NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1699383857|gb|QDI56754|]
View 

GGDEF domain-containing protein [Serratia marcescens]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10005578)

GGDEF domain-containing protein may have diguanylate cyclase (DGC) activity, similar to Escherichia coli DgcT (YcdT) and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

CATH:  3.30.70.270
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0046872|GO:0052621|GO:0005886
PubMed:  11119645|15063857|15289546|15306016|16530465|16045609

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 295-560 1.01e-51

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


:

Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 178.25  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 295 LETVASRHKIYDSQTTIYGMIALAGLVVLLFILPALVFCTNINRWLTKTHNNIVRLSRGEMNIDRNDAFYSRELIAISDA 374
Cdd:COG2199     6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 375 IQQLRQYQLDKVSLESEKQLLIKELEASSFLDPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGH 450
Cdd:COG2199    86 LLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEerleRELARARREGRPLALLLIDLDHFKRINDTYGH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 451 DVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNLtDGRQVRFTTSCGIAPVN 530
Cdd:COG2199   166 AAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYP 244

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1699383857 531 AF-TALQAAIKQADEALYFCKKNGKDRVSVH 560
Cdd:COG2199   245 EDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 295-560 1.01e-51

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 178.25  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 295 LETVASRHKIYDSQTTIYGMIALAGLVVLLFILPALVFCTNINRWLTKTHNNIVRLSRGEMNIDRNDAFYSRELIAISDA 374
Cdd:COG2199     6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 375 IQQLRQYQLDKVSLESEKQLLIKELEASSFLDPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGH 450
Cdd:COG2199    86 LLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEerleRELARARREGRPLALLLIDLDHFKRINDTYGH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 451 DVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNLtDGRQVRFTTSCGIAPVN 530
Cdd:COG2199   166 AAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYP 244

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1699383857 531 AF-TALQAAIKQADEALYFCKKNGKDRVSVH 560
Cdd:COG2199   245 EDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 406-557 7.07e-48

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 163.88  E-value: 7.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:cd01949     3 DPLTGLPNRRAFEerleRLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRltLNLTDGRQVRFTTSCGIAPVNAFTA-LQAAIKQADEALYFCKKNGKDRV 557
Cdd:cd01949    83 FAILLPGTDLEEAEALAERLREAIEE--PFFIDGQEIRVTASIGIATYPEDGEdAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 403-560 5.42e-42

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 148.16  E-value: 5.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857  403 SFLDPLTNIYNRRKFFLEC----QLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYG 478
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELeqelQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857  479 GEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNltDGRQVRFTTSCGIA--PVNAFTALQaAIKQADEALYFCKKNGKDR 556
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAayPNPGEDAED-LLKRADTALYQAKKAGRNQ 159


                   ....
gi 1699383857  557 VSVH 560
Cdd:smart00267 160 VAVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 403-556 2.47e-40

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 143.93  E-value: 2.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 403 SFLDPLTNIYNRRKFFL----ECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYG 478
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEqleqELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 479 GEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNLT-DGRQVRFTTSCGIA--PVNAFTAlQAAIKQADEALYFCKKNGKD 555
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTvSGLPLYVTISIGIAayPNDGEDP-EDLLKRADTALYQAKQAGRN 159


                  .
gi 1699383857 556 R 556
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 406-559 1.04e-37

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 136.70  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:TIGR00254   5 DPLTGLYNRRYLEemldSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRLTLNLTDGRQVRFTTSCGIAP-VNAFTALQAAIKQADEALYFCKKNGKDRVSV 559
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACyPGHGLTLEELLKRADEALYQAKKAGRNRVVV 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
368-557 3.45e-33

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 127.02  E-value: 3.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 368 LIAISDAIQ----------------QLRQyqLDKVSLESEK-QLLIKE----LEASSFLDPLTNIYNRRkfFLECQLLGD 426
Cdd:NF038266   40 LTRISDGYQsaarerelslaerydrQLRR--LEKIVRISDRyQRMMRDlneaLREASTRDPLTGLPNRR--LLMERLREE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 427 SSYPQ----AFCL--IDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQ 500
Cdd:NF038266  116 VERARrsgrPFTLamLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLER 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1699383857 501 LRTRTHRLTLNLTDgRQVRFTTSCGIAPV-NAFTALQAAIKQADEALYFCKKNGKDRV 557
Cdd:NF038266  196 LREAVRALAVRVGD-DVLSVTASAGLAEHrPPEEGLSATLSRADQALYQAKRAGRDRV 252
pleD PRK09581
response regulator PleD; Reviewed
 406-557 4.37e-28

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 117.31  E-value: 4.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFFLECQLL----GDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:PRK09581  295 DGLTGLHNRRYFDMHLKNLieraNERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRLTLNLTDG-RQVRFTTSCGIAPVN-AFTALQAAIKQADEALYFCKKNGKDRV 557
Cdd:PRK09581  375 FVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAELRpSGDTIEALIKRADKALYEAKNTGRNRV 452
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
424-559 2.15e-24

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 104.45  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 424 LGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRT 503
Cdd:NF041606  203 INSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRK 282

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1699383857 504 RTHRLTLnLTDGRQVRFTTSCGIAPVNA-FTALQAAIKQADEALYFCKKNGKDRVSV 559
Cdd:NF041606  283 SIENLSI-LYDEQHIRVTISIGVAEYNFdVESAKSLVERADKALYESKQNGRNRVSI 338
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 295-560 1.01e-51

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 178.25  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 295 LETVASRHKIYDSQTTIYGMIALAGLVVLLFILPALVFCTNINRWLTKTHNNIVRLSRGEMNIDRNDAFYSRELIAISDA 374
Cdd:COG2199     6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 375 IQQLRQYQLDKVSLESEKQLLIKELEASSFLDPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGH 450
Cdd:COG2199    86 LLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEerleRELARARREGRPLALLLIDLDHFKRINDTYGH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 451 DVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNLtDGRQVRFTTSCGIAPVN 530
Cdd:COG2199   166 AAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYP 244

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1699383857 531 AF-TALQAAIKQADEALYFCKKNGKDRVSVH 560
Cdd:COG2199   245 EDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 406-557 7.07e-48

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 163.88  E-value: 7.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:cd01949     3 DPLTGLPNRRAFEerleRLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRltLNLTDGRQVRFTTSCGIAPVNAFTA-LQAAIKQADEALYFCKKNGKDRV 557
Cdd:cd01949    83 FAILLPGTDLEEAEALAERLREAIEE--PFFIDGQEIRVTASIGIATYPEDGEdAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 403-560 5.42e-42

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 148.16  E-value: 5.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857  403 SFLDPLTNIYNRRKFFLEC----QLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYG 478
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELeqelQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857  479 GEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNltDGRQVRFTTSCGIA--PVNAFTALQaAIKQADEALYFCKKNGKDR 556
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAayPNPGEDAED-LLKRADTALYQAKKAGRNQ 159


                   ....
gi 1699383857  557 VSVH 560
Cdd:smart00267 160 VAVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 403-556 2.47e-40

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 143.93  E-value: 2.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 403 SFLDPLTNIYNRRKFFL----ECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYG 478
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEqleqELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 479 GEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNLT-DGRQVRFTTSCGIA--PVNAFTAlQAAIKQADEALYFCKKNGKD 555
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTvSGLPLYVTISIGIAayPNDGEDP-EDLLKRADTALYQAKQAGRN 159


                  .
gi 1699383857 556 R 556
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 406-559 1.04e-37

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 136.70  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:TIGR00254   5 DPLTGLYNRRYLEemldSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRLTLNLTDGRQVRFTTSCGIAP-VNAFTALQAAIKQADEALYFCKKNGKDRVSV 559
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACyPGHGLTLEELLKRADEALYQAKKAGRNRVVV 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
368-557 3.45e-33

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 127.02  E-value: 3.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 368 LIAISDAIQ----------------QLRQyqLDKVSLESEK-QLLIKE----LEASSFLDPLTNIYNRRkfFLECQLLGD 426
Cdd:NF038266   40 LTRISDGYQsaarerelslaerydrQLRR--LEKIVRISDRyQRMMRDlneaLREASTRDPLTGLPNRR--LLMERLREE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 427 SSYPQ----AFCL--IDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQ 500
Cdd:NF038266  116 VERARrsgrPFTLamLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLER 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1699383857 501 LRTRTHRLTLNLTDgRQVRFTTSCGIAPV-NAFTALQAAIKQADEALYFCKKNGKDRV 557
Cdd:NF038266  196 LREAVRALAVRVGD-DVLSVTASAGLAEHrPPEEGLSATLSRADQALYQAKRAGRDRV 252
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 271-562 8.42e-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: 130.28  E-value: 8.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 271 AALISRYVDELSGLSQALYQRSFELETVASRHKIYDSQTTIYGMIALAGLVVLLFILPALVFCTNINRWLTKTHNNIVRL 350
Cdd:COG5001   119 LLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 351 SRGEMNIDRNDAFYSRELIAISDAIQQLRQYQLDKVSLESEKQLLIKELEASSFLDPLTNIYNRRKFF--LEcQLLGDSS 428
Cdd:COG5001   199 LLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLdrLE-QALARAR 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 429 YPQ---AFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNC-SLDNARDIMEQLRTR 504
Cdd:COG5001   278 RSGrrlALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLdDPEDAEAVAERILAA 357

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699383857 505 THR-LTLnltDGRQVRFTTSCGIA--PVNAFTAlQAAIKQADEALYFCKKNGKDRVSVHTQ 562
Cdd:COG5001   358 LAEpFEL---DGHELYVSASIGIAlyPDDGADA-EELLRNADLAMYRAKAAGRNRYRFFDP 414
pleD PRK09581
response regulator PleD; Reviewed
 406-557 4.37e-28

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 117.31  E-value: 4.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFFLECQLL----GDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:PRK09581  295 DGLTGLHNRRYFDMHLKNLieraNERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRLTLNLTDG-RQVRFTTSCGIAPVN-AFTALQAAIKQADEALYFCKKNGKDRV 557
Cdd:PRK09581  375 FVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAELRpSGDTIEALIKRADKALYEAKNTGRNRV 452
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
406-557 6.62e-28

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 117.81  E-value: 6.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 406 DPLTNIYNRRKFF----LECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEE 481
Cdd:PRK15426  401 DPLTRLYNRGALFekarALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 482 FAVLLGNCSLDNARDIMEQLRTRTHRLTLNLTDGRQVRFTTSCGIAPVNA-----FTALQAAikqADEALYFCKKNGKDR 556
Cdd:PRK15426  481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEdgdydFEQLQSL---ADRRLYLAKQAGRNR 557


                  .
gi 1699383857 557 V 557
Cdd:PRK15426  558 V 558
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 397-559 3.76e-27

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 113.00  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 397 KELEASSFLDPLTNIYNRRKFFLECQLLGDSSYPQ----AFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASD 472
Cdd:PRK10245  199 RRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHhrdaTLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 473 IFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTHRLTLNLTDgrQVRFTTSCGIAPVNA-FTALQAAIKQADEALYFCKK 551
Cdd:PRK10245  279 VIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAP--QVTLRISVGVAPLNPqMSHYREWLKSADLALYKAKN 356


                  ....*...
gi 1699383857 552 NGKDRVSV 559
Cdd:PRK10245  357 AGRNRTEV 364
PRK09894 PRK09894
diguanylate cyclase; Provisional
 349-557 8.40e-26

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 107.46  E-value: 8.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 349 RLSRGEMNIDRNDAFYSReLIAISDAIQQLRQYQLdkvslesekqllikelEASSFLDPLTNIYNRRKFF--LECQLLGD 426
Cdd:PRK09894   92 AIVEGHWQDAHFDAFQEG-LLSFTAALTDYKIYLL----------------TIRSNMDVLTGLPGRRVLDesFDHQLRNR 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 427 SSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTH 506
Cdd:PRK09894  155 EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIA 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1699383857 507 RLTLNLTDGRqVRFTTSCGIAPVNAFTALQAAIKQADEALYFCKKNGKDRV 557
Cdd:PRK09894  235 NHAITHSDGR-INITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRV 284
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 390-560 1.08e-24

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 108.99  E-value: 1.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857  390 SEKQLLIKELEASSFLDPLTNIYNRRKFFLE----CQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQ 465
Cdd:PRK09776   652 TESRKMLRQLSYSASHDALTHLANRASFEKQlrrlLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857  466 RAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQL--RTRTHRLTLnltDGRQVRFTTSCGIAPVNAfTALQAA--IKQ 541
Cdd:PRK09776   732 SMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIisAINDYHFPW---EGRVYRVGASAGITLIDA-NNHQASevMSQ 807

                          170
                   ....*....|....*....
gi 1699383857  542 ADEALYFCKKNGKDRVSVH 560
Cdd:PRK09776   808 ADIACYAAKNAGRGRVTVY 826
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
424-559 2.15e-24

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 104.45  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 424 LGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRT 503
Cdd:NF041606  203 INSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRK 282

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1699383857 504 RTHRLTLnLTDGRQVRFTTSCGIAPVNA-FTALQAAIKQADEALYFCKKNGKDRVSV 559
Cdd:NF041606  283 SIENLSI-LYDEQHIRVTISIGVAEYNFdVESAKSLVERADKALYESKQNGRNRVSI 338
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 331-527 1.95e-14

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 76.35  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 331 VFCTNINRWLTKTHNNIVRLSRGEMN--------------------IDRND-------AFYSRE-------LIAISDAIQ 376
Cdd:PRK11359  277 IICRNIESVLNESHVSLFALRNGMPIhwassshgaeyqnaqswsatIRQRDgapagtlQIKTSSgaetsafIERVADISQ 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 377 QLRQyqldkVSLESEKQLliKELEASSFLDPLTNIYNRRKFFLECQLLGDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQA 456
Cdd:PRK11359  357 HLAA-----LALEQEKSR--QHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQA 429

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699383857 457 LVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTHRLTlnLTDGRQVRFTTSCGIA 527
Cdd:PRK11359  430 LLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPI--MIDDKPFPLTLSIGIS 498
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
436-559 1.17e-11

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 67.40  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 436 IDIDNFKQLNDSYGHDVGDQALVAFGHLLQRAFRASDIFCRYGGEEFAVLLGNCSLDN----ARDIMEQLRTrTHRLTLn 511
Cdd:PRK10060  272 LDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAAleamASRILTRLRL-PFRIGL- 349

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1699383857 512 ltdgrqVRFTTSC--GIA--PVNAfTALQAAIKQADEALYFCKKNGKDRVSV 559
Cdd:PRK10060  350 ------IEVYTGCsiGIAlaPEHG-DDSESLIRSADTAMYTAKEGGRGQFCV 394
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 435-552 1.42e-10

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 59.29  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 435 LIDIDNFKQLNDSYGHDVGDQAL----VAFGHLLQRAfraSDIFCRYGGEEFAVLLGNCSLDNARDIMEQLrtRTHRLTL 510
Cdd:cd07556     6 FADIVGFTSLADALGPDEGDELLnelaGRFDSLIRRS---GDLKIKTIGDEFMVVSGLDHPAAAVAFAEDM--REAVSAL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1699383857 511 NLTDGRQVRFttSCGIA--PVNA--------FTALQAAIKQADEALYFCKKN 552
Cdd:cd07556    81 NQSEGNPVRV--RIGIHtgPVVVgvigsrpqYDVWGALVNLASRMESQAKAG 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 472-547 3.94e-10

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 59.15  E-value: 3.94e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699383857 472 DIFCRYGGEEFAVLLGNCSLDNARDIMEQLRTRTHRLtlnltdgRQVRFTTSCGIAPVNaftalqaAIKQADeALY 547
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL-------PSLRVTVSIGVAGDS-------LLKRAD-ALY 176
PRK09966 PRK09966
diguanylate cyclase DgcN;
302-556 5.46e-09

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 58.48  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 302 HKIYDSQTTIYGMIALAGLVVLLfilpalvfctnINRWLtktHNNIVRLSRGEMNID---RNDAFYSRELIaiSDAIQQL 378
Cdd:PRK09966  153 HFIWFSLAVLTGCILLASGIAIT-----------LTRHL---HNGLVEALKNITDVVhdvRSNRNFSRRVS--EERIAEF 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 379 RQYQLDKVSLESEK---QLLIK----ELEASSFLDPLTNIYNRRKFfLEC--QLLGDSS--YPQAFCLIDIDNFKQLNDS 447
Cdd:PRK09966  217 HRFALDFNSLLDEMeewQLRLQaknaQLLRTALHDPLTGLANRAAF-RSGinTLMNNSDarKTSALLFLDGDNFKYINDT 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 448 YGHDVGDQALV-------AFGHLLQRAFrasdifcRYGGEEFA-VLLGNCSLDNARDIMEQLrTRTHRLTLNLTDGRQVR 519
Cdd:PRK09966  296 WGHATGDRVLIeiakrlaEFGGLRHKAY-------RLGGDEFAmVLYDVQSESEVQQICSAL-TQIFNLPFDLHNGHQTT 367

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1699383857 520 FTTSCGIAPVNAFTALQAAIKQADEALYFCKKNGKDR 556
Cdd:PRK09966  368 MTLSIGYAMTIEHASAEKLQELADHNMYQAKHQRAEK 404
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 404-501 3.96e-06

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 49.86  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699383857 404 FLDPLTNIYNRRkFF---LECQLL--GDSSYPQAFCLIDIDNFKQLNDSYGHDVGDQALVAFGHLL----QRafRASDIF 474
Cdd:PRK11059  229 FQDAKTGLGNRL-FFdnqLATLLEdqEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLstfvMR--YPGALL 305

                          90       100
                  ....*....|....*....|....*..
gi 1699383857 475 CRYGGEEFAVLLGNCSLDNARDIMEQL 501
Cdd:PRK11059  306 ARYSRSDFAVLLPHRSLKEADSLASQL 332
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH