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Conserved domains on  [gi|502333110|ref|WP_012766331|]
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MULTISPECIES: EAL domain-containing protein [Gammaproteobacteria]

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 ...
3-209 9.11e-28

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: 105.32  E-value: 9.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSEL-----SSppnwGLvDIEIARFIQDNLCHCSEEYQA------L 70
Cdd:cd01948   12 FELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFiplaeET----GL-IVELGRWVLEEACRQLARWQAggpdlrL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  71 FVNVSEQTLKSDIIFHTWAQIIRAitknYPL---RLVIEITEG--VQDKSLAFRW-SSLTAMGVNLALDDYGDKNSSMAR 144
Cdd:cd01948   87 SVNLSARQLRDPDFLDRLLELLAE----TGLpprRLVLEITESalIDDLEEALATlRRLRALGVRIALDDFGTGYSSLSY 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502333110 145 LLSYDWNYCKFDA---RKLSSFEDYSAILH-----CRRKGIHLIAEQVETPplEENAKL--LGLVWQQGFLHGKP 209
Cdd:cd01948  163 LKRLPVDYLKIDRsfvRDIETDPEDRAIVRaiialAHSLGLKVVAEGVETE--EQLELLreLGCDYVQGYLFSRP 235
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
3-209 9.11e-28

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: 105.32  E-value: 9.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSEL-----SSppnwGLvDIEIARFIQDNLCHCSEEYQA------L 70
Cdd:cd01948   12 FELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFiplaeET----GL-IVELGRWVLEEACRQLARWQAggpdlrL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  71 FVNVSEQTLKSDIIFHTWAQIIRAitknYPL---RLVIEITEG--VQDKSLAFRW-SSLTAMGVNLALDDYGDKNSSMAR 144
Cdd:cd01948   87 SVNLSARQLRDPDFLDRLLELLAE----TGLpprRLVLEITESalIDDLEEALATlRRLRALGVRIALDDFGTGYSSLSY 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502333110 145 LLSYDWNYCKFDA---RKLSSFEDYSAILH-----CRRKGIHLIAEQVETPplEENAKL--LGLVWQQGFLHGKP 209
Cdd:cd01948  163 LKRLPVDYLKIDRsfvRDIETDPEDRAIVRaiialAHSLGLKVVAEGVETE--EQLELLreLGCDYVQGYLFSRP 235
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
3-209 3.43e-23

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: 93.15  E-value: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110    3 FSPALQQIKDVGTGSFVAAEVLARWC-CEGQMLTPSE-LSSPPNWGLvDIEIARFIQDNLC-----HCSEEYQALFVNVS 75
Cdd:pfam00563  13 FVLYYQPIVDLRTGRVVGYEALLRWQhPDGGLISPARfLPLAEELGL-IAELDRWVLEQALadlaqLQLGPDIKLSINLS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   76 EQTLKSdiifHTWAQIIRAITKNYPL---RLVIEITEG---VQDKSLAFRWSSLTAMGVNLALDDYGDKNSSMARLLSYD 149
Cdd:pfam00563  92 PASLAD----PGFLELLRALLKQAGPppsRLVLEITESdllARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLP 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502333110  150 WNYCKFDARKLSSFED-------YSAILH-CRRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:pfam00563 168 PDFVKIDRSLIADIDKdgearaiVRALIAlAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
3-209 1.20e-22

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: 95.62  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSE-LSSPPNWGLVdIEIARFIQDNLCHCSEEYQA------LFVNV 74
Cdd:COG2200  342 LRLYYQPIVDLRTGRVVGYEALLRWRHpDGGLISPAEfIPAAERSGLI-VELDRWVLERALRQLARWPErgldlrLSVNL 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  75 SEQTLKSDiifhTWAQIIRAITKNYPL---RLVIEITEGV--QDKSLAFRW-SSLTAMGVNLALDDYGDKNSSMARLLSY 148
Cdd:COG2200  421 SARSLLDP----DFLERLLELLAEYGLppeRLVLEITESAllEDLEAAIELlARLRALGVRIALDDFGTGYSSLSYLKRL 496
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502333110 149 DWNYCKFDA---RKLSSFEDYSAILH-----CRRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:COG2200  497 PPDYLKIDRsfvRDIARDPRDQAIVRaivalAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
3-209 2.23e-17

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 78.03  E-value: 2.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110     3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSE-LSSPPNWGLVdIEIARFIQDNLCHCSEEYQA-------LFVN 73
Cdd:smart00052  13 FLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEfIPLAEETGLI-VPLGRWVLEQACQQLAEWQAqgpppllISIN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110    74 VSEQTLKSDiifhTWAQIIRAITKNYPL---RLVIEITEGV---QDKSLAFRWSSLTAMGVNLALDDYGDKNSSMARLLS 147
Cdd:smart00052  92 LSARQLISP----DLVPRVLELLEETGLppqRLELEITESVlldDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKR 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   148 YDWNYCKFD----ARKLSSFED----YSAILHCRRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:smart00052 168 LPVDLLKIDksfvRDLQTDPEDeaivQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
72-209 4.73e-06

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 46.60  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  72 VNVSEQTLKSDIIFHTWAQIIRAITKNYPLrLVIEITEG--VQDKSLA------FRwssltAMGVNLALDDYGDKNSSMA 143
Cdd:PRK10060 497 VNVSARQLADQTIFTALKQALQELNFEYCP-IDVELTESclIENEELAlsviqqFS-----QLGAQVHLDDFGTGYSSLS 570
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110 144 RLLSYdwnycKFDARKLssfeDYSAILHCRRKGI-----------------HLIAEQVETPPLEENAKLLGLVWQQGFLH 206
Cdd:PRK10060 571 QLARF-----PIDAIKL----DQSFVRDIHKQPVsqslvraivavaqalnlQVIAEGVETAKEDAFLTKNGVNERQGFLF 641

                 ...
gi 502333110 207 GKP 209
Cdd:PRK10060 642 AKP 644
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
3-209 9.11e-28

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: 105.32  E-value: 9.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSEL-----SSppnwGLvDIEIARFIQDNLCHCSEEYQA------L 70
Cdd:cd01948   12 FELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFiplaeET----GL-IVELGRWVLEEACRQLARWQAggpdlrL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  71 FVNVSEQTLKSDIIFHTWAQIIRAitknYPL---RLVIEITEG--VQDKSLAFRW-SSLTAMGVNLALDDYGDKNSSMAR 144
Cdd:cd01948   87 SVNLSARQLRDPDFLDRLLELLAE----TGLpprRLVLEITESalIDDLEEALATlRRLRALGVRIALDDFGTGYSSLSY 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502333110 145 LLSYDWNYCKFDA---RKLSSFEDYSAILH-----CRRKGIHLIAEQVETPplEENAKL--LGLVWQQGFLHGKP 209
Cdd:cd01948  163 LKRLPVDYLKIDRsfvRDIETDPEDRAIVRaiialAHSLGLKVVAEGVETE--EQLELLreLGCDYVQGYLFSRP 235
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
3-209 3.43e-23

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: 93.15  E-value: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110    3 FSPALQQIKDVGTGSFVAAEVLARWC-CEGQMLTPSE-LSSPPNWGLvDIEIARFIQDNLC-----HCSEEYQALFVNVS 75
Cdd:pfam00563  13 FVLYYQPIVDLRTGRVVGYEALLRWQhPDGGLISPARfLPLAEELGL-IAELDRWVLEQALadlaqLQLGPDIKLSINLS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   76 EQTLKSdiifHTWAQIIRAITKNYPL---RLVIEITEG---VQDKSLAFRWSSLTAMGVNLALDDYGDKNSSMARLLSYD 149
Cdd:pfam00563  92 PASLAD----PGFLELLRALLKQAGPppsRLVLEITESdllARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLP 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502333110  150 WNYCKFDARKLSSFED-------YSAILH-CRRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:pfam00563 168 PDFVKIDRSLIADIDKdgearaiVRALIAlAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
3-209 1.20e-22

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: 95.62  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSE-LSSPPNWGLVdIEIARFIQDNLCHCSEEYQA------LFVNV 74
Cdd:COG2200  342 LRLYYQPIVDLRTGRVVGYEALLRWRHpDGGLISPAEfIPAAERSGLI-VELDRWVLERALRQLARWPErgldlrLSVNL 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  75 SEQTLKSDiifhTWAQIIRAITKNYPL---RLVIEITEGV--QDKSLAFRW-SSLTAMGVNLALDDYGDKNSSMARLLSY 148
Cdd:COG2200  421 SARSLLDP----DFLERLLELLAEYGLppeRLVLEITESAllEDLEAAIELlARLRALGVRIALDDFGTGYSSLSYLKRL 496
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502333110 149 DWNYCKFDA---RKLSSFEDYSAILH-----CRRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:COG2200  497 PPDYLKIDRsfvRDIARDPRDQAIVRaivalAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
3-209 2.23e-17

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 78.03  E-value: 2.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110     3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSE-LSSPPNWGLVdIEIARFIQDNLCHCSEEYQA-------LFVN 73
Cdd:smart00052  13 FLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEfIPLAEETGLI-VPLGRWVLEQACQQLAEWQAqgpppllISIN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110    74 VSEQTLKSDiifhTWAQIIRAITKNYPL---RLVIEITEGV---QDKSLAFRWSSLTAMGVNLALDDYGDKNSSMARLLS 147
Cdd:smart00052  92 LSARQLISP----DLVPRVLELLEETGLppqRLELEITESVlldDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKR 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   148 YDWNYCKFD----ARKLSSFED----YSAILHCRRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:smart00052 168 LPVDLLKIDksfvRDLQTDPEDeaivQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
3-209 1.77e-13

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: 69.03  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARWCC-EGQMLTPSEL-----SSppnwGLVdIEIARFIQDNLCHCSEEYQA------- 69
Cdd:COG5001  439 LELHYQPQVDLATGRIVGAEALLRWQHpERGLVSPAEFiplaeET----GLI-VPLGEWVLREACRQLAAWQDaglpdlr 513
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  70 LFVNVSEQTLKSDiifhTWAQIIRAITKNYPL---RLVIEITEGV--QDKSLAFRW-SSLTAMGVNLALDDYGDKNSSMA 143
Cdd:COG5001  514 VAVNLSARQLRDP----DLVDRVRRALAETGLppsRLELEITESAllEDPEEALETlRALRALGVRIALDDFGTGYSSLS 589
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502333110 144 RLLSYDWNYCKFDA---RKLSSFEDYSAILH-----CRRKGIHLIAEQVETpplEENAKLL---GLVWQQGFLHGKP 209
Cdd:COG5001  590 YLKRLPVDTLKIDRsfvRDLAEDPDDAAIVRaiialAHSLGLEVVAEGVET---EEQLEFLrelGCDYAQGYLFSRP 663
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
47-224 2.32e-13

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 68.29  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  47 LVDIEIARFIQDNLChcseeyqalFVNVSEQTLKSDIIFhtwaqiiraitknyPL---RLVIEITEGVQ-DKSLAFRWSS 122
Cdd:COG3434   50 FLEIGLDRLLGGKLA---------FINFTEELLLSDLPE--------------LLppeRVVLEILEDVEpDEELLEALKE 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110 123 LTAMGVNLALDDYGDkNSSMARLLSYdWNYCKFDARKLSSFEDYSAILHCRRKGIHLIAEQVETPPLEENAKLLGLVWQQ 202
Cdd:COG3434  107 LKEKGYRIALDDFVL-DPEWDPLLPL-ADIIKIDVLALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQ 184
                        170       180
                 ....*....|....*....|....*
gi 502333110 203 GFLHGKPTVIE-KSL--NRAKVLPL 224
Cdd:COG3434  185 GYFFSKPEILKgKKLppSQLTLLQL 209
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
72-209 4.73e-06

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 46.60  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  72 VNVSEQTLKSDIIFHTWAQIIRAITKNYPLrLVIEITEG--VQDKSLA------FRwssltAMGVNLALDDYGDKNSSMA 143
Cdd:PRK10060 497 VNVSARQLADQTIFTALKQALQELNFEYCP-IDVELTESclIENEELAlsviqqFS-----QLGAQVHLDDFGTGYSSLS 570
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110 144 RLLSYdwnycKFDARKLssfeDYSAILHCRRKGI-----------------HLIAEQVETPPLEENAKLLGLVWQQGFLH 206
Cdd:PRK10060 571 QLARF-----PIDAIKL----DQSFVRDIHKQPVsqslvraivavaqalnlQVIAEGVETAKEDAFLTKNGVNERQGFLF 641

                 ...
gi 502333110 207 GKP 209
Cdd:PRK10060 642 AKP 644
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
3-209 4.87e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 46.63  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110   3 FSPALQQIKDVGTGSFVAAEVLARW-CCEGQMLTPSEL-SSPPNWGLVdIEIARFIQDNLCHCSEEYQA------LFVNV 74
Cdd:PRK13561 414 FAIWLQPQVEMRSGKLVSAEALLRMqQPDGSWDLPEGLiDRIESCGLM-VTVGHWVLEESCRLLAAWQErgimlpLSVNL 492
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  75 SE-QTLKSDIIFHTWAQIIR-AITknyPLRLVIEITEGVQ----DKSLAfRWSSLTAMGVNLALDDYGDKNSSMARLlsy 148
Cdd:PRK13561 493 SAlQLMHPNMVADMLELLTRyRIQ---PGTLILEVTESRRiddpHAAVA-ILRPLRNAGVRVALDDFGMGYAGLRQL--- 565
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502333110 149 dwNYCK---FDARKLS-SF-----EDYSA----ILHCRRKGIHLIAEQVETPplEENAKLL--GLVWQQGFLHGKP 209
Cdd:PRK13561 566 --QHMKslpIDVLKIDkMFvdglpEDDSMvaaiIMLAQSLNLQVIAEGVETE--AQRDWLLkaGVGIAQGFLFARA 637
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
69-209 9.56e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 45.92  E-value: 9.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502333110  69 ALFVNVSEQTLKSDIIFHTWAQIIR--AITKNyplRLVIEITEGV---QDKSLAFRWSSLTAMGVNLALDDYGDKNSSMA 143
Cdd:PRK11359 631 ALSVNLSALHFRSNQLPNQVSDAMQawGIDGH---QLTVEITESMmmeHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLS 707
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502333110 144 RLLSY-------DWNY---CKFDARKLSSFEDYSAILHcrRKGIHLIAEQVETPPLEENAKLLGLVWQQGFLHGKP 209
Cdd:PRK11359 708 RLVSLpvteikiDKSFvdrCLTEKRILALLEAITSIGQ--SLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
 
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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