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Conserved domains on  [gi|938470559|ref|WP_054630237|]
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EAL domain-containing protein [Paraclostridium sordellii]

Protein Classification

EAL domain-containing protein( domain architecture ID 10005623)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 11-242 8.88e-48

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: 166.11  E-value: 8.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  11 ILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMElELDKLILISVNITS 90
Cdd:COG2200  344 LYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWP-ERGLDLRLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  91 IEIECDNFEVWINKIFSNENLKYiPYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLI 170
Cdd:COG2200  423 RSLLDPDFLERLLELLAEYGLPP-ERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938470559 171 KMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNILKLLA 242
Cdd:COG2200  502 KIDRSFVRDIARDPRdqaIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 11-242 8.88e-48

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: 166.11  E-value: 8.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  11 ILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMElELDKLILISVNITS 90
Cdd:COG2200  344 LYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWP-ERGLDLRLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  91 IEIECDNFEVWINKIFSNENLKYiPYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLI 170
Cdd:COG2200  423 RSLLDPDFLERLLELLAEYGLPP-ERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938470559 171 KMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNILKLLA 242
Cdd:COG2200  502 KIDRSFVRDIARDPRdqaIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 13-231 3.38e-44

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: 148.62  E-value: 3.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   13 YQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSkmELELDKLILISVNITSie 92
Cdd:pfam00563  17 YQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA--QLQLGPDIKLSINLSP-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   93 ieCDNFEVWINKIFSNENLKYIP---YIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDL 169
Cdd:pfam00563  93 --ASLADPGFLELLRALLKQAGPppsRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDF 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938470559  170 IKMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:pfam00563 171 VKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 13-231 1.66e-42

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: 144.23  E-value: 1.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  13 YQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMeLELDKLILISVNITSIE 92
Cdd:cd01948   16 YQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAGGPDLRLSVNLSARQ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  93 IECDNFEVWINKIFSNENLKYiPYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLIKM 172
Cdd:cd01948   95 LRDPDFLDRLLELLAETGLPP-RRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDYLKI 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938470559 173 DKSIIKDI---KNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:cd01948  174 DRSFVRDIetdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 9-231 7.37e-37

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 129.64  E-value: 7.37e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559     9 LNILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMELELDKLILISVNI 88
Cdd:smart00052  13 FLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGPPPLLISINL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559    89 TSIEIECDNFEVWINKIFSNENLKYIpYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMD 168
Cdd:smart00052  93 SARQLISPDLVPRVLELLEETGLPPQ-RLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVD 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938470559   169 LIKMDKSIIKDI---KNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:smart00052 172 LLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
9-231 2.17e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 83.58  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   9 LNILYQPKVNLkNKKITSLEALSRFKDEKGTLLNTEEVINLAksvEEK---RQLTTSVLNIVIKDLSKMElelDKLI--L 83
Cdd:PRK10060 422 LVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYA---EESgliVPLGRWVMLDVVRQVAKWR---DKGInlR 494

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  84 ISVNITSIEIECDNFEVWINKIFSNENLKYIPyIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIID 163
Cdd:PRK10060 495 VAVNVSARQLADQTIFTALKQALQELNFEYCP-IDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLA 573

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938470559 164 KYNMDLIKMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:PRK10060 574 RFPIDAIKLDQSFVRDIHKQPVsqsLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 11-242 8.88e-48

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: 166.11  E-value: 8.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  11 ILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMElELDKLILISVNITS 90
Cdd:COG2200  344 LYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWP-ERGLDLRLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  91 IEIECDNFEVWINKIFSNENLKYiPYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLI 170
Cdd:COG2200  423 RSLLDPDFLERLLELLAEYGLPP-ERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938470559 171 KMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNILKLLA 242
Cdd:COG2200  502 KIDRSFVRDIARDPRdqaIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 13-231 3.38e-44

