NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15598454|ref|NP_251948|]
View 

hypothetical protein PA3258 [Pseudomonas aeruginosa PAO1]

Protein Classification

bifunctional diguanylate cyclase/phosphodiesterase( domain architecture ID 10112657)

bifunctional diguanylate cyclase/phosphodiesterase (GGDEF/EAL) catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules through its GGDEF domain and linearizes cyclic-di-GMP through its EAL domain; the balance between the two activities determines the cellular level of cyclic di-3',5'-guanylate; contains a a CBS pair domain

CATH:  3.30.70.1230
EC:  2.7.7.65|3.1.4.52
Gene Ontology:  GO:0046872|GO:0052621|GO:0071111
PubMed:  24161944|11119645|15995192|20691189
SCOP:  4001316

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 27-259 2.21e-71

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: 229.74  E-value: 2.21e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  27 SALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNS-PLHSPLALFAVARQCGRLSELELLCRQRA---FSRFRDI 102
Cdd:cd01948   1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEAcrqLARWQAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 103 QGDAMLFLNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSS 182
Cdd:cd01948  81 GPDLRLSVNLSARQLRDPDFLD-RLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598454 183 LRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 290-410 1.03e-38

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


The actual alignment was detected with superfamily member cd04598:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 121  Bit Score: 138.33  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 290 LLLEQRAVDVRTSTQEVVEIFRRQANLNSLAILDEeGRPIGIVHRHALTDALLRPFACDLFLRKPISRLMSDDFLAVELG 369
Cdd:cd04598   1 LLEEAPPVSPDTTNDEVYELFEENPDLHALPVVDN-GRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMDKDPLVVDAD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598454 370 QTLQQVSRLLTSRARQRIEEDFIVTRGGHYAGMGRVIDVLR 410
Cdd:cd04598  80 TPIEELSQLATSRDQRYLYDGFIITENGRYLGVGTGRDLLR 120
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 425-589 8.79e-23

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: 94.93  E-value: 8.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 425 PLTLLPGNVPIQQCLERLLQQRREA----VICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDPgSDFVGHIGGDD 500
Cdd:cd01949   4 PLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRE-SDLVARLGGDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 501 FMLVLgPEDWRTRIDRLLETFqsqcrrfysREHLEAGCFVAHNRHGqreeyplLSLSVGVVHLPAeacQGMDAAHLATLA 580
Cdd:cd01949  83 FAILL-PGTDLEEAEALAERL---------REAIEEPFFIDGQEIR-------VTASIGIATYPE---DGEDAEELLRRA 142


                ....*....
gi 15598454 581 SEAKRQAKA 589
Cdd:cd01949 143 DEALYRAKR 151
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 27-259 2.21e-71

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: 229.74  E-value: 2.21e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  27 SALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNS-PLHSPLALFAVARQCGRLSELELLCRQRA---FSRFRDI 102
Cdd:cd01948   1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEAcrqLARWQAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 103 QGDAMLFLNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSS 182
Cdd:cd01948  81 GPDLRLSVNLSARQLRDPDFLD-RLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598454 183 LRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 12-270 1.67e-66

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: 227.36  E-value: 1.67e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  12 FSLRRERSMTVTEQLSALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNSP-LHSPLALFAVARQCGRLSELELL 90
Cdd:COG2200 316 FAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGgLISPAEFIPAAERSGLIVELDRW 395

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  91 CRQRAFSRFRDIQG---DAMLFLNISPESLLEAGHPpGRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSM 167
Cdd:COG2200 396 VLERALRQLARWPErglDLRLSVNLSARSLLDPDFL-ERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRAL 474

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 168 GFSIALDDLGAGYSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGV 247
Cdd:COG2200 475 GVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGC 554

                       250       260
                ....*....|....*....|...
gi 15598454 248 DLVQGYLFGRPQehPASDVQQML 270
Cdd:COG2200 555 DYAQGYLFGRPL--PLEELEALL 575
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 28-258 1.51e-58

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: 195.61  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    28 ALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNS-PLHSPLALFAVARQCGRLSELELLCRQRAFSRFRDIQ--G 104
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDgGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQlgP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   105 DAMLFLNISPESLLEAGHPpGRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLR 184
Cdd:pfam00563  83 DIKLSINLSPASLADPGFL-ELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598454   185 LWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRP 258
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 32-259 1.57e-56

