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Conserved domains on  [gi|658758354|ref|WP_029774480|]
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MULTISPECIES: EAL and HDOD domain-containing protein [Pseudoalteromonas]

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

CATH:  1.10.3210.10|3.20.20.450
PubMed:  20691189|28186120|15306016

Graphical summary

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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 ...
 1-399 2.65e-172

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


:

Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 487.39  E-value: 2.65e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   1 MSVFVARQAIFNRKQNVVAYELLFRNSAENFFPDIEEGQATARLIMENQLNLGTRHITSGKTALINIGPDSLKHNLCDFL 80
Cdd:COG3434    2 MDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPELL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  81 PCKDVVIELLETIEPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLKFIKLVKFDIAQTPLSDIAEIVEKLKQHkKIK 160
Cdd:COG3434   82 PPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKRY-GIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 161 ILAEKIETQADYHQAHKMGFDYFQGYFFAKPTMHEQQDIDYNYALVVAIYAQVMKPSPDIKQISALFEADAALAYKLMRL 240
Cdd:COG3434  161 LLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKLLRY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 241 INSGVFPIQSKISSIKQALVYLGHERLKKFVSLIVTAH-TAGKKPAELMQVCVVRARFCELIAKQV-SKSLAGEAFLTGL 318
Cdd:COG3434  241 VNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASlSDSGKPPELLETALVRARFCELLAEKLgPKEEADEAFLVGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 319 FSLLDAILDQPMSLLVEKLPFPDDIKAALLNEKNTLYYILNVVQAYETGSWWTLEKAVILLNVKSDVLPGLYNQAVDWAD 398
Cdd:COG3434  321 FSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALAWAD 400


                 .
gi 658758354 399 N 399
Cdd:COG3434  401 E 401
 
Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 1-399 2.65e-172

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 487.39  E-value: 2.65e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   1 MSVFVARQAIFNRKQNVVAYELLFRNSAENFFPDIEEGQATARLIMENQLNLGTRHITSGKTALINIGPDSLKHNLCDFL 80
Cdd:COG3434    2 MDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPELL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  81 PCKDVVIELLETIEPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLKFIKLVKFDIAQTPLSDIAEIVEKLKQHkKIK 160
Cdd:COG3434   82 PPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKRY-GIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 161 ILAEKIETQADYHQAHKMGFDYFQGYFFAKPTMHEQQDIDYNYALVVAIYAQVMKPSPDIKQISALFEADAALAYKLMRL 240
Cdd:COG3434  161 LLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKLLRY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 241 INSGVFPIQSKISSIKQALVYLGHERLKKFVSLIVTAH-TAGKKPAELMQVCVVRARFCELIAKQV-SKSLAGEAFLTGL 318
Cdd:COG3434  241 VNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASlSDSGKPPELLETALVRARFCELLAEKLgPKEEADEAFLVGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 319 FSLLDAILDQPMSLLVEKLPFPDDIKAALLNEKNTLYYILNVVQAYETGSWWTLEKAVILLNVKSDVLPGLYNQAVDWAD 398
Cdd:COG3434  321 FSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALAWAD 400


                 .
gi 658758354 399 N 399
Cdd:COG3434  401 E 401
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 8-191 1.56e-16

