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Conserved domains on  [gi|491536207|ref|WP_005393827|]
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MULTISPECIES: EAL and HDOD domain-containing protein [Vibrio]

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 ...
 1-407 9.26e-178

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


:

Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 501.25  E-value: 9.26e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   1 MNTTYVARQPIFNRKRQTLGYELLFRDGESNAYPShIESNRATYRLIVENFLSLGTNPVIASSRCFINFPHQSLVRRLPR 80
Cdd:COG3434    1 MMDVFVARQPILDRDQRVVGYELLFRSGLENSAPD-VDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  81 SLPKNKIVVEVLETCQPTDDLLDAIRELYREGYLIALDDFTLTPEWRRFLPYVHIVKLDIMAMGLEKACALVKAHLAKRV 160
Cdd:COG3434   80 LLPPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKRYGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 161 KyhFLAERVETAEEFEQAKAAGFKFFQGYFFSKPLVSQTKYVSPEQVLALQLFREVCSPEPDFTRIETIITQDVALSYKL 240
Cdd:COG3434  160 K--LLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 241 LRFVNTQAPNLAVEISSFRQALIYLGQDNLKQFVSLVVASYIS-SNKPRELYHLSLQRAQFCQLMSRYQPFSHLNEQGFM 319
Cdd:COG3434  238 LRYVNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASLSdSGKPPELLETALVRARFCELLAEKLGPKEEADEAFL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 320 VGLLSILDAMLDLSVESLVKQLPLSESVQQALLHRKGVYGALISLEECYERADWSGVEKITTQLGLSLEEVKLSLGEAVR 399
Cdd:COG3434  318 VGLFSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALA 397


                 ....*...
gi 491536207 400 WSQNVATA 407
Cdd:COG3434  398 WADELLSA 405
 
Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 1-407 9.26e-178

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 501.25  E-value: 9.26e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   1 MNTTYVARQPIFNRKRQTLGYELLFRDGESNAYPShIESNRATYRLIVENFLSLGTNPVIASSRCFINFPHQSLVRRLPR 80
Cdd:COG3434    1 MMDVFVARQPILDRDQRVVGYELLFRSGLENSAPD-VDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  81 SLPKNKIVVEVLETCQPTDDLLDAIRELYREGYLIALDDFTLTPEWRRFLPYVHIVKLDIMAMGLEKACALVKAHLAKRV 160
Cdd:COG3434   80 LLPPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKRYGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 161 KyhFLAERVETAEEFEQAKAAGFKFFQGYFFSKPLVSQTKYVSPEQVLALQLFREVCSPEPDFTRIETIITQDVALSYKL 240
Cdd:COG3434  160 K--LLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 241 LRFVNTQAPNLAVEISSFRQALIYLGQDNLKQFVSLVVASYIS-SNKPRELYHLSLQRAQFCQLMSRYQPFSHLNEQGFM 319
Cdd:COG3434  238 LRYVNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASLSdSGKPPELLETALVRARFCELLAEKLGPKEEADEAFL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 320 VGLLSILDAMLDLSVESLVKQLPLSESVQQALLHRKGVYGALISLEECYERADWSGVEKITTQLGLSLEEVKLSLGEAVR 399
Cdd:COG3434  318 VGLFSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALA 397


                 ....*...
gi 491536207 400 WSQNVATA 407
Cdd:COG3434  398 WADELLSA 405
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 9-194 1.44e-19

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: 86.99  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207    9 QPIFN-RKRQTLGYELLFR----DGES---NAYPSHIESNRATYRL---IVENFLS-LGTNPVIASSRCFINFPHQSL-- 74
Cdd:pfam00563  18 QPIVDlRTGRVVGYEALLRwqhpDGGLispARFLPLAEELGLIAELdrwVLEQALAdLAQLQLGPDIKLSINLSPASLad 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   75 ------VRRLPRS--LPKNKIVVEVLETCQPTD--DLLDAIRELYREGYLIALDDFTL----TPEWRRFlpYVHIVKLD- 139
Cdd:pfam00563  98 pgflelLRALLKQagPPPSRLVLEITESDLLARleALREVLKRLRALGIRIALDDFGTgyssLSYLLRL--PPDFVKIDr 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  140 --IMAMGL-EKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKP 194
Cdd:pfam00563 176 slIADIDKdGEARAIVRAliALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 9-195 7.44e-16