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 190.51  E-value: 1.57e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454     32 ILAHGDLHCLFQPILSLSERRLVGYEALTR--GPSNSPLhSPLALFAVARQCGRLSELELLCRQRAFSRFRDIQGDA--- 106
Cdd:smart00052   7 ALENGQFLLYYQPIVSLRTGRLVGVEALIRwqHPEGGII-SPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGppp 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    107 -MLFLNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLRL 185
Cdd:smart00052  86 lLISINLSARQLISPDLVP-RVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSY 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598454    186 WSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:smart00052 165 LKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 290-410 1.03e-38

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341373 [Multi-domain]  Cd Length: 121  Bit Score: 138.33  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 290 LLLEQRAVDVRTSTQEVVEIFRRQANLNSLAILDEeGRPIGIVHRHALTDALLRPFACDLFLRKPISRLMSDDFLAVELG 369
Cdd:cd04598   1 LLEEAPPVSPDTTNDEVYELFEENPDLHALPVVDN-GRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMDKDPLVVDAD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598454 370 QTLQQVSRLLTSRARQRIEEDFIVTRGGHYAGMGRVIDVLR 410
Cdd:cd04598  80 TPIEELSQLATSRDQRYLYDGFIITENGRYLGVGTGRDLLR 120
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
129-270 6.37e-27

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 115.93  E-value: 6.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  129 QLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLRLWSELRPDYVKIDRHFVDGIHLDT 208
Cdd:PRK10060 515 QALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQP 594

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598454  209 VKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQehPASDVQQML 270
Cdd:PRK10060 595 VSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPM--PAVAFERWY 654
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 425-589 8.79e-23

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: 94.93  E-value: 8.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 425 PLTLLPGNVPIQQCLERLLQQRREA----VICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDPgSDFVGHIGGDD 500
Cdd:cd01949   4 PLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRE-SDLVARLGGDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 501 FMLVLgPEDWRTRIDRLLETFqsqcrrfysREHLEAGCFVAHNRHGqreeyplLSLSVGVVHLPAeacQGMDAAHLATLA 580
Cdd:cd01949  83 FAILL-PGTDLEEAEALAERL---------REAIEEPFFIDGQEIR-------VTASIGIATYPE---DGEDAEELLRRA 142


                ....*....
gi 15598454 581 SEAKRQAKA 589
Cdd:cd01949 143 DEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 336-589 2.18e-22

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: 97.36  E-value: 2.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 336 ALTDALLRPFACDLFLRKPISRLMSDDFLAVELGQTLQQVSRLLTSRARQRIEEDFIVTRGGHYAGMGRVIDVLRLIT-E 414
Cdd:COG2199  28 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRlE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 415 EKLQQARHANPLTLLPGNVPIQQCLERLLQ----QRREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIdPGS 490
Cdd:COG2199 108 ERLRRLATHDPLTGLPNRRAFEERLERELArarrEGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASL-RES 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 491 DFVGHIGGDDFMLVL---GPEDWRTRIDRLletfqsqcrrfysREHLEAGCFVAHNRHGQreeyplLSLSVGVVHLPAEa 567
Cdd:COG2199 187 DLVARLGGDEFAVLLpgtDLEEAEALAERL-------------REALEQLPFELEGKELR------VTVSIGVALYPED- 246

                       250       260
                ....*....|....*....|..
gi 15598454 568 cqGMDAAHLATLASEAKRQAKA 589
Cdd:COG2199 247 --GDSAEELLRRADLALYRAKR 266
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 418-589 9.65e-16

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 74.98  E-value: 9.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    418 QQARHaNPLTLLPG----NVPIQQCLERLLQQRREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIdPGSDFV 493
Cdd:smart00267   1 RLAFR-DPLTGLPNrryfEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCL-RPGDLL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    494 GHIGGDDFMLVLgPEDWRTRIDRLLETFQSQCRRFysrehleagcFVAHNRHGQreeyplLSLSVGVVHLPAEacqGMDA 573
Cdd:smart00267  79 ARLGGDEFALLL-PETSLEEAIALAERILQQLREP----------IIIHGIPLY------LTISIGVAAYPNP---GEDA 138

                          170
                   ....*....|....*.
gi 15598454    574 AHLATLASEAKRQAKA 589
Cdd:smart00267 139 EDLLKRADTALYQAKK 154
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 404-504 2.56e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 66.72  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  404 RVIDV------LRLITEEKLQQARHA---NPLTLLPGNVPIQQCLERLLQQRREAVICYIDVDSFKPFNDLYGYARGDEV 474
Cdd:PRK11359 350 RVADIsqhlaaLALEQEKSRQHIEQLiqfDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQA 429

