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Conserved domains on  [gi|1816455706|ref|WP_163470296|]
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EAL domain-containing protein [Fusobacterium sp. IOR10]

Protein Classification

EAL domain-containing protein( domain architecture ID 10005623)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase; similar to Borreliella burgdorferi cyclic di-GMP phosphodiesterase PdeA that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to pGpG

CATH:  3.20.20.450
EC:  3.1.4.52
Gene Ontology:  GO:0071111
PubMed:  15306016|26055114|19756011
SCOP:  4002400

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 470-849 6.05e-63

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: 222.74  E-value: 6.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 470 LNLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLKFRLYGDVFFILF----------EDLTYKK 539
Cdd:COG2200   179 LLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLllllaaaaaaAAALRLL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 540 FEKDIKDWETFIDEKFLVSVSIGKAWSDSDIDLNKLCTNAEEFLKYSKE------EYYDKKRIEELQKFKRKIKFMEQLK 613
Cdd:COG2200   259 LLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGggrgrvVFFAAAEARARRRLALESELREALE 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 614 EGNYRMHLQPKANAENGEIFGAEALTRLYLNN-EIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLiKIS 692
Cdd:COG2200   339 EGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDL-RLS 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 693 LNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIYMY 772
Cdd:COG2200   418 VNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLP 497

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816455706 773 FNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEEL 849
Cdd:COG2200   498 PDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 470-849 6.05e-63

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: 222.74  E-value: 6.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 470 LNLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLKFRLYGDVFFILF----------EDLTYKK 539
Cdd:COG2200   179 LLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLllllaaaaaaAAALRLL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 540 FEKDIKDWETFIDEKFLVSVSIGKAWSDSDIDLNKLCTNAEEFLKYSKE------EYYDKKRIEELQKFKRKIKFMEQLK 613
Cdd:COG2200   259 LLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGggrgrvVFFAAAEARARRRLALESELREALE 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 614 EGNYRMHLQPKANAENGEIFGAEALTRLYLNN-EIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLiKIS 692
Cdd:COG2200   339 EGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDL-RLS 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 693 LNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIYMY 772
Cdd:COG2200   418 VNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLP 497

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816455706 773 FNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEEL 849
Cdd:COG2200   498 PDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 610-845 7.18e-57

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: 195.07  E-value: 7.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 610 EQLKEGNYRMHLQPKANAENGEIFGAEALTRLYL-NNEIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKL 688
Cdd:cd01948     5 RALERGEFELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 689 iKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVL 768
Cdd:cd01948    85 -RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816455706 769 IYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSH 845
Cdd:cd01948   164 KRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 612-843 4.92e-54

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 187.42  E-value: 4.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  612 LKEGNYRMHLQPKANAENGEIFGAEALTRL-YLNNEIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLIK 690
Cdd:smart00052   8 LENGQFLLYYQPIVSLRTGRLVGVEALIRWqHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGPPPLL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  691 ISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNmavLIY 770
Cdd:smart00052  88 ISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS---LSY 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816455706  771 MY---FNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPV 843
Cdd:smart00052 165 LKrlpVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 608-840 1.98e-53

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: 185.60  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 608 FMEQLKEGNYRMHLQPKANAENGEIFGAEALTRLYL-NNEIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGK 686
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 687 klIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMA 766
Cdd:pfam00563  84 --IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816455706 767 VLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKP 840
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 450-844 3.03e-46

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 178.04  E-value: 3.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 450 KYDQLTGLLNHSSYGKKIDKLnLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLKF-RLYGDVF 528
Cdd:PRK11359  377 QFDPLTGLPNRNNLHNYLDDL-VDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLcRIEGTQF 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 529 FILFEDLTYKKFE------KDIKDWETFIDEK-FLVSVSIGKAWsDSDIDLNKLCTNAEEFLKYSKEE---YYDKKRIEE 598
Cdd:PRK11359  456 VLVSLENDVSNITqiadelRNVVSKPIMIDDKpFPLTLSIGISY-DVGKNRDYLLSTAHNAMDYIRKNggnGWQFFSPAM 534

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 599 LQKFKRKIKFMEQLKE----GNYRMHLQPKANAENGEIFGAEALTRLY--LNNEIqSPYKFIPQLERDGFIKYLDKYIFE 672
Cdd:PRK11359  535 NEMVKERLVLGAALKEaisnNQLKLVYQPQIFAETGELYGIEALARWHdpLHGHV-PPSRFIPLAEEIGEIENIGRWVIA 613

