NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2103763153|ref|WP_224252777|]
View 

MULTISPECIES: EAL domain-containing protein [Klebsiella]

Protein Classification

EAL domain-containing protein( domain architecture ID 10112612)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YjcC super family cl34845
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 8-250 3.06e-95

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG4943:

Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 289.51  E-value: 3.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   8 YTSEEEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMR 87
Cdd:COG4943   269 RLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLG 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  88 PLFNKLPDgFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVvDKLNRLHNCGFSIALDDFG 167
Cdd:COG4943   349 DLLAADPD-FHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAIDDFG 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 168 TGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWK 247
Cdd:COG4943   427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506


                  ...
gi 2103763153 248 PMP 250
Cdd:COG4943   507 PLP 509
 
Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 8-250 3.06e-95

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: 289.51  E-value: 3.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   8 YTSEEEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMR 87
Cdd:COG4943   269 RLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLG 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  88 PLFNKLPDgFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVvDKLNRLHNCGFSIALDDFG 167
Cdd:COG4943   349 DLLAADPD-FHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAIDDFG 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 168 TGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWK 247
Cdd:COG4943   427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506


                  ...
gi 2103763153 248 PMP 250
Cdd:COG4943   507 PLP 509
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 15-250 1.06e-86

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: 258.24  E-value: 1.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  15 LRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLfNKLP 94
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  95 DGFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTGYSGLS 174
Cdd:cd01948    82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2103763153 175 YLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPMP 250
Cdd:cd01948   162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 12-250 1.23e-86

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 257.92  E-value: 1.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   12 EEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLFN 91
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   92 KLPDGFHIGLNISASHINSPTFIDDCLHF--QRGFEgkAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTG 169
Cdd:smart00052  81 QGPPPLLISINLSARQLISPDLVPRVLELleETGLP--PQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  170 YSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPM 249
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238


                   .
gi 2103763153  250 P 250
Cdd:smart00052 239 P 239
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 12-248 2.80e-67

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: 208.71  E-value: 2.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  12 EEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLfn 91
Cdd:pfam00563   1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  92 KLPDGFHIGLNISASHINSPTFIDDCLHF-QRGFEGKAvKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTGY 170
Cdd:pfam00563  79 QLGPDIKLSINLSPASLADPGFLELLRALlKQAGPPPS-RLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2103763153 171 SGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKP 248
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
11-255 1.53e-61

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 202.14  E-value: 1.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  11 EEEKLRyAIAQG--YIVpyYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTR---SLMAQVTAQ 85
Cdd:PRK10551  265 GKEILT-GIKRGqfYVE--YQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQhlfELIARDAAE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  86 MRplfNKLPDGFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQeplllngAVVDKLNR------LHNCGF 159
Cdd:PRK10551  342 LQ---KVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITER-------DMVQEEEAtklfawLHSQGI 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 160 SIALDDFGTGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPL 239
Cdd:PRK10551  412 EIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNF 491

                         250
                  ....*....|....*.
gi 2103763153 240 LQGYFFWKPMPYVALV 255
Cdd:PRK10551  492 LQGYWISRPLPLEDFV 507
 
Name Accession Description Interval E-value
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 8-250 3.06e-95

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: 289.51  E-value: 3.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   8 YTSEEEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMR 87
Cdd:COG4943   269 RLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLG 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  88 PLFNKLPDgFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVvDKLNRLHNCGFSIALDDFG 167
Cdd:COG4943   349 DLLAADPD-FHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAIDDFG 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 168 TGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWK 247
Cdd:COG4943   427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506


                  ...
gi 2103763153 248 PMP 250
Cdd:COG4943   507 PLP 509
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 15-250 1.06e-86

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: 258.24  E-value: 1.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  15 LRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLfNKLP 94
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  95 DGFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTGYSGLS 174
Cdd:cd01948    82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2103763153 175 YLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPMP 250
Cdd:cd01948   162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 12-250 1.23e-86

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 257.92  E-value: 1.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   12 EEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLFN 91
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   92 KLPDGFHIGLNISASHINSPTFIDDCLHF--QRGFEgkAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTG 169
Cdd:smart00052  81 QGPPPLLISINLSARQLISPDLVPRVLELleETGLP--PQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  170 YSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPM 249
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238