                         90       100       110
                 ....*....|....*....|....*....|
gi 15598454  475 LLCLAQCLSERIDPGsDFVGHIGGDDFMLV 504
Cdd:PRK11359 430 LLEVVNRFREKLKPD-QYLCRIEGTQFVLV 458
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 425-589 6.37e-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: 61.11  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   425 PLTLLPGNVPIQQCLERLLQ-----QRREAVIcYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIdPGSDFVGHIGGD 499
Cdd:pfam00990   5 PLTGLPNRRYFEEQLEQELQralreGSPVAVL-LIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSL-RRSDLVARLGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   500 DFMLVL---GPEDWRT---RIDRLLETFQsqcrrfysrehleagcfvAHNRHGQREEYplLSLSVGVVHLPAEacqGMDA 573
Cdd:pfam00990  83 EFAILLpetSLEGAQElaeRIRRLLAKLK------------------IPHTVSGLPLY--VTISIGIAAYPND---GEDP 139

                         170
                  ....*....|....*.
gi 15598454   574 AHLATLASEAKRQAKA 589
Cdd:pfam00990 140 EDLLKRADTALYQAKQ 155
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 419-589 2.29e-10

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: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   419 QARHaNPLTLLPGNVPIQQCLERLLQQ----RREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDpGSDFVG 494
Cdd:TIGR00254   1 QAVR-DPLTGLYNRRYLEEMLDSELKRarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVR-GSDVVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   495 HIGGDDFMLVLgpedwrtrIDRLLETFQSQCRRFysREHLEAGCFVAHNRhgqreEYPLLSLSVGVVHLPAeacQGMDAA 574
Cdd:TIGR00254  79 RYGGEEFVVIL--------PGTPLEDALSKAERL--RDAINSKPIEVAGS-----ETLTVTVSIGVACYPG---HGLTLE 140

                         170
                  ....*....|....*
gi 15598454   575 HLATLASEAKRQAKA 589
Cdd:TIGR00254 141 ELLKRADEALYQAKK 155
CBS COG0517
CBS domain [Signal transduction mechanisms];
301-415 4.04e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 57.95  E-value: 4.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 301 TSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLRPFACdlFLRKPISRLMSDDFLAVELGQTLQQVSRLLT 380
Cdd:COG0517  18 ATVREALELMSEK-RIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKD--LLDTPVSEVMTRPPVTVSPDTSLEEAAELME 94

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598454 381 SRarqRIEEDFIVTRGGHYAGMGRVIDVLRLITEE 415
Cdd:COG0517  95 EH---KIRRLPVVDDDGRLVGIITIKDLLKALLEP 126
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 297-343 6.22e-05

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.04  E-value: 6.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15598454   297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLR 343
Cdd:pfam00571  12 VSPDTTLEEALELMREH-GISRLPVVDEDGKLVGIVTLKDLLRALLG 57
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 27-259 2.21e-71

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: 229.74  E-value: 2.21e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  27 SALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNS-PLHSPLALFAVARQCGRLSELELLCRQRA---FSRFRDI 102
Cdd:cd01948   1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEAcrqLARWQAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 103 QGDAMLFLNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSS 182
Cdd:cd01948  81 GPDLRLSVNLSARQLRDPDFLD-RLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598454 183 LRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 12-270 1.67e-66

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: 227.36  E-value: 1.67e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  12 FSLRRERSMTVTEQLSALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNSP-LHSPLALFAVARQCGRLSELELL 90
Cdd:COG2200 316 FAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGgLISPAEFIPAAERSGLIVELDRW 395

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  91 CRQRAFSRFRDIQG---DAMLFLNISPESLLEAGHPpGRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSM 167
Cdd:COG2200 396 VLERALRQLARWPErglDLRLSVNLSARSLLDPDFL-ERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRAL 474

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 168 GFSIALDDLGAGYSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGV 247
Cdd:COG2200 475 GVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGC 554

                       250       260
                ....*....|....*....|...
gi 15598454 248 DLVQGYLFGRPQehPASDVQQML 270
Cdd:COG2200 555 DYAQGYLFGRPL--PLEELEALL 575
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 28-258 1.51e-58

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: 195.61  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    28 ALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNS-PLHSPLALFAVARQCGRLSELELLCRQRAFSRFRDIQ--G 104
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDgGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQlgP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   105 DAMLFLNISPESLLEAGHPpGRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLR 184
Cdd:pfam00563  83 DIKLSINLSPASLADPGFL-ELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598454   185 LWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRP 258
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 32-259 1.57e-56

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 190.51  E-value: 1.57e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454     32 ILAHGDLHCLFQPILSLSERRLVGYEALTR--GPSNSPLhSPLALFAVARQCGRLSELELLCRQRAFSRFRDIQGDA--- 106
Cdd:smart00052   7 ALENGQFLLYYQPIVSLRTGRLVGVEALIRwqHPEGGII-SPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGppp 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    107 -MLFLNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLRL 185
Cdd:smart00052  86 lLISINLSARQLISPDLVP-RVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSY 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598454    186 WSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:smart00052 165 LKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 33-270 3.67e-46

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: 173.04  E-value: 3.67e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  33 LAHGDLHCLFQPILSLSERRLVGYEAL------TRGpsnspLHSPLALFAVARQCGRLSE-----LELLCRQraFSRFRD 101
Cdd:COG5001 434 LERGELELHYQPQVDLATGRIVGAEALlrwqhpERG-----LVSPAEFIPLAEETGLIVPlgewvLREACRQ--LAAWQD 506

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 102 iQGDAMLFL--NISPESLLEAGHPpGRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAG 179
Cdd:COG5001 507 -AGLPDLRVavNLSARQLRDPDLV-DRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTG 584

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 180 YSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:COG5001 585 YSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPL 664

                       250
                ....*....|.
gi 15598454 260 ehPASDVQQML 270
Cdd:COG5001 665 --PAEELEALL 673
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 14-277 4.56e-42

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: 158.93  E-value: 4.56e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  14 LRRERSMtvteqLSALDSILAHGDLHCLFQPILSLSERRLVGYEALTR--GPSNSPLhSPLALFAVARQCGRLSELELLC 91
Cdd:COG4943 266 LRRRLSP-----RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRwrDPDGSVI-SPDIFIPLAEQSGLISPLTRQV 339

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  92 RQRAFSRFRDI-QGDAMLFL--NISPeSLLEAGHPPGRTLQLLQQLGISPNRVVIELTEQTPIDDfDLLDTALHHYRSMG 168
Cdd:COG4943 340 IEQVFRDLGDLlAADPDFHIsiNLSA-SDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDP-AKARAVIAALREAG 417

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 169 FSIALDDLGAGYSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVD 248
Cdd:COG4943 418 HRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQ 497

                       250       260       270
                ....*....|....*....|....*....|...
gi 15598454 249 LVQGYLFGRPQehPASD----VQQMLPSADAPS 277
Cdd:COG4943 498 YGQGWLFAKPL--PAEEfiawLAAQRAPASAPA 528
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 290-410 1.03e-38

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341373 [Multi-domain]  Cd Length: 121  Bit Score: 138.33  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 290 LLLEQRAVDVRTSTQEVVEIFRRQANLNSLAILDEeGRPIGIVHRHALTDALLRPFACDLFLRKPISRLMSDDFLAVELG 369
Cdd:cd04598   1 LLEEAPPVSPDTTNDEVYELFEENPDLHALPVVDN-GRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMDKDPLVVDAD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598454 370 QTLQQVSRLLTSRARQRIEEDFIVTRGGHYAGMGRVIDVLR 410
Cdd:cd04598  80 TPIEELSQLATSRDQRYLYDGFIITENGRYLGVGTGRDLLR 120
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
129-270 6.37e-27

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 115.93  E-value: 6.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  129 QLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLRLWSELRPDYVKIDRHFVDGIHLDT 208
Cdd:PRK10060 515 QALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQP 594

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598454  209 VKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQehPASDVQQML 270
Cdd:PRK10060 595 VSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPM--PAVAFERWY 654
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 43-258 1.24e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 111.73  E-value: 1.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   43 QPILSLSERRLVGYEALTR--GPSNSpLHSPLALFAVARQCGRLSE-----LELLCRQRAFSRFRDIqgDAMLFLNISPE 115
Cdd:PRK13561 419 QPQVEMRSGKLVSAEALLRmqQPDGS-WDLPEGLIDRIESCGLMVTvghwvLEESCRLLAAWQERGI--MLPLSVNLSAL 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  116 SLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLRLWSELRP---D 192
Cdd:PRK13561 496 QLMHPNMVA-DMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSlpiD 574

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598454  193 YVKIDRHFVDGIHLDTvkrEFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRP 258
Cdd:PRK13561 575 VLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 43-259 1.08e-23

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 103.73  E-value: 1.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  43 QPILSlSERRLVGYEALTRGPSNSPLHSPLALFAVARqcgrlseleLLCRqrAFSRF--RDIQGDAMLFLNISPESLLea 120
Cdd:COG3434   9 QPILD-RDQRVVGYELLFRSGLENSAPDVDGDQATAR---------VLLN--AFLEIglDRLLGGKLAFINFTEELLL-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 121 ghppGRTLQLLqqlgiSPNRVVIELTEQTPIDDfDLLDtALHHYRSMGFSIALDDlgagYSSLRLWSELRP--DYVKIDr 198
Cdd:COG3434  75 ----SDLPELL-----PPERVVLEILEDVEPDE-ELLE-ALKELKEKGYRIALDD----FVLDPEWDPLLPlaDIIKID- 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598454 199 hfVDGIHLDTVKRefvgsILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:COG3434 139 --VLALDLEELAE-----LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPE 192
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 425-589 8.79e-23

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: 94.93  E-value: 8.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 425 PLTLLPGNVPIQQCLERLLQQRREA----VICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDPgSDFVGHIGGDD 500
Cdd:cd01949   4 PLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRE-SDLVARLGGDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 501 FMLVLgPEDWRTRIDRLLETFqsqcrrfysREHLEAGCFVAHNRHGqreeyplLSLSVGVVHLPAeacQGMDAAHLATLA 580
Cdd:cd01949  83 FAILL-PGTDLEEAEALAERL---------REAIEEPFFIDGQEIR-------VTASIGIATYPE---DGEDAEELLRRA 142


                ....*....
gi 15598454 581 SEAKRQAKA 589
Cdd:cd01949 143 DEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 336-589 2.18e-22

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: 97.36  E-value: 2.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 336 ALTDALLRPFACDLFLRKPISRLMSDDFLAVELGQTLQQVSRLLTSRARQRIEEDFIVTRGGHYAGMGRVIDVLRLIT-E 414
Cdd:COG2199  28 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRlE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 415 EKLQQARHANPLTLLPGNVPIQQCLERLLQ----QRREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIdPGS 490
Cdd:COG2199 108 ERLRRLATHDPLTGLPNRRAFEERLERELArarrEGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASL-RES 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 491 DFVGHIGGDDFMLVL---GPEDWRTRIDRLletfqsqcrrfysREHLEAGCFVAHNRHGQreeyplLSLSVGVVHLPAEa 567
Cdd:COG2199 187 DLVARLGGDEFAVLLpgtDLEEAEALAERL-------------REALEQLPFELEGKELR------VTVSIGVALYPED- 246

                       250       260
                ....*....|....*....|..
gi 15598454 568 cqGMDAAHLATLASEAKRQAKA 589
Cdd:COG2199 247 --GDSAEELLRRADLALYRAKR 266
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 28-273 4.32e-22

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 101.00  E-value: 4.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   28 ALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGpsNSPLH---SPLALFAVARQCGRLSELEL-----LCRQRAFSRF 99
Cdd:PRK11359 547 ALKEAISNNQLKLVYQPQIFAETGELYGIEALARW--HDPLHghvPPSRFIPLAEEIGEIENIGRwviaeACRQLAEWRS 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  100 RDIQGDAmLFLNISPESLlEAGHPPGRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAG 179
Cdd:PRK11359 625 QNIHIPA-LSVNLSALHF-RSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTG 702

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  180 YSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:PRK11359 703 FSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782

                        250
                 ....*....|....
gi 15598454  260 ehPASDVQQMLPSA 273
Cdd:PRK11359 783 --PAEEIPGWMSSV 794
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
35-258 8.08e-22

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 99.30  E-value: 8.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   35 HGDLHCLFQPILSLSERRLVGYEALTR--GPSNSPLhSPLALFAVARQCGRLSEL-----ELLCRQRAfsRFRDI--QGd 105
Cdd:PRK10551 274 RGQFYVEYQPVVDTQTLRVTGLEALLRwrHPTAGEI-PPDAFINYAEAQKLIVPLtqhlfELIARDAA--ELQKVlpVG- 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  106 AMLFLNISPESLleagHPPG---RTLQLLQQLGISPNRVVIELTEQTPIDD------FDLLdtalhhyRSMGFSIALDDL 176
Cdd:PRK10551 350 AKLGINISPAHL----HSDSfkaDVQRLLASLPADHFQIVLEITERDMVQEeeatklFAWL-------HSQGIEIAIDDF 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  177 GAGYSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFG 256
Cdd:PRK10551 419 GTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWIS 498