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: 76.43  E-value: 7.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   9 QPIFN-RKRQTLGYELLFR---DGESNAYPSHIESNRATYRLIVEnflsLGT-------------NPVIASSRCFIN--- 68
Cdd:cd01948   17 QPIVDlRTGRIVGYEALLRwrhPEGGLISPAEFIPLAEETGLIVE----LGRwvleeacrqlarwQAGGPDLRLSVNlsa 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  69 --FPHQSLVRRLPRSL-----PKNKIVVEVLETC--QPTDDLLDAIRELYREGYLIALDDF-----TLTpEWRRFlpYVH 134
Cdd:cd01948   93 rqLRDPDFLDRLLELLaetglPPRRLVLEITESAliDDLEEALATLRRLRALGVRIALDDFgtgysSLS-YLKRL--PVD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491536207 135 IVKLD---IMAMGL-EKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:cd01948  170 YLKIDrsfVRDIETdPEDRAIVRAiiALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 62-195 2.59e-11

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 63.39  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207    62 SSRCFINFPHQSLVRRL--PRSLPKNKIVVEVLETC--QPTDDLLDAIRELYREGYLIALDDF-----TLTpeWRRFLPy 132
Cdd:smart00052  93 SARQLISPDLVPRVLELleETGLPPQRLELEITESVllDDDESAVATLQRLRELGVRIALDDFgtgysSLS--YLKRLP- 169

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491536207   133 VHIVKLD----IMAMGLEKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:smart00052 170 VDLLKIDksfvRDLQTDPEDEAIVQSiiELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 86-195 4.52e-10

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 61.50  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  86 KIVVEVLETCQPTD--DLLDAIRELYREGYLIALDDFTLTPEWRRFLPY-----VHIVKLD---IMAMGLEKACALVKAH 155
Cdd:PRK11829 524 QLLLEITETAQIQDldEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHlkslpIHMIKLDksfVKNLPEDDAIARIISC 603

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491536207 156 LAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:PRK11829 604 VSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPL 643
 
Name Accession Description Interval E-value
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 1-407 9.26e-178

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 501.25  E-value: 9.26e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   1 MNTTYVARQPIFNRKRQTLGYELLFRDGESNAYPShIESNRATYRLIVENFLSLGTNPVIASSRCFINFPHQSLVRRLPR 80
Cdd:COG3434    1 MMDVFVARQPILDRDQRVVGYELLFRSGLENSAPD-VDGDQATARVLLNAFLEIGLDRLLGGKLAFINFTEELLLSDLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  81 SLPKNKIVVEVLETCQPTDDLLDAIRELYREGYLIALDDFTLTPEWRRFLPYVHIVKLDIMAMGLEKACALVKAHLAKRV 160
Cdd:COG3434   80 LLPPERVVLEILEDVEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADIIKIDVLALDLEELAELVARLKRYGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 161 KyhFLAERVETAEEFEQAKAAGFKFFQGYFFSKPLVSQTKYVSPEQVLALQLFREVCSPEPDFTRIETIITQDVALSYKL 240
Cdd:COG3434  160 K--LLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQLTLLQLLNELNKPDADLDEIEEIIKRDPALSYKL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 241 LRFVNTQAPNLAVEISSFRQALIYLGQDNLKQFVSLVVASYIS-SNKPRELYHLSLQRAQFCQLMSRYQPFSHLNEQGFM 319
Cdd:COG3434  238 LRYVNSAAFGLRRKITSIRQAIVLLGLRQLRRWLSLLLLASLSdSGKPPELLETALVRARFCELLAEKLGPKEEADEAFL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 320 VGLLSILDAMLDLSVESLVKQLPLSESVQQALLHRKGVYGALISLEECYERADWSGVEKITTQLGLSLEEVKLSLGEAVR 399
Cdd:COG3434  318 VGLFSLLDALLDQPMEELLEQLPLSDEIKDALLGREGPLGPLLALAEAYERGDWEAVERLAEELGLSPEQVNEAYLEALA 397


                 ....*...
gi 491536207 400 WSQNVATA 407
Cdd:COG3434  398 WADELLSA 405
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 9-194 1.44e-19