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 673 EVCKLLEKWIKEGKKLIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIG-ELDKESIKSIcSKITRKGF 751
Cdd:PRK11359  614 EACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMmEHDTEIFKRI-QILRDMGV 692

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 752 LISLDDFGAKYSNMAVLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEA 831
Cdd:PRK11359  693 GLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV 772

                         410
                  ....*....|...
gi 1816455706 832 VQGYLFNKPIPVS 844
Cdd:PRK11359  773 IQGYFFSRPLPAE 785
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 452-508 3.76e-03

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: 38.86  E-value: 3.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816455706 452 DQLTGLLNHSSYGKKIDKL----NLESLSsLGVLYIDINDFKNINLVSGREYGDNILKEMS 508
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSElkraRRFQRS-FSVLMIDIDNFKKINDTLGHDVGDEVLREVA 64
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 470-849 6.05e-63

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: 222.74  E-value: 6.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 470 LNLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLKFRLYGDVFFILF----------EDLTYKK 539
Cdd:COG2200   179 LLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLllllaaaaaaAAALRLL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 540 FEKDIKDWETFIDEKFLVSVSIGKAWSDSDIDLNKLCTNAEEFLKYSKE------EYYDKKRIEELQKFKRKIKFMEQLK 613
Cdd:COG2200   259 LLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGggrgrvVFFAAAEARARRRLALESELREALE 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 614 EGNYRMHLQPKANAENGEIFGAEALTRLYLNN-EIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLiKIS 692
Cdd:COG2200   339 EGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDL-RLS 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 693 LNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIYMY 772
Cdd:COG2200   418 VNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLP 497

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816455706 773 FNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEEL 849
Cdd:COG2200   498 PDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 451-850 1.47e-61

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: 220.80  E-value: 1.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 451 YDQLTGLLNHSSYGKKIDKL---NLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSfndyFQTNLK-----FR 522
Cdd:COG5001   253 HDPLTGLPNRRLFLDRLEQAlarARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARR----LRACLRegdtvAR 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 523 LYGDVFFILFEDLTykkfekDIKDWETFI--------------DEKFLVSVSIGKAWSDSDidlnklCTNAEEFLKY--- 585
Cdd:COG5001   329 LGGDEFAVLLPDLD------DPEDAEAVAerilaalaepfeldGHELYVSASIGIALYPDD------GADAEELLRNadl 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 586 ----SKEE------YYDKKRIEELQkfkRKIKfMEQ-----LKEGNYRMHLQPKANAENGEIFGAEALTRlyLNNEIQ-- 648
Cdd:COG5001   397 amyrAKAAgrnryrFFDPEMDERAR---ERLE-LEAdlrraLERGELELHYQPQVDLATGRIVGAEALLR--WQHPERgl 470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 649 -SPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEM 727
Cdd:COG5001   471 vSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEI 550

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 728 TETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIYMYFNTIKIDKSLINDVITNDkskiiiknifkickE-- 805
Cdd:COG5001   551 TESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDP--------------Dda 616

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1816455706 806 ------------LKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEELY 850
Cdd:COG5001   617 aivraiialahsLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALL 673
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 610-845 7.18e-57

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: 195.07  E-value: 7.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 610 EQLKEGNYRMHLQPKANAENGEIFGAEALTRLYL-NNEIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKL 688
Cdd:cd01948     5 RALERGEFELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 689 iKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVL 768
Cdd:cd01948    85 -RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816455706 769 IYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSH 845
Cdd:cd01948   164 KRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 612-843 4.92e-54

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 187.42  E-value: 4.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  612 LKEGNYRMHLQPKANAENGEIFGAEALTRL-YLNNEIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLIK 690
Cdd:smart00052   8 LENGQFLLYYQPIVSLRTGRLVGVEALIRWqHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGPPPLL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  691 ISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNmavLIY 770
Cdd:smart00052  88 ISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS---LSY 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816455706  771 MY---FNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPV 843
Cdd:smart00052 165 LKrlpVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 608-840 1.98e-53

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: 185.60  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 608 FMEQLKEGNYRMHLQPKANAENGEIFGAEALTRLYL-NNEIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGK 686
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 687 klIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMA 766
Cdd:pfam00563  84 --IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816455706 767 VLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKP 840
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 450-844 3.03e-46

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 178.04  E-value: 3.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 450 KYDQLTGLLNHSSYGKKIDKLnLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLKF-RLYGDVF 528
Cdd:PRK11359  377 QFDPLTGLPNRNNLHNYLDDL-VDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLcRIEGTQF 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 529 FILFEDLTYKKFE------KDIKDWETFIDEK-FLVSVSIGKAWsDSDIDLNKLCTNAEEFLKYSKEE---YYDKKRIEE 598
Cdd:PRK11359  456 VLVSLENDVSNITqiadelRNVVSKPIMIDDKpFPLTLSIGISY-DVGKNRDYLLSTAHNAMDYIRKNggnGWQFFSPAM 534

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 599 LQKFKRKIKFMEQLKE----GNYRMHLQPKANAENGEIFGAEALTRLY--LNNEIqSPYKFIPQLERDGFIKYLDKYIFE 672
Cdd:PRK11359  535 NEMVKERLVLGAALKEaisnNQLKLVYQPQIFAETGELYGIEALARWHdpLHGHV-PPSRFIPLAEEIGEIENIGRWVIA 613

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 673 EVCKLLEKWIKEGKKLIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIG-ELDKESIKSIcSKITRKGF 751
Cdd:PRK11359  614 EACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMmEHDTEIFKRI-QILRDMGV 692

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 752 LISLDDFGAKYSNMAVLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEA 831
Cdd:PRK11359  693 GLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV 772

                         410
                  ....*....|...
gi 1816455706 832 VQGYLFNKPIPVS 844
Cdd:PRK11359  773 IQGYFFSRPLPAE 785
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 612-850 3.78e-39

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: 153.15  E-value: 3.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 612 LKEGNYRMHLQPKANAENGEIFGAEALTRLYLNN-EIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLiK 690
Cdd:COG4943   280 IKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDgSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDF-H 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 691 ISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETiGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIY 770
Cdd:COG4943   359 ISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITER-GFIDPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQT 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 771 MYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEELY 850
Cdd:COG4943   438 LPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWL 517
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
452-850 8.37e-36

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 144.82  E-value: 8.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 452 DQLTGLLNHSSYGKKI-DKLNLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLKF-RLYGDVFF 529
Cdd:PRK10060  240 DSITGLPNRNAIQELIdHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLaRLGGDEFL 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 530 ILFEDLTYKKFEKDIKDWETFIDEKF---LVSV----SIGKA-WSDSDIDLNKLCTNAEEFLKYSKEEYYDKKRIEELQK 601
Cdd:PRK10060  320 VLASHTSQAALEAMASRILTRLRLPFrigLIEVytgcSIGIAlAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEM 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 602 FKRKIKFM-------EQLKEGNYRMHLQPKANAeNGEIFGAEALTRlYLNNE--IQSPYKFIPQLERDGFIKYLDKYIFE 672
Cdd:PRK10060  400 NQRVFEYLwldtnlrKALENDQLVIHYQPKITW-RGEVRSLEALVR-WQSPErgLIPPLEFISYAEESGLIVPLGRWVML 477

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 673 EVCKLLEKWIKEGKKLiKISLNFS--RLTFMTpgIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKG 750
Cdd:PRK10060  478 DVVRQVAKWRDKGINL-RVAVNVSarQLADQT--IFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLG 554

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 751 FLISLDDFGAKYSNMAVLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCE 830
Cdd:PRK10060  555 AQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVN 634

                         410       420
                  ....*....|....*....|
gi 1816455706 831 AVQGYLFNKPIPVSHFEELY 850
Cdd:PRK10060  635 ERQGFLFAKPMPAVAFERWY 654
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 558-852 4.90e-34

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 139.08  E-value: 4.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 558 SVSIGKAWSDSDIdlnklctNAEEFLKYS-------------KEEYYDKKRIEELQK-FKRKIKFMEQLKEGNYRMHLQP 623
Cdd:PRK13561  348 SCSIGIAMFYGDL-------TAEQLYSRAisaaftarrkgknQIQFFDPQQMEAAQKrLTEESDILNALENHQFAIWLQP 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 624 KANAENGEIFGAEALTRLYLNN-EIQSPYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKKLiKISLNFSRLTFMT 702
Cdd:PRK13561  421 QVEMRSGKLVSAEALLRMQQPDgSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIML-PLSVNLSALQLMH 499

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 703 PGIVEEIIEISNKYNI-PREYIeIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIYMY---FNTIKI 778
Cdd:PRK13561  500 PNMVADMLELLTRYRIqPGTLI-LEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKI 578

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816455706 779 DKSLInDVITNDKSKIIIKNIFKICkeLKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEELYIK 852
Cdd:PRK13561  579 DKMFV-DGLPEDDSMVAAIIMLAQS--LNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEERYLE 649
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 609-850 4.48e-27

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 117.74  E-value: 4.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 609 MEQLKEGNYRMHLQPKANAENGEIFGAEALTRLYLNNEIQS-PYKFIPQLERDGFIKYLDKYIFEEVCKLLEKWIKEGKk 687
Cdd:PRK11829  411 LQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVlPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGV- 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 688 LIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTETIGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAV 767
Cdd:PRK11829  490 SLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRY 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 768 LIYMY---FNTIKIDKSLINDVITNDKSKIIIKNIFKIckeLKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVS 844
Cdd:PRK11829  570 LNHLKslpIHMIKLDKSFVKNLPEDDAIARIISCVSDV---LKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRA 646


                  ....*.
gi 1816455706 845 HFEELY 850
Cdd:PRK11829  647 EFEAQY 652
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
612-846 3.46e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 82.35  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 612 LKEGNYRMHLQPKANAENGEIFGAEALTRLY--LNNEIqSPYKFIPQLERDGFIKYLDKYIFEEVCK---LLEKWIKEGK 686
Cdd:PRK10551  272 IKRGQFYVEYQPVVDTQTLRVTGLEALLRWRhpTAGEI-PPDAFINYAEAQKLIVPLTQHLFELIARdaaELQKVLPVGA 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 687 KLikiSLNFSRLTFMTPGIVEEIIEISNkyNIPREYIEI--EMTETiGELDKESIKSICSKITRKGFLISLDDFGAKYSn 764
Cdd:PRK10551  351 KL---GINISPAHLHSDSFKADVQRLLA--SLPADHFQIvlEITER-DMVQEEEATKLFAWLHSQGIEIAIDDFGTGHS- 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 765 maVLIYM---YFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPI 841
Cdd:PRK10551  424 --ALIYLerfTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501


                  ....*
gi 1816455706 842 PVSHF 846
Cdd:PRK10551  502 PLEDF 506
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 451-589 1.41e-15

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: 74.90  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 451 YDQLTGLLNHSSYGKKIDKLNLESL---SSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYF-QTNLKFRLYGD 526
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLrESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816455706 527 VFFILFEDLTY-------KKFEKDIKDWETFIDEKFLVSVSIGKA-WSDSDIDLNKLCTNAEEFLKYSKEE 589
Cdd:cd01949    82 EFAILLPGTDLeeaealaERLREAIEEPFFIDGQEIRVTASIGIAtYPEDGEDAEELLRRADEALYRAKRS 152
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 447-846 6.95e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 79.33  E-value: 6.95e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  447 YTGKYDQLTGLLNHSSYGKKIDKLnLESLSSLG----VLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQ-TNLKF 521
Cdd:PRK09776   663 YSASHDALTHLANRASFEKQLRRL-LQTVNSTHqrhaLVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRsSDVLA 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  522 RLYGDVFFILFEDLTYKKFE-------KDIKD----WEtfiDEKFLVSVSIGKAWSDSDIDLnklctnAEEFLKYSKEEY 590
Cdd:PRK09776   742 RLGGDEFGLLLPDCNVESARfiatriiSAINDyhfpWE---GRVYRVGASAGITLIDANNHQ------ASEVMSQADIAC 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  591 YDKKRI------------EELQKFKRKIKFMEQLKEG--NYRMHLQ-----PKANAENGEIfgaEALTRLYL-NNEIQSP 650
Cdd:PRK09776   813 YAAKNAgrgrvtvyepqqAAAHSEHRALSLAEQWRMIkeNQLMMLAhgvasPRIPEARNHW---LISLRLWDpEGEIIDE 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  651 YKFIPQLERDGFIKYLDKYIFEEVckLLEKWIKEGKKLIKISLNFSRLTFMTPGIVEEIIEISNKYNIPREYIEIEMTET 730
Cdd:PRK09776   890 GAFRPAAEDPALMHALDRRVIHEF--FRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITET 967

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  731 IGELDKESIKSICSKITRKGFLISLDDFGAKYSNMAVLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFKICKELKIDS 810
Cdd:PRK09776   968 ALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKT 1047

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1816455706  811 IAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHF 846
Cdd:PRK09776  1048 IAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 451-589 3.29e-13

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: 70.78  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 451 YDQLTGLLNHSSYGKKIDKLNLESL---SSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYF-QTNLKFRLYGD 526
Cdd:COG2199   116 HDPLTGLPNRRAFEERLERELARARregRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLrESDLVARLGGD 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816455706 527 VFFILFEDLTY-------KKFEKDIKDWETFIDEKFL-VSVSIGKA-WSDSDIDLNKLCTNAEEFLKYSKEE 589
Cdd:COG2199   196 EFAVLLPGTDLeeaealaERLREALEQLPFELEGKELrVTVSIGVAlYPEDGDSAEELLRRADLALYRAKRA 267
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 693-844 6.19e-11

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 65.21  E-value: 6.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 693 LNFSRLTFMtpgivEEIIEIsnkynIPREYIEIEMTETIgELDKESIKSiCSKITRKGFLISLDDFGAKYSNMAVLiyMY 772
Cdd:COG3434    66 INFTEELLL-----SDLPEL-----LPPERVVLEILEDV-EPDEELLEA-LKELKEKGYRIALDDFVLDPEWDPLL--PL 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816455706 773 FNTIKIDkslindVITNDKSKIIIKNIFKICKELKIdsIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVS 844
Cdd:COG3434   132 ADIIKID------VLALDLEELAELVARLKRYGIKL--LAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 451-583 3.26e-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: 50.71  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 451 YDQLTGLLNHSSYGKKIDKL--NLESL-SSLGVLYIDINDFKNINLVSGREYGDNILKEMSNsfndYFQTNLK-----FR 522
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQElqRALREgSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQ----RLSSSLRrsdlvAR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816455706 523 LYGDVFFILFEDLTYKKF-------EKDIKDWETFI---DEKFLVSVSIGKA-WSDSDIDLNKLCTNAEEFL 583
Cdd:pfam00990  79 LGGDEFAILLPETSLEGAqelaeriRRLLAKLKIPHtvsGLPLYVTISIGIAaYPNDGEDPEDLLKRADTAL 150
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 451-595 8.39e-07

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 49.55  E-value: 8.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  451 YDQLTGLLNHSSYGKKIDKL---NLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYF-QTNLKFRLYGD 526
Cdd:smart00267   5 RDPLTGLPNRRYFEEELEQElqrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLrPGDLLARLGGD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706  527 VFFILFEDLTY-----------KKFEKDIkdweTFIDEKFLVSVSIGKAWSDSDIDlnklctNAEEFLKYSKEEYYDKKR 595
Cdd:smart00267  85 EFALLLPETSLeeaialaerilQQLREPI----IIHGIPLYLTISIGVAAYPNPGE------DAEDLLKRADTALYQAKK 154
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 722-849 1.73e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 44.22  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 722 YIEIEMTETIGELDKESIKSICSKITrkgflISLDDFGAKYSNMAVLIYMYFNTIKIDKSLINDVITNDKSKIIIKNIFK 801
Cdd:PRK11596  129 WLRFELVEHIRLPKDSPFASMCEFGP-----LWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLH 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1816455706 802 ICKELKIDSIAEGVETEEQFTALKKLGCEAVQGYLFNKPIPVSHFEEL 849
Cdd:PRK11596  204 LMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLETL 251
PRK09966 PRK09966
diguanylate cyclase DgcN;
448-535 2.86e-04

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 44.23  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816455706 448 TGKYDQLTGLLNHSSYGKKIDKL--NLESLSSLGVLYIDINDFKNINLVSGREYGDNILKEMSNSFNDYFQTNLK-FRLY 524
Cdd:PRK09966  247 TALHDPLTGLANRAAFRSGINTLmnNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKaYRLG 326

                          90
                  ....*....|.
gi 1816455706 525 GDVFFILFEDL 535
Cdd:PRK09966  327 GDEFAMVLYDV 337
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 452-508 3.76e-03

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: 38.86  E-value: 3.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816455706 452 DQLTGLLNHSSYGKKIDKL----NLESLSsLGVLYIDINDFKNINLVSGREYGDNILKEMS 508
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSElkraRRFQRS-FSVLMIDIDNFKKINDTLGHDVGDEVLREVA 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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