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: 148.62  E-value: 3.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   13 YQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSkmELELDKLILISVNITSie 92
Cdd:pfam00563  17 YQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA--QLQLGPDIKLSINLSP-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   93 ieCDNFEVWINKIFSNENLKYIP---YIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDL 169
Cdd:pfam00563  93 --ASLADPGFLELLRALLKQAGPppsRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDF 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938470559  170 IKMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:pfam00563 171 VKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 13-231 1.66e-42

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: 144.23  E-value: 1.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  13 YQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMeLELDKLILISVNITSIE 92
Cdd:cd01948   16 YQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAGGPDLRLSVNLSARQ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  93 IECDNFEVWINKIFSNENLKYiPYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLIKM 172
Cdd:cd01948   95 LRDPDFLDRLLELLAETGLPP-RRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDYLKI 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938470559 173 DKSIIKDI---KNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:cd01948  174 DRSFVRDIetdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 9-231 7.37e-37

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 129.64  E-value: 7.37e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559     9 LNILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMELELDKLILISVNI 88
Cdd:smart00052  13 FLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGPPPLLISINL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559    89 TSIEIECDNFEVWINKIFSNENLKYIpYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMD 168
Cdd:smart00052  93 SARQLISPDLVPRVLELLEETGLPPQ-RLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVD 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938470559   169 LIKMDKSIIKDI---KNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:smart00052 172 LLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 13-242 1.51e-32

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: 124.50  E-value: 1.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  13 YQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAksvEEK---RQLTTSVLNIVIKDLSKMELELDKLILISVNIT 89
Cdd:COG5001  443 YQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLA---EETgliVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLS 519

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  90 SIEIECDNFEVWINKIFSNENLKyiP-YIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFN-----Kveiid 163
Cdd:COG5001  520 ARQLRDPDLVDRVRRALAETGLP--PsRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSslsylK----- 592

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559 164 KYNMDLIKMDKSIIKDI---KNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNILKL 240
Cdd:COG5001  593 RLPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672


                 ..
gi 938470559 241 LA 242
Cdd:COG5001  673 LR 674
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 13-242 2.97e-32

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: 123.10  E-value: 2.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  13 YQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAksveEK----RQLTTSVLNIVIKDLSKMeLELDKLILISVNI 88
Cdd:COG4943  289 YQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLA----EQsgliSPLTRQVIEQVFRDLGDL-LAADPDFHISINL 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  89 TSIEIECDNFEVWINKIFSNENLKYIPyIEFELSEKNKIENSlNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMD 168
Cdd:COG4943  364 SASDLLSPRFLDDLERLLARTGVAPQQ-IVLEITERGFIDPA-KARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVD 441

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938470559 169 LIKMDKSIIKDIK---NNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNILKLLA 242
Cdd:COG4943  442 ILKIDKSFVDAIGtdsANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLA 518
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
9-231 2.17e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 83.58  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   9 LNILYQPKVNLkNKKITSLEALSRFKDEKGTLLNTEEVINLAksvEEK---RQLTTSVLNIVIKDLSKMElelDKLI--L 83
Cdd:PRK10060 422 LVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYA---EESgliVPLGRWVMLDVVRQVAKWR---DKGInlR 494

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  84 ISVNITSIEIECDNFEVWINKIFSNENLKYIPyIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIID 163
Cdd:PRK10060 495 VAVNVSARQLADQTIFTALKQALQELNFEYCP-IDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLA 573

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938470559 164 KYNMDLIKMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:PRK10060 574 RFPIDAIKLDQSFVRDIHKQPVsqsLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 3-231 6.90e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 76.35  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559   3 KESIK--CLNILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMELELDK 80
Cdd:PRK11359 549 KEAISnnQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIH 628

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  81 LILISVNITSIEIECDNFEVWINKIFSNENlkyIP--YIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNK 158
Cdd:PRK11359 629 IPALSVNLSALHFRSNQLPNQVSDAMQAWG---IDghQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSG 705

