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Conserved domains on  [gi|2473993559|ref|WP_277641921|]
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EAL domain-containing protein [Wolinella succinogenes]

Protein Classification

EAL domain-containing protein( domain architecture ID 10112612)

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

CATH:  3.20.20.450
EC:  3.1.4.52
Gene Ontology:  GO:0071111
SCOP:  4002400

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
6-228 1.14e-39

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: 136.52  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   6 ADIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRFKES-LVPPDIVFDAAHKDEWLF----FALEAAVKSF-QLEHR 79
Cdd:cd01948     1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGgLISPAEFIPLAEETGLIVelgrWVLEEACRQLaRWQAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  80 PGNATLFLNLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPFSLF 154
Cdd:cd01948    81 GPDLRLSVNLSARQLRDPDFLDRLLELLAEtglppRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473993559 155 SFSLLDYAKVMKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY-RP 228
Cdd:cd01948   161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFsRP 235
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
6-228 1.14e-39

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: 136.52  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   6 ADIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRFKES-LVPPDIVFDAAHKDEWLF----FALEAAVKSF-QLEHR 79
Cdd:cd01948     1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGgLISPAEFIPLAEETGLIVelgrWVLEEACRQLaRWQAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  80 PGNATLFLNLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPFSLF 154
Cdd:cd01948    81 GPDLRLSVNLSARQLRDPDFLDRLLELLAEtglppRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473993559 155 SFSLLDYAKVMKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY-RP 228
Cdd:cd01948   161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFsRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
6-228 9.96e-33

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: 124.51  E-value: 9.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   6 ADIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRFKE-SLVPPDIVFDAAHK-------DEWLffaLEAAVKSF-QL 76
Cdd:COG2200   331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERsglivelDRWV---LERALRQLaRW 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  77 EHRPGNATLFLNLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPF 151
Cdd:COG2200   408 PERGLDLRLSVNLSARSLLDPDFLERLLELLAEyglppERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGY 487
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 152 SlfSFSLL-----DYakvMKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY 226
Cdd:COG2200   488 S--SLSYLkrlppDY---LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562

                  ...
gi 2473993559 227 -RP 228
Cdd:COG2200   563 gRP 565
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
12-226 2.81e-26

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: 101.63  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  12 LTQRHFGCEYQPIIQLSNESILAYEALARFRFKES-LVPPDIVFDAAHK-------DEWLffaLEAAVKSFQLEHRPGNA 83
Cdd:pfam00563   8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGgLISPARFLPLAEElgliaelDRWV---LEQALADLAQLQLGPDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  84 TLFLNLDPhLCIKRAHINHW-EKLFK-----DEKIVVEIIENtdssnvELVKNFASLLLNID------IPIALDDIGNPF 151
Cdd:pfam00563  85 KLSINLSP-ASLADPGFLELlRALLKqagppPSRLVLEITES------DLLARLEALREVLKrlralgIRIALDDFGTGY 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473993559 152 SlfSFSLLDYAKV--MKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY 226
Cdd:pfam00563 158 S--SLSYLLRLPPdfVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYF 232
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
7-228 1.72e-23

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 94.59  E-value: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559    7 DIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRF-KESLVPPDIVFDAAHK-------DEWLffaLEAAVKSFQ--L 76
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEFIPLAEEtglivplGRWV---LEQACQQLAewQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   77 EHRPGNATLFLNLDP-HLCIKRaHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNP 150
Cdd:smart00052  80 AQGPPPLLISINLSArQLISPD-LVPRVLELLEEtglppQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  151 FSlfSFSLL-----DYAKVmkfDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFL 225
Cdd:smart00052 159 YS--SLSYLkrlpvDLLKI---DKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYL 233

                   ....
gi 2473993559  226 Y-RP 228
Cdd:smart00052 234 FsRP 237
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
1-228 6.92e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 46.69  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   1 MLLFPADIEAIlTQRHFGCEYQPIIQLSNESILAYEALARFRFKE-SLVPPDIVFDAA-------HKDEWlffALEAAVK 72
Cdd:PRK11359  542 LVLGAALKEAI-SNNQLKLVYQPQIFAETGELYGIEALARWHDPLhGHVPPSRFIPLAeeigeieNIGRW---VIAEACR 617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  73 sfQL-EHRPGNA---TLFLNLDPhLCIKRAHI-NHWEKLFKDEKIVVEI--IENTDSSNVELVKNFAS---LLLNIDIPI 142
Cdd:PRK11359  618 --QLaEWRSQNIhipALSVNLSA-LHFRSNQLpNQVSDAMQAWGIDGHQltVEITESMMMEHDTEIFKriqILRDMGVGL 694
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 143 ALDDIGNPFSlfSFSLLDYAKV--MKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKA 220
Cdd:PRK11359  695 SVDDFGTGFS--GLSRLVSLPVteIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV 772

                  ....*....
gi 2473993559 221 VQGFLY-RP 228
Cdd:PRK11359  773 IQGYFFsRP 781
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
6-228 1.14e-39

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: 136.52  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   6 ADIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRFKES-LVPPDIVFDAAHKDEWLF----FALEAAVKSF-QLEHR 79
Cdd:cd01948     1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGgLISPAEFIPLAEETGLIVelgrWVLEEACRQLaRWQAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  80 PGNATLFLNLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPFSLF 154
Cdd:cd01948    81 GPDLRLSVNLSARQLRDPDFLDRLLELLAEtglppRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473993559 155 SFSLLDYAKVMKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY-RP 228
Cdd:cd01948   161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFsRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
6-228 9.96e-33

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: 124.51  E-value: 9.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   6 ADIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRFKE-SLVPPDIVFDAAHK-------DEWLffaLEAAVKSF-QL 76
Cdd:COG2200   331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERsglivelDRWV---LERALRQLaRW 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  77 EHRPGNATLFLNLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPF 151
Cdd:COG2200   408 PERGLDLRLSVNLSARSLLDPDFLERLLELLAEyglppERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGY 487
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 152 SlfSFSLL-----DYakvMKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY 226
Cdd:COG2200   488 S--SLSYLkrlppDY---LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLF 562

                  ...
gi 2473993559 227 -RP 228
Cdd:COG2200   563 gRP 565
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
12-226 2.81e-26

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: 101.63  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  12 LTQRHFGCEYQPIIQLSNESILAYEALARFRFKES-LVPPDIVFDAAHK-------DEWLffaLEAAVKSFQLEHRPGNA 83
Cdd:pfam00563   8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGgLISPARFLPLAEElgliaelDRWV---LEQALADLAQLQLGPDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  84 TLFLNLDPhLCIKRAHINHW-EKLFK-----DEKIVVEIIENtdssnvELVKNFASLLLNID------IPIALDDIGNPF 151
Cdd:pfam00563  85 KLSINLSP-ASLADPGFLELlRALLKqagppPSRLVLEITES------DLLARLEALREVLKrlralgIRIALDDFGTGY 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473993559 152 SlfSFSLLDYAKV--MKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY 226
Cdd:pfam00563 158 S--SLSYLLRLPPdfVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYF 232
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
7-228 1.72e-23

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 94.59  E-value: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559    7 DIEAILTQRHFGCEYQPIIQLSNESILAYEALARFRF-KESLVPPDIVFDAAHK-------DEWLffaLEAAVKSFQ--L 76
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEFIPLAEEtglivplGRWV---LEQACQQLAewQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   77 EHRPGNATLFLNLDP-HLCIKRaHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNP 150
Cdd:smart00052  80 AQGPPPLLISINLSArQLISPD-LVPRVLELLEEtglppQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  151 FSlfSFSLL-----DYAKVmkfDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFL 225
Cdd:smart00052 159 YS--SLSYLkrlpvDLLKI---DKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYL 233

                   ....
gi 2473993559  226 Y-RP 228
Cdd:smart00052 234 FsRP 237
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
12-228 2.06e-16

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: 77.89  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  12 LTQRHFGCEYQPIIQLSNESILAYEALARFRFKE-SLVPPDIVFDAAHK-------DEWlffALEAAVKSFQLEHRPGNA 83
Cdd:COG5001   434 LERGELELHYQPQVDLATGRIVGAEALLRWQHPErGLVSPAEFIPLAEEtglivplGEW---VLREACRQLAAWQDAGLP 510
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  84 TLFL--NLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPFSlfSF 156
Cdd:COG5001   511 DLRVavNLSARQLRDPDLVDRVRRALAEtglppSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYS--SL 588
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2473993559 157 SLL-----DyakVMKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY-RP 228
Cdd:COG5001   589 SYLkrlpvD---TLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFsRP 663
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
4-228 1.78e-11

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: 63.01  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   4 FPADIEAILTQRHFGCEYQPIIQLSNESILAYEALARFR-FKESLVPPDI-----------------VFDAAHKD--EWL 63
Cdd:COG4943   272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRdPDGSVISPDIfiplaeqsglispltrqVIEQVFRDlgDLL 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  64 ffaleAAVKSFqlehrpgnaTLFLNL------DPHLC--IKRAhINHWEklFKDEKIVVEIIEnTDSSNVELVKNFASLL 135
Cdd:COG4943   352 -----AADPDF---------HISINLsasdllSPRFLddLERL-LARTG--VAPQQIVLEITE-RGFIDPAKARAVIAAL 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 136 LNIDIPIALDDIGNPFSlfSFSLL-----DYAKVMKF--DrhwlTLRESDPSYLILmKSFIEFCDHKRILTVLEGVENED 208
Cdd:COG4943   414 REAGHRIAIDDFGTGYS--SLSYLqtlpvDILKIDKSfvD----AIGTDSANSAVV-PHIIEMAKTLNLDVVAEGVETEE 486
                         250       260
                  ....*....|....*....|.
gi 2473993559 209 HLQFAQEMGVKAVQGFLY-RP 228
Cdd:COG4943   487 QADYLRARGVQYGQGWLFaKP 507
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
1-228 6.92e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 46.69  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   1 MLLFPADIEAIlTQRHFGCEYQPIIQLSNESILAYEALARFRFKE-SLVPPDIVFDAA-------HKDEWlffALEAAVK 72
Cdd:PRK11359  542 LVLGAALKEAI-SNNQLKLVYQPQIFAETGELYGIEALARWHDPLhGHVPPSRFIPLAeeigeieNIGRW---VIAEACR 617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  73 sfQL-EHRPGNA---TLFLNLDPhLCIKRAHI-NHWEKLFKDEKIVVEI--IENTDSSNVELVKNFAS---LLLNIDIPI 142
Cdd:PRK11359  618 --QLaEWRSQNIhipALSVNLSA-LHFRSNQLpNQVSDAMQAWGIDGHQltVEITESMMMEHDTEIFKriqILRDMGVGL 694
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 143 ALDDIGNPFSlfSFSLLDYAKV--MKFDRHWLTLRESDPSYLILMKSFIEFCDHKRILTVLEGVENEDHLQFAQEMGVKA 220
Cdd:PRK11359  695 SVDDFGTGFS--GLSRLVSLPVteIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV 772

                  ....*....
gi 2473993559 221 VQGFLY-RP 228
Cdd:PRK11359  773 IQGYFFsRP 781
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
7-228 1.65e-05

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 45.32  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559   7 DIEAILTQRHFGCEYQPIIQLSNESILAYEALARF-RFKESLVPPDIVFDAAHKD-------EWLffaLEAAVKSFQLEH 78
Cdd:PRK11829  409 DLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWcQPDGSYVLPSGFVHFAEEEgmmvplgNWV---LEEACRILADWK 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559  79 RPG-NATLFLNLDPHLCIKRAHINHWEKLFKD-----EKIVVEIIENTDSSNVELVKNFASLLLNIDIPIALDDIGNPFS 152
Cdd:PRK11829  486 ARGvSLPLSVNISGLQVQNKQFLPHLKTLISHyhidpQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYS 565
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 153 lfSFSLLDYAK-----VMKFDRHWLTLRESDPSYLILMKSFIEFCdhkRILTVLEGVENEDHLQFAQEMGVKAVQGFLYR 227
Cdd:PRK11829  566 --SLRYLNHLKslpihMIKLDKSFVKNLPEDDAIARIISCVSDVL---KVRVMAEGVETEEQRQWLLEHGIQCGQGFLFS 640

                  .
gi 2473993559 228 P 228
Cdd:PRK11829  641 P 641
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
116-228 7.34e-04

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 40.44  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473993559 116 IIENTDSSnVELVKNFASLllniDIPIALDDIGNPFSlfsfSLLDYAK----VMKFDRHWLTLRESDPSYLILMKSFIEF 191
Cdd:PRK10060  536 LIENEELA-LSVIQQFSQL----GAQVHLDDFGTGYS----SLSQLARfpidAIKLDQSFVRDIHKQPVSQSLVRAIVAV 606
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2473993559 192 CDHKRILTVLEGVENEDHLQFAQEMGVKAVQGFLY-RP 228
Cdd:PRK10060  607 AQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFaKP 644
 
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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