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: 78.13  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354    8 QAIFN-RKQNVVAYELLFR--------NSAENFFPDIEEGQATARL---IMENQLNLGTRHITSGKTAL-INIGPDSLKH 74
Cdd:pfam00563  18 QPIVDlRTGRVVGYEALLRwqhpdgglISPARFLPLAEELGLIAELdrwVLEQALADLAQLQLGPDIKLsINLSPASLAD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   75 N-LCDFL---------PCKDVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDFvyNEQWERFLKFIKL----VKFD- 137
Cdd:pfam00563  98 PgFLELLrallkqagpPPSRLVLEITESdlLARLEALREVLKRLRALGIRIALDDF--GTGYSSLSYLLRLppdfVKIDr 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758354  138 ----------IAQTPLSDIAEIVEKLKqhkkIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:pfam00563 176 sliadidkdgEARAIVRALIALAHSLG----IKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 8-191 1.69e-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: 72.58  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   8 QAIFN-RKQNVVAYELLFR--------NSAENFFPDIEEGQATARL---IMENQLNLGTRHITSGKTAL--INIGPDSLK 73
Cdd:cd01948   17 QPIVDlRTGRIVGYEALLRwrhpegglISPAEFIPLAEETGLIVELgrwVLEEACRQLARWQAGGPDLRlsVNLSARQLR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  74 H-NLCDF---------LPCKDVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDF--VYN--EQWERF-LKFIKL--- 133
Cdd:cd01948   97 DpDFLDRllellaetgLPPRRLVLEITESalIDDLEEALATLRRLRALGVRIALDDFgtGYSslSYLKRLpVDYLKIdrs 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 134 -VKfDIAQTPLS-DIAEIVEKLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:cd01948  177 fVR-DIETDPEDrAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 8-191 1.72e-08

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 54.92  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354     8 QAIFN-RKQNVVAYELLFR--------NSAENFFPDIEE-GQATA--RLIMEN--QLNLGTRHITSGKTAL-INIGPDSL 72
Cdd:smart00052  18 QPIVSlRTGRLVGVEALIRwqhpeggiISPDEFIPLAEEtGLIVPlgRWVLEQacQQLAEWQAQGPPPLLIsINLSARQL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354    73 KHNlcDF------------LPCKDVVIELLETI--EPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLK-----FIKL 133
Cdd:smart00052  98 ISP--DLvprvlelleetgLPPQRLELEITESVllDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKrlpvdLLKI 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758354   134 VK-F--DIAQTPLSD-IAEIVEKLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:smart00052 176 DKsFvrDLQTDPEDEaIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 87-203 6.65e-07

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 51.48  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  87 IELLET--IEPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLK--------FIKLVKFDIAQTPLSD-IAEIVEKLKQ 155
Cdd:PRK11829 527 LEITETaqIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkslpihMIKLDKSFVKNLPEDDaIARIISCVSD 606

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 658758354 156 HKKIKILAEKIET--QADYHQAHkmGFDYFQGYFFAKPTmhEQQDIDYNY 203
Cdd:PRK11829 607 VLKVRVMAEGVETeeQRQWLLEH--GIQCGQGFLFSPPL--PRAEFEAQY 652
 
Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 1-399 2.65e-172

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 487.39  E-value: 2.65e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   1 MSVFVARQAIFNRKQNVVAYELLFRNSAENFFPDIEEGQATARLIMENQLNLGTRHITSGKTALINIGPDSLKHNLCDFL 80
Cdd:COG3434    2 MDVFVARQPILDRDQRVVGYELLFRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPELL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  81 PCKDVVIELLETIEPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLKFIKLVKFDIAQTPLSDIAEIVEKLKQHkKIK 160
Cdd:COG3434   82 PPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKRY-GIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 161 ILAEKIETQADYHQAHKMGFDYFQGYFFAKPTMHEQQDIDYNYALVVAIYAQVMKPSPDIKQISALFEADAALAYKLMRL 240
Cdd:COG3434  161 LLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKLLRY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 241 INSGVFPIQSKISSIKQALVYLGHERLKKFVSLIVTAH-TAGKKPAELMQVCVVRARFCELIAKQV-SKSLAGEAFLTGL 318
Cdd:COG3434  241 VNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASlSDSGKPPELLETALVRARFCELLAEKLgPKEEADEAFLVGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 319 FSLLDAILDQPMSLLVEKLPFPDDIKAALLNEKNTLYYILNVVQAYETGSWWTLEKAVILLNVKSDVLPGLYNQAVDWAD 398
Cdd:COG3434  321 FSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALAWAD 400


                 .
gi 658758354 399 N 399
Cdd:COG3434  401 E 401
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 8-191 1.56e-16