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938470559 159 VEIIDKYNMDLIKMDKSIIKDIKNNKK---LIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:PRK11359 706 LSRLVSLPVTEIKIDKSFVDRCLTEKRilaLLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
11-239 4.16e-14

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 71.18  E-value: 4.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  11 ILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMELELDKLILISVNITS 90
Cdd:PRK10551 279 VEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLPVGAKLGINISP 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  91 IEIECDNFEVWINKIFSNENLKYIPYIeFELSEKNKIENSLNMKrKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLI 170
Cdd:PRK10551 359 AHLHSDSFKADVQRLLASLPADHFQIV-LEITERDMVQEEEATK-LFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYL 436

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938470559 171 KMDKSIIKDIKNN---KKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNILK 239
Cdd:PRK10551 437 KIDRGFIQAIGTEtvtSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVR 508
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 14-231 4.89e-14

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 71.13  E-value: 4.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  14 QPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAksveEKRQLTTSVLNIVIKDLSKMELELDK---LILISVNITS 90
Cdd:PRK11829 424 QPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFA----EEEGMMVPLGNWVLEEACRILADWKArgvSLPLSVNISG 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  91 IEIECDNFEVWINKIFSNENLKyIPYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVG---SGFNKVEIIDKYNM 167
Cdd:PRK11829 500 LQVQNKQFLPHLKTLISHYHID-PQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGigySSLRYLNHLKSLPI 578

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938470559 168 DLIKMDKSIIKDIKNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:PRK11829 579 HMIKLDKSFVKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 14-231 2.35e-09

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 57.03  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  14 QPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMELELDKLILiSVNITSIEI 93
Cdd:PRK13561 419 QPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPL-SVNLSALQL 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  94 ECDNFEVWINKIFSNENLKYIPYIeFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYN---MDLI 170
Cdd:PRK13561 498 MHPNMVADMLELLTRYRIQPGTLI-LEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVL 576

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938470559 171 KMDKSIIKDIKNNKKLIDMICKTAKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:PRK13561 577 KIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 135-242 2.95e-08

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 53.27  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559 135 RKIKFLKNKGFKVSFDDVGSGFNKVEIIDKynMDLIKMDksiIKDIknNKKLIDMICKTAKEKGFEVVAEGIEDMETYMI 214
Cdd:COG3434  102 EALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID---VLAL--DLEELAELVARLKRYGIKLLAEKVETREEFEL 174

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 938470559 215 LKNLNCELGQGFYFHKPN---------SFQNILKLLA 242
Cdd:COG3434  175 CKELGFDLFQGYFFSKPEilkgkklppSQLTLLQLLN 211
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 117-238 1.54e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 48.52  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  117 IEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYNMDLIKMDKSIIKDIKNN---KKLIDMICKT 193
Cdd:PRK09776  960 LHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNlmdEMLISIIQGH 1039

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 938470559  194 AKEKGFEVVAEGIEDMETYMILKNLNCELGQGFYFHKPNSFQNIL 238
Cdd:PRK09776 1040 AQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLL 1084
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 11-231 4.20e-06

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 47.16  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  11 ILYQPKVNLKNKKITSLEALSRFKDEKGTLLNTEEVINLAKSVEEKRQLTTSVLNIVIKDLSKMELELdklilISVNITS 90
Cdd:PRK11059 418 RLYQQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEEN-----LSINLSV 492

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938470559  91 IEIECDNFEVWinkiFSNENLKYI----PYIEFELSEKNKIENSLNMKRKIKFLKNKGFKVSFDDVGSGFNKVEIIDKYN 166
Cdd:PRK11059 493 DSLLSRAFQRW----LRDTLLQCPrsqrKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELN 568

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938470559 167 MDLIKMDKSIIKDIK---NNKKLI-DMI--CKTAKEKgfeVVAEGIEDMETYMILKNLNCELGQGFYFHKP 231
Cdd:PRK11059 569 VELIKLHPSLVRNIHkrtENQLFVrSLVgaCAGTETQ---VFATGVESREEWQTLQELGVSGGQGDFFAES 636
 
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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