NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|823297162|ref|WP_047052696|]
View 

MULTISPECIES: EAL and HDOD domain-containing protein [Enterobacteriaceae]

Protein Classification

EAL and HDOD domain-containing protein( domain architecture ID 11465797)

EAL and HDOD (HD-related output domain) domain-containing protein may act as a cyclic diguanylate phosphodiesterase; similar to Bacillus subtilis protein YuxH and Vibrio cholerae cyclic di-GMP phosphodiesterase CdgJ

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
1-406 4.00e-174

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


:

Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 492.01  E-value: 4.00e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   1 MYSFIARQPIFDSKMQTVAYELLFRDGMNNAFPDVSPEYATSKMISDQFLCIPIHRIAGKHSSFINVPHQMIISGLVDTL 80
Cdd:COG3434    2 MDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPELL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  81 PGEKVVIEILEDAVPDDALFSAVKSMHEKGYQLALDDFTLDSAWNRFMPYISVIKFDVREKHQNEIFQYIKDNKPllKGI 160
Cdd:COG3434   82 PPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKR--YGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 161 QFLAEKVETREEYDRYCQAGFSLFQGFFFSRPEIMKNKCLSQNPLTLSRLMMEVHRESPDFATLERLFKSDLTLSYKIMR 240
Cdd:COG3434  160 KLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKLLR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 241 YVRNILFKThginQSDNLTLKQMLMFLGCNELRRFVSVAALASMSTSGVS-ELYHQSIVRGKFCELICGKIDKTSLSYNA 319
Cdd:COG3434  240 YVNSAAFGL----RRKITSIRQAIVLLGLRQLRRWLSLLLLASLSDSGKPpELLETALVRARFCELLAEKLGPKEEADEA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 320 FICGLFSLLDVILELPMADLIKQITIPENVTDALCEQKGELFTILNLSLCYEKLDWNGTTEICHALNLPEFSVIEAMQTA 399
Cdd:COG3434  316 FLVGLFSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEA 395

                 ....*..
gi 823297162 400 TKWADEL 406
Cdd:COG3434  396 LAWADEL 402
 
Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
1-406 4.00e-174

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 492.01  E-value: 4.00e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   1 MYSFIARQPIFDSKMQTVAYELLFRDGMNNAFPDVSPEYATSKMISDQFLCIPIHRIAGKHSSFINVPHQMIISGLVDTL 80
Cdd:COG3434    2 MDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPELL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  81 PGEKVVIEILEDAVPDDALFSAVKSMHEKGYQLALDDFTLDSAWNRFMPYISVIKFDVREKHQNEIFQYIKDNKPllKGI 160
Cdd:COG3434   82 PPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKR--YGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 161 QFLAEKVETREEYDRYCQAGFSLFQGFFFSRPEIMKNKCLSQNPLTLSRLMMEVHRESPDFATLERLFKSDLTLSYKIMR 240
Cdd:COG3434  160 KLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKLLR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 241 YVRNILFKThginQSDNLTLKQMLMFLGCNELRRFVSVAALASMSTSGVS-ELYHQSIVRGKFCELICGKIDKTSLSYNA 319
Cdd:COG3434  240 YVNSAAFGL----RRKITSIRQAIVLLGLRQLRRWLSLLLLASLSDSGKPpELLETALVRARFCELLAEKLGPKEEADEA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 320 FICGLFSLLDVILELPMADLIKQITIPENVTDALCEQKGELFTILNLSLCYEKLDWNGTTEICHALNLPEFSVIEAMQTA 399
Cdd:COG3434  316 FLVGLFSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEA 395

                 ....*..
gi 823297162 400 TKWADEL 406
Cdd:COG3434  396 LAWADEL 402
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
8-192 1.26e-14

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: 72.96  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   8 QPIFDSK-MQTVAYELLFR-----DGMnnafpdVSP--------EYATSKMISDQFL---CIPIHRIAGKHSS---FINV 67
Cdd:cd01948   17 QPIVDLRtGRIVGYEALLRwrhpeGGL------ISPaefiplaeETGLIVELGRWVLeeaCRQLARWQAGGPDlrlSVNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  68 -PHQMIISGLVDT---------LPGEKVVIEILEDAVPDD--ALFSAVKSMHEKGYQLALDDF-----TLdSAWNRFmpY 130
Cdd:cd01948   91 sARQLRDPDFLDRllellaetgLPPRRLVLEITESALIDDleEALATLRRLRALGVRIALDDFgtgysSL-SYLKRL--P 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823297162 131 ISVIKFD---VREKHQNEifqyikDNKPLLKGIQFL---------AEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:cd01948  168 VDYLKIDrsfVRDIETDP------EDRAIVRAIIALahslglkvvAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
8-192 1.94e-12