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: 78.13  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354    8 QAIFN-RKQNVVAYELLFR--------NSAENFFPDIEEGQATARL---IMENQLNLGTRHITSGKTAL-INIGPDSLKH 74
Cdd:pfam00563  18 QPIVDlRTGRVVGYEALLRwqhpdgglISPARFLPLAEELGLIAELdrwVLEQALADLAQLQLGPDIKLsINLSPASLAD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   75 N-LCDFL---------PCKDVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDFvyNEQWERFLKFIKL----VKFD- 137
Cdd:pfam00563  98 PgFLELLrallkqagpPPSRLVLEITESdlLARLEALREVLKRLRALGIRIALDDF--GTGYSSLSYLLRLppdfVKIDr 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658758354  138 ----------IAQTPLSDIAEIVEKLKqhkkIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:pfam00563 176 sliadidkdgEARAIVRALIALAHSLG----IKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
208-319 7.79e-16

HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 76.54  E-value: 7.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 208 AIYAQVMK----PSPDIKQISALFEADAALAYKLMRLINSGVFPIQSKISSIKQALVYLGHERLKKFV-SLIVTAHTAGK 282
Cdd:COG1639   15 EVALRLLElladPDASLAELARLISQDPALTARLLRLANSAYYGLGRKITSVEQAVVLLGLDTVRNLAlALALRQLFSAK 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 658758354 283 KPA------ELMQVCVVRARFCELIAKQVSKSLAGEAFLTGLF 319
Cdd:COG1639   95 LPAygldlrRFWRHSLAVAAAARALARRLGLLDPEEAFLAGLL 137
HDOD pfam08668
HDOD domain;
205-318 1.24e-14

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 71.87  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  205 LVVAIYAQVMKPSPDIKQISALFEADAALAYKLMRLINSGVFPIQSKISSIKQALVYLGHERLKKFVSLIVTAHTAGKKP 284
Cdd:pfam08668   7 VALRILALLNDPDSSISDIAELISRDPALTARLLRLANSAYYGLRRPISTISQAVVLLGLRTVRNLALGISVKRIFRGTP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 658758354  285 A------ELMQVCVVRARFCELIAKQVSKSLAGEAFLTGL 318
Cdd:pfam08668  87 PlgfdlkGFWEHSLACALAARLLARRLGLDDPEEAFLAGL 126
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 8-191 1.69e-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: 72.58  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   8 QAIFN-RKQNVVAYELLFR--------NSAENFFPDIEEGQATARL---IMENQLNLGTRHITSGKTAL--INIGPDSLK 73
Cdd:cd01948   17 QPIVDlRTGRIVGYEALLRwrhpegglISPAEFIPLAEETGLIVELgrwVLEEACRQLARWQAGGPDLRlsVNLSARQLR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  74 H-NLCDF---------LPCKDVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDF--VYN--EQWERF-LKFIKL--- 133
Cdd:cd01948   97 DpDFLDRllellaetgLPPRRLVLEITESalIDDLEEALATLRRLRALGVRIALDDFgtGYSslSYLKRLpVDYLKIdrs 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 134 -VKfDIAQTPLS-DIAEIVEKLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:cd01948  177 fVR-DIETDPEDrAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 3-191 6.71e-14

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: 73.28  E-value: 6.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354   3 VFVARQAIFN-RKQNVVAYELLFR--------NSAENFFPDIEE-GQATA--RLIMENQLNLGTRHITSGKTAL--INIG 68
Cdd:COG2200  342 LRLYYQPIVDlRTGRVVGYEALLRwrhpdgglISPAEFIPAAERsGLIVEldRWVLERALRQLARWPERGLDLRlsVNLS 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  69 PDSLKH-NLCDFL---------PCKDVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDFV--YN--EQWERF-LKFI 131
Cdd:COG2200  422 ARSLLDpDFLERLlellaeyglPPERLVLEITESalLEDLEAAIELLARLRALGVRIALDDFGtgYSslSYLKRLpPDYL 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658758354 132 KL----VKfDIAQTP-----LSDIAEIVEKLKqhkkIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:COG2200  502 KIdrsfVR-DIARDPrdqaiVRAIVALAHRLG----LKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 8-191 1.72e-08

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 54.92  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354     8 QAIFN-RKQNVVAYELLFR--------NSAENFFPDIEE-GQATA--RLIMEN--QLNLGTRHITSGKTAL-INIGPDSL 72
Cdd:smart00052  18 QPIVSlRTGRLVGVEALIRwqhpeggiISPDEFIPLAEEtGLIVPlgRWVLEQacQQLAEWQAQGPPPLLIsINLSARQL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354    73 KHNlcDF------------LPCKDVVIELLETI--EPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLK-----FIKL 133
Cdd:smart00052  98 ISP--DLvprvlelleetgLPPQRLELEITESVllDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKrlpvdLLKI 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658758354   134 VK-F--DIAQTPLSD-IAEIVEKLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:smart00052 176 DKsFvrDLQTDPEDEaIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 87-203 6.65e-07

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 51.48  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  87 IELLET--IEPTDDNYQLCRELFHKNYKLALDDFVYNEQWERFLK--------FIKLVKFDIAQTPLSD-IAEIVEKLKQ 155
Cdd:PRK11829 527 LEITETaqIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkslpihMIKLDKSFVKNLPEDDaIARIISCVSD 606

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 658758354 156 HKKIKILAEKIET--QADYHQAHkmGFDYFQGYFFAKPTmhEQQDIDYNY 203
Cdd:PRK11829 607 VLKVRVMAEGVETeeQRQWLLEH--GIQCGQGFLFSPPL--PRAEFEAQY 652
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 65-191 2.11e-05

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: 46.69  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  65 INIGPDSLKH-NLCDF---------LPCKDVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDF-------------- 118
Cdd:COG5001  516 VNLSARQLRDpDLVDRvrralaetgLPPSRLELEITESalLEDPEEALETLRALRALGVRIALDDFgtgysslsylkrlp 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354 119 VyneqweRFLK----FIKlvkfDIAQTPlsDIAEIVE---KLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:COG5001  596 V------DTLKidrsFVR----DLAEDP--DDAAIVRaiiALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRP 663
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
65-191 2.91e-04

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 43.06  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  65 INIGPDSLkHNlCDFlpCKDVViELLETIePTDD-------------NYQLCRELFH----KNYKLALDDF-------VY 120
Cdd:PRK10551 354 INISPAHL-HS-DSF--KADVQ-RLLASL-PADHfqivleiterdmvQEEEATKLFAwlhsQGIEIAIDDFgtghsalIY 427

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658758354 121 NEQWE-RFLK----FIKLVKFDIAQTPLSDIaeiVEKLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:PRK10551 428 LERFTlDYLKidrgFIQAIGTETVTSPVLDA---VLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
77-191 5.63e-04

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 41.98  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  77 CDFLPCKdVVIELLET--IEPTDDNYQLCRELFHKNYKLALDDFV--YNE--QWERF-LKFIKLVK-F--DIAQTPLSD- 145
Cdd:PRK10060 520 LNFEYCP-IDVELTESclIENEELALSVIQQFSQLGAQVHLDDFGtgYSSlsQLARFpIDAIKLDQsFvrDIHKQPVSQs 598

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 658758354 146 -IAEIVeKLKQHKKIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:PRK10060 599 lVRAIV-AVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 63-191 3.14e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 39.70  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658758354  63 ALIN---IGPDSLkhnlcdflpckdvVIELLET--IEPTDDNYQLCRELFHKNYKLALDDF---VYNEQWERFLKF--IK 132
Cdd:PRK13561 508 ELLTryrIQPGTL-------------ILEVTESrrIDDPHAAVAILRPLRNAGVRVALDDFgmgYAGLRQLQHMKSlpID 574

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658758354 133 LVKFD---IAQTPLSD-----IAEIVEKLKqhkkIKILAEKIETQADYHQAHKMGFDYFQGYFFAKP 191
Cdd:PRK13561 575 VLKIDkmfVDGLPEDDsmvaaIIMLAQSLN----LQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
 
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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