLETL 251
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
355-501 |
1.02e-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: 47.87 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 355 INVScsdicSKTFYQRLIDTLQQEgvagkHIMLEITERQSGRiEDIMQSICLYKEHGVLFALDDFGTGYSNLKWLSMLDV 434
Cdd:COG3434 66 INFT-----EELLLSDLPELLPPE-----RVVLEILEDVEPD-EELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADI 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516026079 435 deIKIDksitdsigTQSINRHILPGLIAMFKDMPRTIVFEGVENEAQHLFLQgNLPESCAQGWYFSK 501
Cdd:COG3434 135 --IKID--------VLALDLEELAELVARLKRYGIKLLAEKVETREEFELCK-ELGFDLFQGYFFSK 190
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
269-500 |
7.52e-04 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 42.16 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 269 TRLENAIINKELHFVYQPLYrVKDKSIIGVEVLLRWNDKQMGNIGPDIFIPLAEENGLINKISLYVVEHAIKEcgaALRE 348
Cdd:PRK11059 406 TLLEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPL---LRYW 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 349 KDITLSINVSCSDICSKTFYQRLIDTL-QQEGVAGKHIMLEITERQSGRIEDIMQSIC-LYKEHGVLFALDDFG-----T 421
Cdd:PRK11059 482 PEENLSINLSVDSLLSRAFQRWLRDTLlQCPRSQRKRLIFELAEADVCQHISRLRPVLrMLRGLGCRLAVDQAGltvvsT 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516026079 422 GYsnlkwLSMLDVDEIKIDKSITDSIGTQSINRHILPGLIAMFKDMpRTIVF-EGVENEAQHLFLQGnLPESCAQGWYFS 500
Cdd:PRK11059 562 SY-----IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGT-ETQVFaTGVESREEWQTLQE-LGVSGGQGDFFA 634
|
|
| |