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: 66.57  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162    8 QPIFDSKM-QTVAYELLFRdgMNNAFPDVSPEYATSKMISDQFLCIPIHR--------------IAGKHSSFINVPHQMI 72
Cdd:pfam00563  18 QPIVDLRTgRVVGYEALLR--WQHPDGGLISPARFLPLAEELGLIAELDRwvleqaladlaqlqLGPDIKLSINLSPASL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   73 -ISGLVDTL---------PGEKVVIEILEDAVP--DDALFSAVKSMHEKGYQLALDDFTLD----SAWNRFMPyiSVIKF 136
Cdd:pfam00563  96 aDPGFLELLrallkqagpPPSRLVLEITESDLLarLEALREVLKRLRALGIRIALDDFGTGysslSYLLRLPP--DFVKI 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823297162  137 D---VREKHQN----EIFQYIKDnkpLLK--GIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:pfam00563 174 DrslIADIDKDgearAIVRALIA---LAHslGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
80-192 7.79e-12

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 64.93  E-value: 7.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162    80 LPGEKVVIEILEDAV--PDDALFSAVKSMHEKGYQLALDDFTLD----SAWNRFMpyISVIKFD---VREKHQNE----I 146
Cdd:smart00052 115 LPPQRLELEITESVLldDDESAVATLQRLRELGVRIALDDFGTGysslSYLKRLP--VDLLKIDksfVRDLQTDPedeaI 192
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 823297162   147 FQYIKDnkpLLK--GIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:smart00052 193 VQSIIE---LAQklGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
73-192 2.92e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 46.30  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  73 ISGLVD--TLPGEKVVIEILEDAV--PDDALFSAVKSMHEKGYQLALDDF-TLDSAWNRF--MPyISVIKFD-------V 138
Cdd:PRK11359 650 VSDAMQawGIDGHQLTVEITESMMmeHDTEIFKRIQILRDMGVGLSVDDFgTGFSGLSRLvsLP-VTEIKIDksfvdrcL 728
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 823297162 139 REKHQNEIFQYIKDNKPLLKgIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:PRK11359 729 TEKRILALLEAITSIGQSLN-LTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
 
Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
1-406 4.00e-174

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 492.01  E-value: 4.00e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   1 MYSFIARQPIFDSKMQTVAYELLFRDGMNNAFPDVSPEYATSKMISDQFLCIPIHRIAGKHSSFINVPHQMIISGLVDTL 80
Cdd:COG3434    2 MDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPELL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  81 PGEKVVIEILEDAVPDDALFSAVKSMHEKGYQLALDDFTLDSAWNRFMPYISVIKFDVREKHQNEIFQYIKDNKPllKGI 160
Cdd:COG3434   82 PPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKR--YGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 161 QFLAEKVETREEYDRYCQAGFSLFQGFFFSRPEIMKNKCLSQNPLTLSRLMMEVHRESPDFATLERLFKSDLTLSYKIMR 240
Cdd:COG3434  160 KLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKLLR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 241 YVRNILFKThginQSDNLTLKQMLMFLGCNELRRFVSVAALASMSTSGVS-ELYHQSIVRGKFCELICGKIDKTSLSYNA 319
Cdd:COG3434  240 YVNSAAFGL----RRKITSIRQAIVLLGLRQLRRWLSLLLLASLSDSGKPpELLETALVRARFCELLAEKLGPKEEADEA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 320 FICGLFSLLDVILELPMADLIKQITIPENVTDALCEQKGELFTILNLSLCYEKLDWNGTTEICHALNLPEFSVIEAMQTA 399
Cdd:COG3434  316 FLVGLFSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEA 395

                 ....*..
gi 823297162 400 TKWADEL 406
Cdd:COG3434  396 LAWADEL 402
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
64-192 3.41e-15

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: 77.52  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  64 FINV-PHQMIISGLVDTL---------PGEKVVIEILEDAVPDD--ALFSAVKSMHEKGYQLALDDF-TLDSAWNRFMPY 130
Cdd:COG2200  417 SVNLsARSLLDPDFLERLlellaeyglPPERLVLEITESALLEDleAAIELLARLRALGVRIALDDFgTGYSSLSYLKRL 496
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823297162 131 -ISVIKFD---VREKHQNE----IFQYIKDnkpLLK--GIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:COG2200  497 pPDYLKIDrsfVRDIARDPrdqaIVRAIVA---LAHrlGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
8-192 1.26e-14

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: 72.96  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   8 QPIFDSK-MQTVAYELLFR-----DGMnnafpdVSP--------EYATSKMISDQFL---CIPIHRIAGKHSS---FINV 67
Cdd:cd01948   17 QPIVDLRtGRIVGYEALLRwrhpeGGL------ISPaefiplaeETGLIVELGRWVLeeaCRQLARWQAGGPDlrlSVNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  68 -PHQMIISGLVDT---------LPGEKVVIEILEDAVPDD--ALFSAVKSMHEKGYQLALDDF-----TLdSAWNRFmpY 130
Cdd:cd01948   91 sARQLRDPDFLDRllellaetgLPPRRLVLEITESALIDDleEALATLRRLRALGVRIALDDFgtgysSL-SYLKRL--P 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823297162 131 ISVIKFD---VREKHQNEifqyikDNKPLLKGIQFL---------AEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:cd01948  168 VDYLKIDrsfVRDIETDP------EDRAIVRAIIALahslglkvvAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
8-192 1.94e-12

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: 66.57  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162    8 QPIFDSKM-QTVAYELLFRdgMNNAFPDVSPEYATSKMISDQFLCIPIHR--------------IAGKHSSFINVPHQMI 72
Cdd:pfam00563  18 QPIVDLRTgRVVGYEALLR--WQHPDGGLISPARFLPLAEELGLIAELDRwvleqaladlaqlqLGPDIKLSINLSPASL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   73 -ISGLVDTL---------PGEKVVIEILEDAVP--DDALFSAVKSMHEKGYQLALDDFTLD----SAWNRFMPyiSVIKF 136
Cdd:pfam00563  96 aDPGFLELLrallkqagpPPSRLVLEITESDLLarLEALREVLKRLRALGIRIALDDFGTGysslSYLLRLPP--DFVKI 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823297162  137 D---VREKHQN----EIFQYIKDnkpLLK--GIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:pfam00563 174 DrslIADIDKDgearAIVRALIA---LAHslGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
80-192 7.79e-12

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 64.93  E-value: 7.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162    80 LPGEKVVIEILEDAV--PDDALFSAVKSMHEKGYQLALDDFTLD----SAWNRFMpyISVIKFD---VREKHQNE----I 146
Cdd:smart00052 115 LPPQRLELEITESVLldDDESAVATLQRLRELGVRIALDDFGTGysslSYLKRLP--VDLLKIDksfVRDLQTDPedeaI 192
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 823297162   147 FQYIKDnkpLLK--GIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:smart00052 193 VQSIIE---LAQklGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
65-192 3.87e-09

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: 58.63  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  65 INV-PHQMIISGLVDT---------LPGEKVVIEILEDAV---PDDALfSAVKSMHEKGYQLALDDF--------TLdsa 123
Cdd:COG5001  516 VNLsARQLRDPDLVDRvrralaetgLPPSRLELEITESALledPEEAL-ETLRALRALGVRIALDDFgtgysslsYL--- 591
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162 124 wnRFMPyISVIKFD---VREKHQNEifqyikDNKPLLK---------GIQFLAEKVETREEYDRYCQAGFSLFQGFFFSR 191
Cdd:COG5001  592 --KRLP-VDTLKIDrsfVRDLAEDP------DDAAIVRaiialahslGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSR 662

                 .
gi 823297162 192 P 192
Cdd:COG5001  663 P 663
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
73-192 2.92e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 46.30  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  73 ISGLVD--TLPGEKVVIEILEDAV--PDDALFSAVKSMHEKGYQLALDDF-TLDSAWNRF--MPyISVIKFD-------V 138
Cdd:PRK11359 650 VSDAMQawGIDGHQLTVEITESMMmeHDTEIFKRIQILRDMGVGLSVDDFgTGFSGLSRLvsLP-VTEIKIDksfvdrcL 728
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 823297162 139 REKHQNEIFQYIKDNKPLLKgIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:PRK11359 729 TEKRILALLEAITSIGQSLN-LTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
81-192 9.75e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 41.24  E-value: 9.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  81 PGeKVVIEILEDAVPDD--ALFSAVKSMHEKGYQLALDDFTLDSA----WNRF--MPyISVIKFDvrekhqNEIFQYIKD 152
Cdd:PRK13561 517 PG-TLILEVTESRRIDDphAAVAILRPLRNAGVRVALDDFGMGYAglrqLQHMksLP-IDVLKID------KMFVDGLPE 588
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 823297162 153 NKPLLKGI---------QFLAEKVETREEYDRYCQAGFSLFQGFFFSRP 192
Cdd:PRK13561 589 DDSMVAAIimlaqslnlQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
80-193 2.18e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 40.43  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162   80 LPGEKVVIEILEDAV--PDDALFSAVKSMHEKGYQLALDDFTLD-SAWNRFMPY-ISVIKFD---VREKHQN----EIFQ 148
Cdd:PRK09776  955 LPPRLLHLEITETALlnHAESASRLVQKLRLAGCRVVLSDFGRGlSSFNYLKAFmADYLKLDgelVANLHGNlmdeMLIS 1034
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 823297162  149 YIKDNKPLLkGIQFLAEKVETREEYDRYCQAGFSLFQGFFFSRPE 193
Cdd:PRK09776 1035 IIQGHAQRL-GMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
83-204 4.78e-03

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 39.15  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823297162  83 EKVVIEILEDAVPDDALFSA--VKSMHEKGYQLALDDFTLDSAWNRFMPYISVIKFDVREKHQNEIFQYIKDN------- 153
Cdd:PRK11829 523 QQLLLEITETAQIQDLDEALrlLRELQGLGLLIALDDFGIGYSSLRYLNHLKSLPIHMIKLDKSFVKNLPEDDaiariis 602
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 823297162 154 --KPLLKgIQFLAEKVETREEYDRYCQAGFSLFQGFFFSrPEIMKNKCLSQNP 204
Cdd:PRK11829 603 cvSDVLK-VRVMAEGVETEEQRQWLLEHGIQCGQGFLFS-PPLPRAEFEAQYF 653
 
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