                   .
gi 2103763153  250 P 250
Cdd:smart00052 239 P 239
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 12-262 6.83e-82

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: 258.94  E-value: 6.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  12 EEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNtttPSR---SPAEFIPLAERTGLIIPLTRSLMAQVTAQMRP 88
Cdd:COG5001   427 EADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQH---PERglvSPAEFIPLAEETGLIVPLGEWVLREACRQLAA 503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  89 LFNKLPDGFHIGLNISASHINSPTFID---DCLHfQRGFEGKAvkLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDD 165
Cdd:COG5001   504 WQDAGLPDLRVAVNLSARQLRDPDLVDrvrRALA-ETGLPPSR--LELEITESALLEDPEEALETLRALRALGVRIALDD 580

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 166 FGTGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFF 245
Cdd:COG5001   581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLF 660

                         250
                  ....*....|....*..
gi 2103763153 246 WKPMPYVALVMLLLSKP 262
Cdd:COG5001   661 SRPLPAEELEALLRARA 677
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 12-258 2.23e-80

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: 252.78  E-value: 2.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  12 EEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLFN 91
Cdd:COG2200   330 ESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPE 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  92 KLPDgFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTGYS 171
Cdd:COG2200   410 RGLD-LRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYS 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 172 GLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPMPY 251
Cdd:COG2200   489 SLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPL 568


                  ....*..
gi 2103763153 252 VALVMLL 258
Cdd:COG2200   569 EELEALL 575
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 12-248 2.80e-67

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: 208.71  E-value: 2.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  12 EEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLfn 91
Cdd:pfam00563   1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  92 KLPDGFHIGLNISASHINSPTFIDDCLHF-QRGFEGKAvKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTGY 170
Cdd:pfam00563  79 QLGPDIKLSINLSPASLADPGFLELLRALlKQAGPPPS-RLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2103763153 171 SGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKP 248
Cdd:pfam00563 158 SSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
11-255 1.53e-61

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 202.14  E-value: 1.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  11 EEEKLRyAIAQG--YIVpyYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTR---SLMAQVTAQ 85
Cdd:PRK10551  265 GKEILT-GIKRGqfYVE--YQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQhlfELIARDAAE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  86 MRplfNKLPDGFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQeplllngAVVDKLNR------LHNCGF 159
Cdd:PRK10551  342 LQ---KVLPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITER-------DMVQEEEAtklfawLHSQGI 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 160 SIALDDFGTGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPL 239
Cdd:PRK10551  412 EIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNF 491

                         250
                  ....*....|....*.
gi 2103763153 240 LQGYFFWKPMPYVALV 255
Cdd:PRK10551  492 LQGYWISRPLPLEDFV 507
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 15-250 1.82e-45

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 162.63  E-value: 1.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  15 LRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQM---RPLFN 91
Cdd:PRK11359  548 LKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLaewRSQNI 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  92 KLPDgfhIGLNISASHINS---PTFIDDCLHfQRGFEGKavKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGT 168
Cdd:PRK11359  628 HIPA---LSVNLSALHFRSnqlPNQVSDAMQ-AWGIDGH--QLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGT 701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 169 GYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKP 248
Cdd:PRK11359  702 GFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781


                  ..
gi 2103763153 249 MP 250
Cdd:PRK11359  782 LP 783
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
15-267 5.23e-43

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 154.84  E-value: 5.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  15 LRYAIAQGYIVPYYQPLVNGkTGEIYGVEILARWQnttTPSR---SPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLFN 91
Cdd:PRK10060  413 LRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQ---SPERgliPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRD 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  92 KlPDGFHIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALDDFGTGYS 171
Cdd:PRK10060  489 K-GINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYS 567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 172 GLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPMPY 251
Cdd:PRK10060  568 SLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPA 647

                         250
                  ....*....|....*.
gi 2103763153 252 VALVMLLLSKPKARII 267
Cdd:PRK10060  648 VAFERWYKRYLKRKLI 663
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 10-250 5.15e-37

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 138.31  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  10 SEEEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQVTAQ---- 85
Cdd:PRK13561  400 TEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLlaaw 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  86 -----MRPLfnklpdgfhiGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFS 160
Cdd:PRK13561  480 qergiMLPL----------SVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVR 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 161 IALDDFGTGYSGLSYLHE---LVFDYIKIDQSFVgrvTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNI 237
Cdd:PRK13561  550 VALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFV---DGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGV 626

                         250
                  ....*....|...
gi 2103763153 238 PLLQGYFFWKPMP 250
Cdd:PRK13561  627 GIAQGFLFARALP 639
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 10-250 9.82e-37

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 137.38  E-value: 9.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  10 SEEEKLRYAIAQGYIVPYYQPLVNGKTGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRSLMAQ-----VTA 84
Cdd:PRK11829  405 TQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEacrilADW 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  85 QMRPLfnKLPdgfhIGLNISASHINSPTFIDDCLHFQRGFEGKAVKLMLEITEQEPLLLNGAVVDKLNRLHNCGFSIALD 164
Cdd:PRK11829  485 KARGV--SLP----LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALD 558

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 165 DFGTGYSGLSYLH---ELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMartLSLRIIAEGVETQAQLDYLNRQNIPLLQ 241
Cdd:PRK11829  559 DFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDV---LKVRVMAEGVETEEQRQWLLEHGIQCGQ 635


                  ....*....
gi 2103763153 242 GYFFWKPMP 250
Cdd:PRK11829  636 GFLFSPPLP 644
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 57-255 1.28e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 88.19  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153   57 SPAEFIPLAERTGLIIPLTRSLMAQVTAQMRPLFNKlpDGFHIGLNISASHINSPTFIDDcLHFQrgFEGKAV---KLML 133
Cdd:PRK09776   888 DEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS--KGLSIALPLSVAGLSSPTLLPF-LLEQ--LENSPLpprLLHL 962

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  134 EITEqEPLLLNGAVVDK-LNRLHNCGFSIALDDFGTGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMAR 212
Cdd:PRK09776   963 EITE-TALLNHAESASRlVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQ 1041

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2103763153  213 TLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPMPYVALV 255
Cdd:PRK09776  1042 RLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLL 1084
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 130-269 3.70e-14

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 71.37  E-value: 3.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 130 KLMLEITEQEPLllNGAVVDKLNRLHNCGFSIALDDFgtgySGLSYLHELV--FDYIKIDqsfVGRVTGETpssklLDCV 207
Cdd:COG3434    85 RVVLEILEDVEP--DEELLEALKELKEKGYRIALDDF----VLDPEWDPLLplADIIKID---VLALDLEE-----LAEL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2103763153 208 IEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYFFWKPMP---------YVALVMLL--LSKPKARI--IEE 269
Cdd:COG3434   151 VARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEIlkgkklppsQLTLLQLLneLNKPDADLdeIEE 225
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 163-251 1.15e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 57.32  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 163 LDDFGTGYSGLSYLHELVFDYIKID--------QSFVGRvtgetpssKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNR 234
Cdd:PRK11596  157 LDDFGTGMANFSALSEVRYDYIKVArelfimlrQSEEGR--------NLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQR 228

                          90
                  ....*....|....*..
gi 2103763153 235 QNIPLLQGYFFWKPMPY 251
Cdd:PRK11596  229 SPAFAAQGYFLSRPAPF 245
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 15-252 1.78e-06

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 48.71  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  15 LRYAIAQGYIVPYYQPLVNGKtGEIYGVEILARWQNTTTPSRSPAEFIPLAERTGLIIPLTRslmaQVTAQMRPLFNKLP 94
Cdd:PRK11059  408 LEQTLVRGGPRLYQQPAVTRD-GKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDR----QVIERVLPLLRYWP 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153  95 DGfHIGLNISASHINSPTFI----DDCLHFQRGfegKAVKLMLEITE------QEPLllnGAVVDKLNRLhncGFSIALD 164
Cdd:PRK11059  483 EE-NLSINLSVDSLLSRAFQrwlrDTLLQCPRS---QRKRLIFELAEadvcqhISRL---RPVLRMLRGL---GCRLAVD 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103763153 165 DFGTGYSGLSYLHELVFDYIKIDQSFVGRVTGETPSSKLLDCVIEMARTLSLRIIAEGVETQAQLDYLNRQNIPLLQGYF 244
Cdd:PRK11059  553 QAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDF 632


                  ....*...
gi 2103763153 245 FWKPMPYV 252
Cdd:PRK11059  633 FAESQPLD 640
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH