NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1770949870|ref|WP_152626058|]
View 

MULTISPECIES: diguanylate cyclase domain-containing protein [Acidithrix]

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 ...
 97-238 3.84e-18

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: 81.56  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:COG2199   116 HDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLdhfkrindtyghAAGDEV----------LKEVARRLRASLRE 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQ--VAQIK---AGSTIVHKISAGVAGYPTNGAAPQELFGRSTLALEHA 238
Cdd:COG2199   186 SDLVARLGGDEFAVLLPGTDLEEAEALAERLReaLEQLPfelEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRA 264
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 97-238 3.84e-18

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: 81.56  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:COG2199   116 HDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLdhfkrindtyghAAGDEV----------LKEVARRLRASLRE 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQ--VAQIK---AGSTIVHKISAGVAGYPTNGAAPQELFGRSTLALEHA 238
Cdd:COG2199   186 SDLVARLGGDEFAVLLPGTDLEEAEALAERLReaLEQLPfelEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRA 264
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 97-238 4.36e-17

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: 76.06  E-value: 4.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIdhfkqindtyghAAGDEV----------LKEVAERLRSSLRE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQvAQIKAGSTIVHK-----ISAGVAGYPTNGAAPQELFGRSTLALEHA 238
Cdd:cd01949    72 SDLVARLGGDEFAILLPGTDLEEAEALAERLR-EAIEEPFFIDGQeirvtASIGIATYPEDGEDAEELLRRADEALYRA 149
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 97-241 5.91e-15

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 70.35  E-value: 5.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870   97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQLSFIDQVT-----PSNEEIassIISFASLLRLTLREADVVARI 171
Cdd:smart00267   5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINdtyghAVGDEL---LQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770949870  172 GDYRFGLILEDTDEEGSAWVAER----VQVAQIKAGSTIVHKISAGVAGYPTNGAAPQELFGRSTLALEHALAA 241
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERilqqLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 97-241 2.37e-11

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: 60.34  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLdnfkrindtyghSVGDEV----------LQEVAQRLSSSLRR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQVAQIKAGSTIVHK-------ISAGVAGYPTNGAAPQELFGRSTLALEH 237
Cdd:pfam00990  73 SDLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSglplyvtISIGIAAYPNDGEDPEDLLKRADTALYQ 152


                  ....
gi 1770949870 238 ALAA 241
Cdd:pfam00990 153 AKQA 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 97-244 4.43e-11

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: 59.66  E-value: 4.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQLSFIDQV--TPSNEEIASSIISFASLLRLTLREADVVARIGDY 174
Cdd:TIGR00254   4 RDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKIndTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770949870 175 RFGLILEDTDEEGSAWVAERVQ-VAQIK----AGSTIVH-KISAGVAGYPTNGAAPQELFGRSTLALEHALAASNE 244
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRdAINSKpievAGSETLTvTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
pleD PRK09581
response regulator PleD; Reviewed
 154-238 8.61e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 49.51  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870 154 FASLLRLTLREADVVARIGDYRFGLILEDTDEEGSAWVAERVQVA------QIKAGSTIVHK-ISAGVAGYPTNGAAPQE 226
Cdd:PRK09581  353 FAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKiaeepfIISDGKERLNVtVSIGVAELRPSGDTIEA 432

                          90
                  ....*....|..
gi 1770949870 227 LFGRSTLALEHA 238
Cdd:PRK09581  433 LIKRADKALYEA 444
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 97-238 3.84e-18

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: 81.56  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:COG2199   116 HDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLdhfkrindtyghAAGDEV----------LKEVARRLRASLRE 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQ--VAQIK---AGSTIVHKISAGVAGYPTNGAAPQELFGRSTLALEHA 238
Cdd:COG2199   186 SDLVARLGGDEFAVLLPGTDLEEAEALAERLReaLEQLPfelEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRA 264
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 97-238 4.36e-17

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: 76.06  E-value: 4.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIdhfkqindtyghAAGDEV----------LKEVAERLRSSLRE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQvAQIKAGSTIVHK-----ISAGVAGYPTNGAAPQELFGRSTLALEHA 238
Cdd:cd01949    72 SDLVARLGGDEFAILLPGTDLEEAEALAERLR-EAIEEPFFIDGQeirvtASIGIATYPEDGEDAEELLRRADEALYRA 149
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 97-241 5.91e-15

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 70.35  E-value: 5.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870   97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQLSFIDQVT-----PSNEEIassIISFASLLRLTLREADVVARI 171
Cdd:smart00267   5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINdtyghAVGDEL---LQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770949870  172 GDYRFGLILEDTDEEGSAWVAER----VQVAQIKAGSTIVHKISAGVAGYPTNGAAPQELFGRSTLALEHALAA 241
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERilqqLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 97-241 2.37e-11

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: 60.34  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQL------------SFIDQVtpsneeiassIISFASLLRLTLRE 164
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLdnfkrindtyghSVGDEV----------LQEVAQRLSSSLRR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870 165 ADVVARIGDYRFGLILEDTDEEGSAWVAERVQVAQIKAGSTIVHK-------ISAGVAGYPTNGAAPQELFGRSTLALEH 237
Cdd:pfam00990  73 SDLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSglplyvtISIGIAAYPNDGEDPEDLLKRADTALYQ 152


                  ....
gi 1770949870 238 ALAA 241
Cdd:pfam00990 153 AKQA 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 97-244 4.43e-11

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: 59.66  E-value: 4.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQLSFIDQV--TPSNEEIASSIISFASLLRLTLREADVVARIGDY 174
Cdd:TIGR00254   4 RDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKIndTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770949870 175 RFGLILEDTDEEGSAWVAERVQ-VAQIK----AGSTIVH-KISAGVAGYPTNGAAPQELFGRSTLALEHALAASNE 244
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRdAINSKpievAGSETLTvTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
pleD PRK09581
response regulator PleD; Reviewed
 154-238 8.61e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 49.51  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870 154 FASLLRLTLREADVVARIGDYRFGLILEDTDEEGSAWVAERVQVA------QIKAGSTIVHK-ISAGVAGYPTNGAAPQE 226
Cdd:PRK09581  353 FAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKiaeepfIISDGKERLNVtVSIGVAELRPSGDTIEA 432

                          90
                  ....*....|..
gi 1770949870 227 LFGRSTLALEHA 238
Cdd:PRK09581  433 LIKRADKALYEA 444
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
97-222 1.43e-06

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 48.86  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870  97 TDPETGLSTFPVFKAILEAKVATARRRLWPVTVVQIQLSFIDQVT-----PSNEEIASSIisfASLLRLTLREADVVARI 171
Cdd:PRK15426  400 HDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINdrfghQAGDRVLSHA---AGLISSSLRAQDVAGRV 476

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1770949870 172 GDYRFGLILEDTDEEGSAWVAERVQVA------QIKAGSTIVHKISAGVAGYPTNGA 222
Cdd:PRK15426  477 GGEEFCVVLPGASLAEAAQVAERIRLRinekeiLVAKSTTIRISASLGVSSAEEDGD 533
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 166-216 1.21e-05

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: 44.51  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1770949870 166 DVVARIGDYRFGLILEDTDEEGSAWVAERVQVAqIKAGSTIVHKISAGVAG 216
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREA-VAELPSLRVTVSIGVAG 165
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 150-241 3.43e-03

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 38.27  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770949870 150 SIISFASLLRLTLREADVVARIGDYRFGLILEDTDEEGS----AWVAERVQVAQIKAGSTIVHKISAGVAGYPTNGAAPQ 225
Cdd:PRK10245  262 AIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAitamSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYR 341

                          90
                  ....*....|....*.
gi 1770949870 226 ELFGRSTLALEHALAA 241
Cdd:PRK10245  342 EWLKSADLALYKAKNA 357
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 155-200 6.97e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 37.73  E-value: 6.97e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1770949870  155 ASLLRLTLREADVVARIGDYRFGLILEDTDEEGSAWVAERVqVAQI 200
Cdd:PRK09776   727 ASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI-ISAI 771
 
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