|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
176-846 |
0e+00 |
|
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: 619.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 176 AIKPTSDHAPIDLAKASVMVFVDRLTPAKLAKLGGDYGIANLHLLAGGAAGDKESLALEGTPHRLAWVSSRPGSAMLRET 255
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 256 ALPLLGIFVLAAGLLFWLSRSAVLNARAVDRQQKVLKRSNQALLASEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDV 335
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 336 TGYQPEAWIGRRLDELLDSDTVNIVKWLEGLPDADAPSSLVCAFRDSQ-GQARVGKLSASAIRNGVASGYRGTAADITDE 414
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLaLRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 415 VEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRAST 493
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARaRRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 494 RDQDMVARLGGDEFVVVSTHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYE 573
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 574 AKAAGRNTWRFYLEAMDSHLAEKKLRETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLA 653
Cdd:COG5001 401 AKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 654 EESDLIVQIGNWVLREACATAASWP----GEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVD 729
Cdd:COG5001 481 EETGLIVPLGEWVLREACRQLAAWQdaglPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 730 GALRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVET 809
Cdd:COG5001 561 EALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVET 640
|
650 660 670
....*....|....*....|....*....|....*..
gi 518201632 810 EGQMHILRDEQCHELQGFLLSRPLDAQRLRDLLEREA 846
Cdd:COG5001 641 EEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARA 677
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
410-844 |
3.50e-109 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 349.75 E-value: 3.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 410 DITDEVEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLaEKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERL 489
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI-NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 490 RASTRDQDMVARLGGDEFVVVSTHVSSKLeIEKFCSRLIDVINrevayegHSFHVG-------ASIGVALAPEHGGDPRG 562
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEFLVLASHTSQAA-LEAMASRILTRLR-------LPFRIGlievytgCSIGIALAPEHGDDSES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 563 LLRCADVAMYEAKAAGRNTWRFYLEAMDSHLAEKKLRETELRAALQNGEFELYYQPRFLAQEQtIASAEALIRWNHPRRG 642
Cdd:PRK10060 373 LIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRGE-VRSLEALVRWQSPERG 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 643 LIGPDEFIGLAEESDLIVQIGNWVLREACATAASWPG---EVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEV 719
Cdd:PRK10060 452 LIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVEL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 720 TENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALN 799
Cdd:PRK10060 532 TESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALN 611
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 518201632 800 LRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDAQRLRDLLER 844
Cdd:PRK10060 612 LQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
601-837 |
6.88e-104 |
|
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: 321.03 E-value: 6.88e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 601 TELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASWP-- 678
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 679 -GEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSL 757
Cdd:cd01948 81 gPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 758 GYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDAQR 837
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
600-833 |
8.20e-94 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 294.51 E-value: 8.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 600 ETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASW-- 677
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 678 --PGEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYS 755
Cdd:smart00052 81 qgPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518201632 756 SLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPL 833
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
602-832 |
7.13e-74 |
|
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: 241.45 E-value: 7.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 602 ELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASW--PG 679
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 680 EVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSLGY 759
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518201632 760 LRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRP 832
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
424-581 |
6.98e-43 |
|
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: 153.26 E-value: 6.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 424 LSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARL 502
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRaRRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 503 GGDEFVVVSTHVSSKLEIEKfCSRLIDVINREVAY--EGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAKAAGRN 580
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSK-AERLRDAINSKPIEvaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
.
gi 518201632 581 T 581
Cdd:TIGR00254 160 R 160
|
|
| CHASE4 |
pfam05228 |
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various ... |
59-220 |
1.77e-20 |
|
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in prokaryotes. Specifically, CHASE4 domains are found in histidine kinases in Archaea and in predicted diguanylate cyclases/phosphodiesterases in Bacteria. Environmental factors that are recognized by CHASE4 domains are not known at this time.
Pssm-ID: 428380 Cd Length: 139 Bit Score: 88.15 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 59 ALQNRRENSEQFSTTYSFWTDAYVYLGNRvdvDWAFTKNNLGSVLYTTNGYDGVFVIDDRGT-RYAMLEGELSERSLADS 137
Cdd:pfam05228 1 ALEQELDSLDRLLRDWAVWDDTYDFVQDG---NPDYIESNLGPETFENLGLDLILFVDADGKlVYDLENGKPDSPLLSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 138 LNADtgdilrsarraavdeaAISRYVDFDGAPAILVASAIKPTSDHAPIdlakASVMVFVDRLTPAKLAKLgGDYGIANL 217
Cdd:pfam05228 78 SPDS----------------GLSGIVLLGGGPALVAARPILTSDGSGPP----RGTLVMGRYLDEAFLDRL-SELTLLDL 136
|
...
gi 518201632 218 HLL 220
Cdd:pfam05228 137 TLS 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
176-846 |
0e+00 |
|
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: 619.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 176 AIKPTSDHAPIDLAKASVMVFVDRLTPAKLAKLGGDYGIANLHLLAGGAAGDKESLALEGTPHRLAWVSSRPGSAMLRET 255
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 256 ALPLLGIFVLAAGLLFWLSRSAVLNARAVDRQQKVLKRSNQALLASEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDV 335
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 336 TGYQPEAWIGRRLDELLDSDTVNIVKWLEGLPDADAPSSLVCAFRDSQ-GQARVGKLSASAIRNGVASGYRGTAADITDE 414
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLaLRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 415 VEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRAST 493
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARaRRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 494 RDQDMVARLGGDEFVVVSTHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYE 573
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 574 AKAAGRNTWRFYLEAMDSHLAEKKLRETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLA 653
Cdd:COG5001 401 AKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 654 EESDLIVQIGNWVLREACATAASWP----GEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVD 729
Cdd:COG5001 481 EETGLIVPLGEWVLREACRQLAAWQdaglPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 730 GALRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVET 809
Cdd:COG5001 561 EALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVET 640
|
650 660 670
....*....|....*....|....*....|....*..
gi 518201632 810 EGQMHILRDEQCHELQGFLLSRPLDAQRLRDLLEREA 846
Cdd:COG5001 641 EEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARA 677
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
410-844 |
3.50e-109 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 349.75 E-value: 3.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 410 DITDEVEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLaEKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERL 489
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI-NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 490 RASTRDQDMVARLGGDEFVVVSTHVSSKLeIEKFCSRLIDVINrevayegHSFHVG-------ASIGVALAPEHGGDPRG 562
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEFLVLASHTSQAA-LEAMASRILTRLR-------LPFRIGlievytgCSIGIALAPEHGDDSES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 563 LLRCADVAMYEAKAAGRNTWRFYLEAMDSHLAEKKLRETELRAALQNGEFELYYQPRFLAQEQtIASAEALIRWNHPRRG 642
Cdd:PRK10060 373 LIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRGE-VRSLEALVRWQSPERG 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 643 LIGPDEFIGLAEESDLIVQIGNWVLREACATAASWPG---EVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEV 719
Cdd:PRK10060 452 LIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVEL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 720 TENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALN 799
Cdd:PRK10060 532 TESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALN 611
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 518201632 800 LRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDAQRLRDLLER 844
Cdd:PRK10060 612 LQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
272-843 |
1.77e-107 |
|
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: 342.92 E-value: 1.77e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 272 WLSRSAVLNARAVDRQQKVLKRSNQALLASEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDEL 351
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 352 LDSDTVNIVKWLEGLPDADAPSSLVCAFRDSQGQARVGKLSASAIRNGVASGYRGTAADITDEVEAHAKIQHLSLHDALT 431
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 432 GLPNRNKLFQFLERLLAEKAG--KSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARLGGDEFVV 509
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLAlaLLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 510 VSTHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAKAAGRNTWRFYLEAM 589
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 590 DSHLAEKKLrETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLRE 669
Cdd:COG2200 321 ARARRRLAL-ESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 670 ACATAASWPG---EVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLN 746
Cdd:COG2200 400 ALRQLARWPErglDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 747 MDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQG 826
Cdd:COG2200 480 LDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQG 559
|
570
....*....|....*..