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: 86.99  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207    9 QPIFN-RKRQTLGYELLFR----DGES---NAYPSHIESNRATYRL---IVENFLS-LGTNPVIASSRCFINFPHQSL-- 74
Cdd:pfam00563  18 QPIVDlRTGRVVGYEALLRwqhpDGGLispARFLPLAEELGLIAELdrwVLEQALAdLAQLQLGPDIKLSINLSPASLad 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   75 ------VRRLPRS--LPKNKIVVEVLETCQPTD--DLLDAIRELYREGYLIALDDFTL----TPEWRRFlpYVHIVKLD- 139
Cdd:pfam00563  98 pgflelLRALLKQagPPPSRLVLEITESDLLARleALREVLKRLRALGIRIALDDFGTgyssLSYLLRL--PPDFVKIDr 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  140 --IMAMGL-EKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKP 194
Cdd:pfam00563 176 slIADIDKdGEARAIVRAliALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 64-195 6.30e-16

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: 79.44  E-value: 6.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  64 RCFINFPHQSL--------VRRLPR--SLPKNKIVVEVLET--CQPTDDLLDAIRELYREGYLIALDDFTL---TPEWRR 128
Cdd:COG2200  415 RLSVNLSARSLldpdflerLLELLAeyGLPPERLVLEITESalLEDLEAAIELLARLRALGVRIALDDFGTgysSLSYLK 494

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491536207 129 FLPyVHIVKLD---IMAMGL-EKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:COG2200  495 RLP-PDYLKIDrsfVRDIARdPRDQAIVRAivALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPL 566
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 9-195 7.44e-16

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: 76.43  E-value: 7.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207   9 QPIFN-RKRQTLGYELLFR---DGESNAYPSHIESNRATYRLIVEnflsLGT-------------NPVIASSRCFIN--- 68
Cdd:cd01948   17 QPIVDlRTGRIVGYEALLRwrhPEGGLISPAEFIPLAEETGLIVE----LGRwvleeacrqlarwQAGGPDLRLSVNlsa 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  69 --FPHQSLVRRLPRSL-----PKNKIVVEVLETC--QPTDDLLDAIRELYREGYLIALDDF-----TLTpEWRRFlpYVH 134
Cdd:cd01948   93 rqLRDPDFLDRLLELLaetglPPRRLVLEITESAliDDLEEALATLRRLRALGVRIALDDFgtgysSLS-YLKRL--PVD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491536207 135 IVKLD---IMAMGL-EKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:cd01948  170 YLKIDrsfVRDIETdPEDRAIVRAiiALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
209-323 1.17e-13

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


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 69.99  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207 209 ALQLFREVCSPEPDFTRIETIITQDVALSYKLLRFVNTQAPNLAVEISSFRQALIYLGQDNLKQFV-SLVVASYISSNKP 287
Cdd:COG1639   17 ALRLLELLADPDASLAELARLISQDPALTARLLRLANSAYYGLGRKITSVEQAVVLLGLDTVRNLAlALALRQLFSAKLP 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491536207 288 ------RELYHLSLQRAQFCQLMSRYQPFSHLnEQGFMVGLL 323
Cdd:COG1639   97 aygldlRRFWRHSLAVAAAARALARRLGLLDP-EEAFLAGLL 137
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 62-195 2.59e-11

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 63.39  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207    62 SSRCFINFPHQSLVRRL--PRSLPKNKIVVEVLETC--QPTDDLLDAIRELYREGYLIALDDF-----TLTpeWRRFLPy 132
Cdd:smart00052  93 SARQLISPDLVPRVLELleETGLPPQRLELEITESVllDDDESAVATLQRLRELGVRIALDDFgtgysSLS--YLKRLP- 169

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491536207   133 VHIVKLD----IMAMGLEKACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:smart00052 170 VDLLKIDksfvRDLQTDPEDEAIVQSiiELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 74-195 1.07e-10

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: 63.40  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  74 LVRRLPRS-LPKNKIVVEVLETCQ-PTDDLLDAIRELYREGYLIALDDF-----------TLTpewrrflpyVHIVKLD- 139
Cdd:COG4943  377 LERLLARTgVAPQQIVLEITERGFiDPAKARAVIAALREAGHRIAIDDFgtgysslsylqTLP---------VDILKIDk 447

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491536207 140 --IMAMGLEKACALVKAH---LAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:COG4943  448 sfVDAIGTDSANSAVVPHiieMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPL 508
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 82-210 1.16e-10

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: 63.25  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  82 LPKNKIVVEVLETC--QPTDDLLDAIRELYREGYLIALDDF--------TLtpewRRFlPyVHIVKLD---IMAMGL-EK 147
Cdd:COG5001  541 LPPSRLELEITESAllEDPEEALETLRALRALGVRIALDDFgtgysslsYL----KRL-P-VDTLKIDrsfVRDLAEdPD 614

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491536207 148 ACALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPLvsqtkyvSPEQVLAL 210
Cdd:COG5001  615 DAAIVRAiiALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPL-------PAEELEAL 672
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 86-195 4.52e-10

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 61.50  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  86 KIVVEVLETCQPTD--DLLDAIRELYREGYLIALDDFTLTPEWRRFLPY-----VHIVKLD---IMAMGLEKACALVKAH 155
Cdd:PRK11829 524 QLLLEITETAQIQDldEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHlkslpIHMIKLDksfVKNLPEDDAIARIISC 603

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491536207 156 LAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:PRK11829 604 VSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPL 643
HDOD pfam08668
HDOD domain;
208-323 1.95e-09

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 56.85  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  208 LALQLFREVCSPEPDFTRIETIITQDVALSYKLLRFVNTQAPNLAVEISSFRQALIYLGQDNLKQFVSlvVASYISSNKP 287
Cdd:pfam08668   7 VALRILALLNDPDSSISDIAELISRDPALTARLLRLANSAYYGLRRPISTISQAVVLLGLRTVRNLAL--GISVKRIFRG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 491536207  288 RELYHL--------SLQRAQFCQLMSRYQPFSHLnEQGFMVGLL 323
Cdd:pfam08668  85 TPPLGFdlkgfwehSLACALAARLLARRLGLDDP-EEAFLAGLL 127
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 86-205 6.72e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 54.72  E-value: 6.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  86 KIVVEVLETCQpTDDLLDAI---RELYREGYLIALDDFTLTPEWRRFLPYVHIVKLDIMAM------GLEKACALVKA-- 154
Cdd:PRK13561 519 TLILEVTESRR-IDDPHAAVailRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPIDVLKIdkmfvdGLPEDDSMVAAii 597

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491536207 155 HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL---VSQTKYVSPE 205
Cdd:PRK13561 598 MLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALpieIFEERYLEEK 651
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 81-211 1.92e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 50.15  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  81 SLPKNKIVVEVLETC--QPTDDLLDAIRELYREGYLIALDDFTLTpewrrFLPYVHIVKLDIMAMGLEKA----C----- 149
Cdd:PRK11359 658 GIDGHQLTVEITESMmmEHDTEIFKRIQILRDMGVGLSVDDFGTG-----FSGLSRLVSLPVTEIKIDKSfvdrCltekr 732

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491536207 150 --ALVKA--HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPLVSQTKYVSPEQVLALQ 211
Cdd:PRK11359 733 ilALLEAitSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLK 798
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
75-195 1.20e-05

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 47.29  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  75 VRRLPRSLPKN--KIVVEVLETCQPTDDLLDAIRE-LYREGYLIALDDF-----TLTPEWRRFLPYVHIVKLDIMAMGLE 146
Cdd:PRK10551 370 VQRLLASLPADhfQIVLEITERDMVQEEEATKLFAwLHSQGIEIAIDDFgtghsALIYLERFTLDYLKIDRGFIQAIGTE 449

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491536207 147 KACALV---KAHLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:PRK10551 450 TVTSPVldaVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
87-195 5.70e-04

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 41.98  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491536207  87 IVVEVLETCQPTDD--LLDAIRELYREGYLIALDDF-----TLTPEWRrfLPyVHIVKLD-IMAMGLEK---ACALVKA- 154
Cdd:PRK10060 527 IDVELTESCLIENEelALSVIQQFSQLGAQVHLDDFgtgysSLSQLAR--FP-IDAIKLDqSFVRDIHKqpvSQSLVRAi 603

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491536207 155 -HLAKRVKYHFLAERVETAEEFEQAKAAGFKFFQGYFFSKPL 195
Cdd:PRK10060 604 vAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPM 645
 
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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