gi 518201632 827 FLLSRPLDAQRLRDLLE 843
Cdd:COG2200 560 YLFGRPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
601-837 |
6.88e-104 |
|
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: 321.03 E-value: 6.88e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 601 TELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASWP-- 678
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 679 -GEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSL 757
Cdd:cd01948 81 gPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 758 GYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDAQR 837
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
416-838 |
1.61e-95 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 317.10 E-value: 1.61e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 416 EAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAEKagkSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRD 495
Cdd:PRK11359 367 KSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKA---VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKP 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 496 QDMVARLGGDEFVVVStHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALapEHGGDPRGLLRCADVAMYEAK 575
Cdd:PRK11359 444 DQYLCRIEGTQFVLVS-LENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 576 AAGRNTWRFYLEAMDSHLAEKKLRETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEE 655
Cdd:PRK11359 521 KNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEE 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 656 SDLIVQIGNWVLREACATAASWPGEVM----VSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGA 731
Cdd:PRK11359 601 IGEIENIGRWVIAEACRQLAEWRSQNIhipaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEI 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 732 LRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEG 811
Cdd:PRK11359 681 FKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKE 760
|
410 420
....*....|....*....|....*..
gi 518201632 812 QMHILRDEQCHELQGFLLSRPLDAQRL 838
Cdd:PRK11359 761 QFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
600-833 |
8.20e-94 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 294.51 E-value: 8.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 600 ETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASW-- 677
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWqa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 678 --PGEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYS 755
Cdd:smart00052 81 qgPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518201632 756 SLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPL 833
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
602-832 |
7.13e-74 |
|
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: 241.45 E-value: 7.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 602 ELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASW--PG 679
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 680 EVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSLGY 759
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518201632 760 LRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRP 832
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
416-833 |
3.90e-69 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 241.77 E-value: 3.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 416 EAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAEKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRD 495
Cdd:PRK11829 223 DAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDD 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 496 QDMVARLGGDEFVVVSTHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAK 575
Cdd:PRK11829 303 SDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 576 AAGRNTWRFYleamDSHLAEK-KLR---ETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIG 651
Cdd:PRK11829 383 HEGRNQIMVF----EPHLIEKtHKRltqENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVH 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 652 LAEESDLIVQIGNWVLREACATAASWPGE---VMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDV 728
Cdd:PRK11829 459 FAEEEGMMVPLGNWVLEEACRILADWKARgvsLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 729 DGALRTMTALKELGVRLNMDDFGTGYSSLGYLR---TYPFDSIKIDKRFVASMEKtgrDRSIVQAIINLGNALNLRVTAE 805
Cdd:PRK11829 539 DEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLPE---DDAIARIISCVSDVLKVRVMAE 615
|
410 420
....*....|....*....|....*...
gi 518201632 806 GVETEGQMHILRDEQCHELQGFLLSRPL 833
Cdd:PRK11829 616 GVETEEQRQWLLEHGIQCGQGFLFSPPL 643
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
600-853 |
4.24e-66 |
|
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: 230.19 E-value: 4.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 600 ETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREACATAASWPG 679
Cdd:COG4943 273 RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 680 E---VMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLnDVDGALRTMTALKELGVRLNMDDFGTGYSS 756
Cdd:COG4943 353 AdpdFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFGTGYSS 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 757 LGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDAQ 836
Cdd:COG4943 432 LSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAE 511
|
250
....*....|....*..
gi 518201632 837 RLRDLLEREAGQTQAPQ 853
Cdd:COG4943 512 EFIAWLAAQRAPASAPA 528
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
417-833 |
7.68e-66 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 232.68 E-value: 7.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 417 AHAKIQHLSLHDALTGLPNRNKLFQFLERLLAekaGKSPVAVLMLdldRFKPINDQHG---HPAGDAVLYAIAERLRAST 493
Cdd:PRK13561 223 QYEEQSRNATRFPVSDLPNKALLMALLEQVVA---RKQTTALMII---TCETLRDTAGvlkEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 494 RDQDMVARLGGDEFVVVSTHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALapEHGGDPRG-LLRCADVAMY 572
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAM--FYGDLTAEqLYSRAISAAF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 573 EAKAAGRNTWRFYlEAMDSHLAEKKL-RETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIG 651
Cdd:PRK13561 375 TARRKGKNQIQFF-DPQQMEAAQKRLtEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLID 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 652 LAEESDLIVQIGNWVLREACATAASWPG---EVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDV 728
Cdd:PRK13561 454 RIESCGLMVTVGHWVLEESCRLLAAWQErgiMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 729 DGALRTMTALKELGVRLNMDDFGTGYSSLGYL---RTYPFDSIKIDKRFVASMEKtgrDRSIVQAIINLGNALNLRVTAE 805
Cdd:PRK13561 534 HAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAE 610
|
410 420
....*....|....*....|....*...
gi 518201632 806 GVETEGQMHILRDEQCHELQGFLLSRPL 833
Cdd:PRK13561 611 GVETEAQRDWLLKAGVGIAQGFLFARAL 638
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
426-583 |
2.07e-61 |
|
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: 204.71 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 426 LHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARLGG 504
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARaRRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518201632 505 DEFVVVSTHVSSKlEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAKAAGRNTWR 583
Cdd:cd01949 81 DEFAILLPGTDLE-EAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
409-585 |
4.72e-61 |
|
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: 208.29 E-value: 4.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 409 ADITDEVEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAE 487
Cdd:COG2199 98 EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARaRREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVAR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 488 RLRASTRDQDMVARLGGDEFVVVSTHVSSKlEIEKFCSRLIDVINR-EVAYEGHSFHVGASIGVALAPEHGGDPRGLLRC 566
Cdd:COG2199 178 RLRASLRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRR 256
|
170
....*....|....*....
gi 518201632 567 ADVAMYEAKAAGRNTWRFY 585
Cdd:COG2199 257 ADLALYRAKRAGRNRVVVY 275
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
405-832 |
2.13e-56 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 211.07 E-value: 2.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 405 RGTAADITDEVEAHAKIQHLS---LHDALTGLPNRNKLFQFLERLLAEKAGKSPVAVL-MLDLDRFKPINDQHGHPAGDA 480
Cdd:PRK09776 642 IGSVLVIQDVTESRKMLRQLSysaSHDALTHLANRASFEKQLRRLLQTVNSTHQRHALvFIDLDRFKAVNDSAGHAAGDA 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 481 VLYAIAERLRASTRDQDMVARLGGDEFVVVSTHVSSKlEIEKFCSRLIDVIN-REVAYEGHSFHVGASIGVALAPEHGGD 559
Cdd:PRK09776 722 LLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVE-SARFIATRIISAINdYHFPWEGRVYRVGASAGITLIDANNHQ 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 560 PRGLLRCADVAMYEAKAAGRNTWRFY----LEAMDSHlaEKKLRETELRAALQNGEFELYYQ---PRflaQEQTIASAEA 632
Cdd:PRK09776 801 ASEVMSQADIACYAAKNAGRGRVTVYepqqAAAHSEH--RALSLAEQWRMIKENQLMMLAHGvasPR---IPEARNHWLI 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 633 LIRWNHPRRGLIGPDEFIGLAEESDLIVQIGNWVLREAC---ATAASWPGeVMVSVNVSPAQFMTGDIVWQVREALRLAR 709
Cdd:PRK09776 876 SLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFrqaAKAVASKG-LSIALPLSVAGLSSPTLLPFLLEQLENSP 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 710 LDARRLELEVTENVMLNDVDGALRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQ 789
Cdd:PRK09776 955 LPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLIS 1034
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 518201632 790 AIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRP 832
Cdd:PRK09776 1035 IIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
425-580 |
2.99e-55 |
|
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: 187.85 E-value: 2.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 425 SLHDALTGLPNRNKLFQFLERLL--AEKAGkSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARL 502
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELqrALREG-SPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 503 GGDEFVVVSTHVSSK--LEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAKAAGRN 580
Cdd:pfam00990 80 GGDEFAILLPETSLEgaQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
423-585 |
7.20e-52 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 178.60 E-value: 7.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 423 HLSLHDALTGLPNRNKLFQFLERLL-AEKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVAR 501
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELqRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 502 LGGDEFVVVSTHVSSKlEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAKAAGRNT 581
Cdd:smart00267 81 LGGDEFALLLPETSLE-EAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 518201632 582 WRFY 585
Cdd:smart00267 160 VAVY 163
|
|
| CHASE4 |
COG3322 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
35-731 |
7.16e-45 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442551 [Multi-domain] Cd Length: 724 Bit Score: 173.20 E-value: 7.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 35 WAILHIARHQDDIAIEQSHFYVEKALQNRRENSEQFSTTYSFWTDAYVYLGNRvdvDWAFTKNNLGSVLYTTNGYDGVFV 114
Cdd:COG3322 28 LILLSSFSELEEQAAERDVERVLNALDAELDQLARLVADWAVWDDTYEFVQDG---DPEWIESNLGDWTFENLGLDLVLV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 115 IDDRGT-RYAMleGELSERSLADSLNADTGDILRSAR---RAAVDEAAISRYVDFDGAPAILVASAIKPTSDHAPIdlak 190
Cdd:COG3322 105 LDPDGRlVYSK--GYDLEDGELVPLPEALAPLLARARallRHASPDSSVSGLLRLDGGPALVAARPILPSDGPGPP---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 191 ASVMVFVDRLTPAKLAKLGGDYGIaNLHLLAGGAAGDKESLALEGTPHR-----------------LAWVSSRP----GS 249
Cdd:COG3322 179 RGTLVFGRYLDEAFLARLAERTGL-DLTLSPADPPAPPDQVVEPLSDDTiagyvplrdidgqpvllLRWTPPRPiyqqGR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 250 AMLRETALPLLGIFVLAAGLLFWLSRSAVLNARavdrqqkvlkrsnqaLLASEERFKSIAEAASDWIWEVDGHFVFTYLS 329
Cdd:COG3322 258 ALLRYLLPALLLLGLLLALLALLLLRLVLLLLL---------------LLLRLVLSRLLLLLLRLLLLELLRALELLLLL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 330 VRFRDVTGYQPEAWIGRRLDELLDSDTVNIVKWLEGLPDADAPSSLVCAFRDSQGQARVGKLSASAIRNGVASGYRGTAA 409
Cdd:COG3322 323 LRRLLLLLLLLRLLLLLLDLLAALNLLLLLRALAERLVALALLALLLLGLLGLLAALRRLGLLAILALAEEAARLLLLAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 410 DITDEVEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAEKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERL 489
Cdd:COG3322 403 AIAGELLIGIEVLLALGLELAGSAIALARAAAALALLLAAAAAARLAARAASGLLRDLLEADELEDRLRRALLAEAAALL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 490 RASTRDQDMVARLGGDEFVVVSTHVSSKLEIEKFCSRLIDVINREVAYEGHSFHVGASIGVALAPEHGGDPRGLLRCADV 569
Cdd:COG3322 483 LLALLALELLLALGDAALEILLAILLLGLVLEAQLAELERLLLLGEAGGELLEEIALLAALLAGLLLAVLLSLLLRLLLL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 570 AMYEAKAAGRNTWRFYLEAMDSHLAEKKLRETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEF 649
Cdd:COG3322 563 IDALVALAEAAAGLLEALLEEEVELRRALLEAEELLLIALALLSLGLALALDDGGRGLAGLLLLFRLSGIGLLLLRRLLG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 650 IGLAEESDLIVQIGNWVLREACATAASWPGEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVD 729
Cdd:COG3322 643 DDLLGLLAALIDLILALAGSLLLLTLAAAAEATAVVLVAELLEGALLLQALALISLLELLLLLLLLELQLLEQVLSAPAA 722
|
..
gi 518201632 730 GA 731
Cdd:COG3322 723 LA 724
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
424-581 |
6.98e-43 |
|
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: 153.26 E-value: 6.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 424 LSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARL 502
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRaRRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 503 GGDEFVVVSTHVSSKLEIEKfCSRLIDVINREVAY--EGHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAKAAGRN 580
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSK-AERLRDAINSKPIEvaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
.
gi 518201632 581 T 581
Cdd:TIGR00254 160 R 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
600-840 |
6.85e-41 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 158.23 E-value: 6.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 600 ETELRAALQNGEFELYYQPRFLAQEQTIASAEALIRWNHPRRGLIGPDEFIGLAEESDLIV----QIGNWVLREACATAA 675
Cdd:PRK10551 265 GKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVpltqHLFELIARDAAELQK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 676 SWPGEVMVSVNVSPAQFMTGDIVWQVREALRLARLDARRLELEVTENVMLNDVDgALRTMTALKELGVRLNMDDFGTGYS 755
Cdd:PRK10551 345 VLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEE-ATKLFAWLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 756 SLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDA 835
Cdd:PRK10551 424 ALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPL 503
|
....*
gi 518201632 836 QRLRD 840
Cdd:PRK10551 504 EDFVR 508
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
418-580 |
3.14e-31 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 124.41 E-value: 3.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 418 HAKIQHLSLHDALTGLPNRNKLFQFLERLLAeKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQD 497
Cdd:PRK09894 122 IYLLTIRSNMDVLTGLPGRRVLDESFDHQLR-NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 498 MVARLGGDEFVVV---STHVSSKLEIEKFCSrliDVINREVAYEGHSFHVGASIGVALAPEhGGDPRGLLRCADVAMYEA 574
Cdd:PRK09894 201 TVYRYGGEEFIIClkaATDEEACRAGERIRQ---LIANHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEG 276
|
....*.
gi 518201632 575 KAAGRN 580
Cdd:PRK09894 277 KQTGRN 282
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
424-580 |
2.41e-29 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 122.32 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 424 LSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARL 502
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERaNERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 503 GGDEFVVVSTHVSskleIEKfCSRLIDVINREVAYE-------GHSFHVGASIGVALAPEHGGDPRGLLRCADVAMYEAK 575
Cdd:PRK09581 371 GGEEFVVVMPDTD----IED-AIAVAERIRRKIAEEpfiisdgKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAK 445
|
....*
gi 518201632 576 AAGRN 580
Cdd:PRK09581 446 NTGRN 450
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
420-580 |
2.97e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 117.42 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 420 KIQHLSLHDALTGLPNRNKLFQFLERLLAE-KAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQDM 498
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRGALFEKARALAKRcQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 499 VARLGGDEFVVVSTHVSSKlEIEKFCSRLIDVINRE--VAYEGHSFHVGASIGVALAPEHG-GDPRGLLRCADVAMYEAK 575
Cdd:PRK15426 473 AGRVGGEEFCVVLPGASLA-EAAQVAERIRLRINEKeiLVAKSTTIRISASLGVSSAEEDGdYDFEQLQSLADRRLYLAK 551
|
....*
gi 518201632 576 AAGRN 580
Cdd:PRK15426 552 QAGRN 556
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
418-575 |
5.46e-25 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 108.56 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 418 HAKIQHLSLHDALTGLPNRNKLFQFLERLLAEKAGKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQD 497
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518201632 498 MVARLGGDEFVVVSTHVSSKLEIEKFCSRLIDVINREVA-YEGHSFHVGASIGVALAPEHGGDPRgLLRCADVAMYEAK 575
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDlHNGHQTTMTLSIGYAMTIEHASAEK-LQELADHNMYQAK 398
|
|
| CHASE4 |
pfam05228 |
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various ... |
59-220 |
1.77e-20 |
|
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in prokaryotes. Specifically, CHASE4 domains are found in histidine kinases in Archaea and in predicted diguanylate cyclases/phosphodiesterases in Bacteria. Environmental factors that are recognized by CHASE4 domains are not known at this time.
Pssm-ID: 428380 Cd Length: 139 Bit Score: 88.15 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 59 ALQNRRENSEQFSTTYSFWTDAYVYLGNRvdvDWAFTKNNLGSVLYTTNGYDGVFVIDDRGT-RYAMLEGELSERSLADS 137
Cdd:pfam05228 1 ALEQELDSLDRLLRDWAVWDDTYDFVQDG---NPDYIESNLGPETFENLGLDLILFVDADGKlVYDLENGKPDSPLLSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 138 LNADtgdilrsarraavdeaAISRYVDFDGAPAILVASAIKPTSDHAPIdlakASVMVFVDRLTPAKLAKLgGDYGIANL 217
Cdd:pfam05228 78 SPDS----------------GLSGIVLLGGGPALVAARPILTSDGSGPP----RGTLVMGRYLDEAFLDRL-SELTLLDL 136
|
...
gi 518201632 218 HLL 220
Cdd:pfam05228 137 TLS 139
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
416-580 |
2.65e-16 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 81.41 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 416 EAHAKIQHLSLHDALTGLPNRnKLFQFLERLLAEKA--GKSPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRAST 493
Cdd:PRK10245 196 EHKRRLQVMSTRDGMTGVYNR-RHWETLLRNEFDNCrrHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 494 RDQDMVARLGGDEFVVVSTHVSSKLEIEKFcSRLIDVINREVAYEGHSFHVGASIGVA-LAPEHgGDPRGLLRCADVAMY 572
Cdd:PRK10245 275 RGSDVIGRFGGDEFAVIMSGTPAESAITAM-SRVHEGLNTLRLPNAPQVTLRISVGVApLNPQM-SHYREWLKSADLALY 352
|
....*...
gi 518201632 573 EAKAAGRN 580
Cdd:PRK10245 353 KAKNAGRN 360
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
428-834 |
3.01e-16 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 82.99 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 428 DALTGLPNRnkLFqFLERL--LAEKAGK--SPVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLRASTRDQD--MVAR 501
Cdd:PRK11059 231 DAKTGLGNR--LF-FDNQLatLLEDQEMvgAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPgaLLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 502 LGGDEFVVVSTHVSSKlEIEKFCSRLI---------DVINREVAyeghsFHvgasIGVALApeHGGDPRG-LLRCADVAM 571
Cdd:PRK11059 308 YSRSDFAVLLPHRSLK-EADSLASQLLkavdalpppKMLDRDDF-----LH----IGICAY--RSGQSTEqVMEEAEMAL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 572 YEAKAAGRNTWRFYLEAMDSHLAEKKLR-ETELRAALQNGEFELYYQPRFLAqEQTIASAEALIRWNHPRRGLIGPDEFI 650
Cdd:PRK11059 376 RSAQLQGGNGWFVYDKAQLPEKGRGSVRwRTLLEQTLVRGGPRLYQQPAVTR-DGKVHHRELFCRIRDGQGELLSAELFM 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 651 GLAEESDLIVQIGNWVLREACATAASWPGEVMvSVNVSPAQFMTGDIVWQVREAL-RLARLDARRLELEVTENVMLNDVD 729
Cdd:PRK11059 455 PMVQQLGLSEQYDRQVIERVLPLLRYWPEENL-SINLSVDSLLSRAFQRWLRDTLlQCPRSQRKRLIFELAEADVCQHIS 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 730 GALRTMTALKELGVRLNMDDFGTGYSSLGYLRTYPFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVET 809
Cdd:PRK11059 534 RLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVES 613
|
410 420
....*....|....*....|....*..
gi 518201632 810 EGQMHILRDEQCHELQG--FLLSRPLD 834
Cdd:PRK11059 614 REEWQTLQELGVSGGQGdfFAESQPLD 640
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
293-535 |
1.57e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 68.51 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 293 RSNQALLASEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDELLDSDTVN-IVKWLEGLPDADA 371
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDeFLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 372 PSSLVCAFRDSQGQARVGKLSASAIRN--GVASGYRGTAADITDEVEAHAKIQHLSLHDALTGLPNRNKLFQFLERLLAE 449
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDedGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 450 KAGKSPVAVLMLDLDRF--KPINDQHGHPAGDAVLYAIAERLRASTRDQDMVARLGGDEFVVVSTHVSSKLEIEKFCSRL 527
Cdd:COG2202 161 YVNPAAEELLGYSPEELlgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGGEVIG 240
|
....*...
gi 518201632 528 IDVINREV 535
Cdd:COG2202 241 VLGIVRDI 248
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
292-421 |
4.99e-11 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 63.89 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 292 KRSNQALLASEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDELLDSDTVNIVK--WLEGLPDA 369
Cdd:COG2202 126 KRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLelLRRLLEGG 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 518201632 370 DAPSSLVCAFRDSQGQARVgkLSASAIR---NGVASGYRGTAADITDEVEAHAKI 421
Cdd:COG2202 206 RESYELELRLKDGDGRWVW--VEASAVPlrdGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
681-841 |
1.28e-09 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 59.63 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 681 VMVSVNVSpaqfmtGDIVWQVREALRLARLDARR--LELEVTENVMLNDVDgalrTMTALKELGvRLNMDDFGTG---YS 755
Cdd:PRK11596 100 LLASVNID------GPTLIALRQQPAILRLIERLpwLRFELVEHIRLPKDS----PFASMCEFG-PLWLDDFGTGmanFS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 756 SLGYLRtypFDSIKIDKRFVASMEKTGRDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRPLDA 835
Cdd:PRK11596 169 ALSEVR---YDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPF 245
|
....*.
gi 518201632 836 QRLRDL 841
Cdd:PRK11596 246 ETLETL 251
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
301-421 |
1.04e-08 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 54.22 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 301 SEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDELLDSDTVNIVKW-----LEGLPdadAPSSL 375
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRErierrLEGEP---EPVSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 518201632 376 VCAFRDSQGQARVGKLSASAIR-NGVASGYRGTAADITDEVEAHAKI 421
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEVSVSPIRtNGGELGVVGIVRDITERKEAEEAL 124
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
455-559 |
2.29e-08 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 53.51 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 455 PVAVLMLDLDRFKPINDQHGHPAGDAVLYAIAERLR-ASTRDQDMVARLGGDEFVVVS--THVSSKLEiekFCSRLIDVI 531
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDsLIRRSGDLKIKTIGDEFMVVSglDHPAAAVA---FAEDMREAV 77
|
90 100
....*....|....*....|....*...
gi 518201632 532 NREVAYEGHsfHVGASIGVALAPEHGGD 559
Cdd:cd07556 78 SALNQSEGN--PVRVRIGIHTGPVVVGV 103
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
497-575 |
2.92e-07 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 51.45 E-value: 2.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518201632 497 DMVARLGGDEFVVVSTHVSSKlEIEKFCSRLidvinREVAYEGHSFHVGASIGVALAPehggdprgLLRCADvAMYEAK 575
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLE-GALAVAERI-----REAVAELPSLRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
685-832 |
3.51e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 53.65 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 685 VNVSPAqFMTGDIvwqvrealrLARLDARRLELEVTENVmlnDVDGAL-RTMTALKELGVRLNMDDFGtgySSLGYLRTY 763
Cdd:COG3434 66 INFTEE-LLLSDL---------PELLPPERVVLEILEDV---EPDEELlEALKELKEKGYRIALDDFV---LDPEWDPLL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 764 PF-DSIKIDkrfVASMektgrDRSIVQAIINLGNALNLRVTAEGVETEGQMHILRDEQCHELQGFLLSRP 832
Cdd:COG3434 130 PLaDIIKID---VLAL-----DLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
303-355 |
3.10e-06 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 45.47 E-value: 3.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 518201632 303 ERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDELLDSD 355
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPE 53
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
312-411 |
7.18e-06 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 45.32 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 312 ASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDELLDSDTVNIVK-WLEGLPDADAPSSLVCAFRDSQGQARVGK 390
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELReRLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 518201632 391 LSASAIRNGVAS--GYRGTAADI 411
Cdd:cd00130 81 VSLTPIRDEGGEviGLLGVVRDI 103
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
297-433 |
9.11e-04 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 42.53 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518201632 297 ALLASEERFKSIAEAASDWIWEVDGHFVFTYLSVRFRDVTGYQPEAWIGRRLDELLDSDTVnIVKWLEGLPDADAPSSLV 376
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP-LRELLERALAEGQPVTER 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518201632 377 -CAFRDSQGQARVGKLSASAIRNGVASGYR-GTAADITDEVEAHAKIQHLSLHDALTGL 433
Cdd:COG3852 80 eVTLRRKDGEERPVDVSVSPLRDAEGEGGVlLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| |