                 ..
gi 15598454  257 RP 258
Cdd:PRK10551 499 RP 500
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 17-273 8.73e-21

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 96.55  E-value: 8.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   17 ERSMTVTEQLSALDSILAHGDLHCLFQPILSLSERRLVGYEALTRGPSNSPLHS-PLALFAVARQCGRLSELELLCRQRA 95
Cdd:PRK11829 398 EKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVlPSGFVHFAEEEGMMVPLGNWVLEEA 477

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   96 FSRFRDIQGDAM---LFLNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIA 172
Cdd:PRK11829 478 CRILADWKARGVslpLSVNISGLQVQNKQFLP-HLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIA 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  173 LDDLGAGYSSLRLWSELRP---DYVKIDRHFVDGIHLDTVKREFVGSIlkmARASRAQVIAEGIELPEELAVLSEMGVDL 249
Cdd:PRK11829 557 LDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQC 633

                        250       260
                 ....*....|....*....|....
gi 15598454  250 VQGYLFGRPQehPASDVQQMLPSA 273
Cdd:PRK11829 634 GQGFLFSPPL--PRAEFEAQYFSS 655
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 110-259 6.44e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 88.19  E-value: 6.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   110 LNISPESLLEAGHPPgRTLQLLQQLGISPNRVVIELTEQTPIDDFDLLDTALHHYRSMGFSIALDDLGAGYSSLRLWSEL 189
Cdd:PRK09776  930 LPLSVAGLSSPTLLP-FLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAF 1008

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   190 RPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:PRK09776 1009 MADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 221-522 3.23e-17

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: 85.21  E-value: 3.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 221 ARASRAQVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQEHPASDVQQMLPSADAPSQSSSDEHGDLRALLLEQRAVDVR 300
Cdd:COG5001  46 LLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALA 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 301 TSTQEVVEIFRRQANLNSLAILDEEGRPIGIVHRHALTDALLRPFACDLFLRKPISRLMSDDFLAVELGQTLQQVSRLLT 380
Cdd:COG5001 126 ALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRL 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 381 SRARQRIEEDFIVTRGGHYAGMGRVIDVLRLITEEKLQQAR---HAN--PLTLLPGNVPIQQCLERLLQQRRE----AVI 451
Cdd:COG5001 206 LRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERlrhLAYhdPLTGLPNRRLFLDRLEQALARARRsgrrLAL 285

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598454 452 CYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDPGsDFVGHIGGDDFMLVL----GPEDWRTRIDRLLETFQ 522
Cdd:COG5001 286 LFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREG-DTVARLGGDEFAVLLpdldDPEDAEAVAERILAALA 359
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 418-589 9.65e-16

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 74.98  E-value: 9.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    418 QQARHaNPLTLLPG----NVPIQQCLERLLQQRREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIdPGSDFV 493
Cdd:smart00267   1 RLAFR-DPLTGLPNrryfEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCL-RPGDLL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454    494 GHIGGDDFMLVLgPEDWRTRIDRLLETFQSQCRRFysrehleagcFVAHNRHGQreeyplLSLSVGVVHLPAEacqGMDA 573
Cdd:smart00267  79 ARLGGDEFALLL-PETSLEEAIALAERILQQLREP----------IIIHGIPLY------LTISIGVAAYPNP---GEDA 138

                          170
                   ....*....|....*.
gi 15598454    574 AHLATLASEAKRQAKA 589
Cdd:smart00267 139 EDLLKRADTALYQAKK 154
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 404-504 2.56e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 66.72  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  404 RVIDV------LRLITEEKLQQARHA---NPLTLLPGNVPIQQCLERLLQQRREAVICYIDVDSFKPFNDLYGYARGDEV 474
Cdd:PRK11359 350 RVADIsqhlaaLALEQEKSRQHIEQLiqfDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQA 429

                         90       100       110
                 ....*....|....*....|....*....|
gi 15598454  475 LLCLAQCLSERIDPGsDFVGHIGGDDFMLV 504
Cdd:PRK11359 430 LLEVVNRFREKLKPD-QYLCRIEGTQFVLV 458
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 425-589 6.37e-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: 61.11  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   425 PLTLLPGNVPIQQCLERLLQ-----QRREAVIcYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIdPGSDFVGHIGGD 499
Cdd:pfam00990   5 PLTGLPNRRYFEEQLEQELQralreGSPVAVL-LIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSL-RRSDLVARLGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   500 DFMLVL---GPEDWRT---RIDRLLETFQsqcrrfysrehleagcfvAHNRHGQREEYplLSLSVGVVHLPAEacqGMDA 573
Cdd:pfam00990  83 EFAILLpetSLEGAQElaeRIRRLLAKLK------------------IPHTVSGLPLY--VTISIGIAAYPND---GEDP 139

                         170
                  ....*....|....*.
gi 15598454   574 AHLATLASEAKRQAKA 589
Cdd:pfam00990 140 EDLLKRADTALYQAKQ 155
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 419-589 2.29e-10

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: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   419 QARHaNPLTLLPGNVPIQQCLERLLQQ----RREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDpGSDFVG 494
Cdd:TIGR00254   1 QAVR-DPLTGLYNRRYLEEMLDSELKRarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVR-GSDVVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   495 HIGGDDFMLVLgpedwrtrIDRLLETFQSQCRRFysREHLEAGCFVAHNRhgqreEYPLLSLSVGVVHLPAeacQGMDAA 574
Cdd:TIGR00254  79 RYGGEEFVVIL--------PGTPLEDALSKAERL--RDAINSKPIEVAGS-----ETLTVTVSIGVACYPG---HGLTLE 140

                         170
                  ....*....|....*
gi 15598454   575 HLATLASEAKRQAKA 589
Cdd:TIGR00254 141 ELLKRADEALYQAKK 155
CBS COG0517
CBS domain [Signal transduction mechanisms];
301-415 4.04e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 57.95  E-value: 4.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 301 TSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLRPFACdlFLRKPISRLMSDDFLAVELGQTLQQVSRLLT 380
Cdd:COG0517  18 ATVREALELMSEK-RIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKD--LLDTPVSEVMTRPPVTVSPDTSLEEAAELME 94

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598454 381 SRarqRIEEDFIVTRGGHYAGMGRVIDVLRLITEE 415
Cdd:COG0517  95 EH---KIRRLPVVDDDGRLVGIITIKDLLKALLEP 126
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 354-505 1.62e-09

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 60.84  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   354 PISRLMSDDFLAVELGQTLQQVSRL---------------LTSRARQRIEEDFIV-TRGG-----HYAGM------GRVI 406
Cdd:PRK09776  563 PVAEKMTGWTQEEALGVPLLTVLHItfgdngplmeniyscLTSRSAAYLEQDVVLhCRSGgsydvHYSITplstldGENI 642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   407 D---VLRLITEEKLQQ---ARHA--NPLTLLPGNVPIQQCLERLLQQRRE----AVICYIDVDSFKPFNDLYGYARGDEV 474
Cdd:PRK09776  643 GsvlVIQDVTESRKMLrqlSYSAshDALTHLANRASFEKQLRRLLQTVNSthqrHALVFIDLDRFKAVNDSAGHAAGDAL 722

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15598454   475 LLCLAQCLSERIDPgSDFVGHIGGDDFMLVL 505
Cdd:PRK09776  723 LRELASLMLSMLRS-SDVLARLGGDEFGLLL 752
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 77-260 6.05e-09

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 58.72  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   77 VARQCGRLSELELLCRQRAFSRFRDIQGDAmLFLNISPESLLeagHPP-GRTLQ--LLQQLGISPNRVVIELTEQTPIDD 153
Cdd:PRK11059 456 MVQQLGLSEQYDRQVIERVLPLLRYWPEEN-LSINLSVDSLL---SRAfQRWLRdtLLQCPRSQRKRLIFELAEADVCQH 531

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  154 FDLLDTALHHYRSMGFSIALDDLGAGYSSLRLWSELRPDYVKIDRHFVDGIHLDTVKREFVGSILKMARASRAQVIAEGI 233
Cdd:PRK11059 532 ISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGV 611

                        170       180
                 ....*....|....*....|....*..
gi 15598454  234 ELPEELAVLSEMGVDLVQGYLFGRPQE 260
Cdd:PRK11059 612 ESREEWQTLQELGVSGGQGDFFAESQP 638
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 297-415 1.06e-08

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 53.68  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRhalTDALLRPFACDL-FLRKPISRLMSDDFLAVELGQTLQQV 375
Cdd:COG2905  12 VSPDATVREAARLMTEK-GVGSLVVVDDDGRLVGIITD---RDLRRRVLAEGLdPLDTPVSEVMTRPPITVSPDDSLAEA 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598454 376 SRLLTSRARQRIeedfIVTRGGHYAGMGRVIDVLRLITEE 415
Cdd:COG2905  88 LELMEEHRIRHL----PVVDDGKLVGIVSITDLLRALSEE 123
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
301-415 1.68e-08

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 53.33  E-value: 1.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 301 TSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLRPFACDL---FLRKPISRLMSDDFLAVELGQTLQQVSR 377
Cdd:COG3448  19 TTLREALELMREH-GIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeerLLDLPVEDVMTRPVVTVTPDTPLEEAAE 97

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598454 378 LLTSRARQRIeedFIVTRGGHYAGMGRVIDVLRLITEE 415
Cdd:COG3448  98 LMLEHGIHRL---PVVDDDGRLVGIVTRTDLLRALARL 132
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 42-259 3.06e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 55.01  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454   42 FQPILSLSERrLVGYEALTR--GPSN-SPLHSPLALFAVARQCGRL----SELELLCRQRAFsrFrdIQGDAMLFLNISp 114
Cdd:PRK11596  34 FQPIYRTSGR-LMAIELLTAvtHPSNpSQRLSPERYFAEITVSHRLdvvkEQLDLLAQWADF--F--VRHGLLASVNID- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  115 eslleaghppGRTLQLLQQlgispNRVVIELTEQTPIDDFDLLDtalHHYRSMGFSIA---------LDDLGAG---YSS 182
Cdd:PRK11596 108 ----------GPTLIALRQ-----QPAILRLIERLPWLRFELVE---HIRLPKDSPFAsmcefgplwLDDFGTGmanFSA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598454  183 LrlwSELRPDYVKIDRHFVDGIHLDTVKREFVGSILK-MARASRAqVIAEGIELPEELAVLSEMGVDLVQGYLFGRPQ 259
Cdd:PRK11596 170 L---SEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHlMNRYCRG-VIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
412-521 1.43e-07

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 54.69  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  412 ITEEKLQQAR---HAN--PLTLLPGNVPIQQCLERLLQQR-REAV-ICYIDVDSFKPFNDLYGYARGDEVL----LCLAQ 480
Cdd:PRK10060 223 ITEERRAQERlriLANtdSITGLPNRNAIQELIDHAINAAdNNQVgIVYLDLDNFKKVNDAYGHMFGDQLLqdvsLAILS 302

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15598454  481 CLSEridpgSDFVGHIGGDDFmLVLGP-------EDWRTRI-DRLLETF 521
Cdd:PRK10060 303 CLEE-----DQTLARLGGDEF-LVLAShtsqaalEAMASRIlTRLRLPF 345
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 297-410 1.69e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 49.94  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLRPfacDLFLRKPISRLMSDDFLAVELGQTLQQVS 376
Cdd:cd02205   7 VDPDTTVREALELMAEN-GIGALPVVDDDGKLVGIVTERDILRALVEG---GLALDTPVAEVMTPDVITVSPDTDLEEAL 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598454 377 RLLTSRARQRIeedFIVTRGGHYAGMGRVIDVLR 410
Cdd:cd02205  83 ELMLEHGIRRL---PVVDDDGKLVGIVTRRDILR 113
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 440-505 5.33e-07

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 52.14  E-value: 5.33e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598454  440 ERLLQQRREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDpGSDFVGHIGGDDFMLVL 505
Cdd:PRK10245 228 DNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLR-GSDVIGRFGGDEFAVIM 292
PRK09966 PRK09966
diguanylate cyclase DgcN;
417-505 1.00e-06

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 51.55  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  417 LQQARHaNPLTLLPGNVPIQQCLERLLQQ---RREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERidPGSDFV 493
Cdd:PRK09966 245 LRTALH-DPLTGLANRAAFRSGINTLMNNsdaRKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEF--GGLRHK 321

                         90
                 ....*....|...
gi 15598454  494 GH-IGGDDFMLVL 505
Cdd:PRK09966 322 AYrLGGDEFAMVL 334
pleD PRK09581
response regulator PleD; Reviewed
 435-505 4.32e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 49.51  E-value: 4.32e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598454  435 IQQCLERLLQQRREAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDpGSDFVGHIGGDDFMLVL 505
Cdd:PRK09581 310 LKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIR-GTDLIARYGGEEFVVVM 379
PRK09894 PRK09894
diguanylate cyclase; Provisional
 385-505 1.33e-05

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 47.37  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  385 QRIEEDFIVTrgGHYAGMGRVIDVLRL----ITEEKLQQARHANPLTLLPGNVPIQQCLERLLQqRREAVICYI---DVD 457
Cdd:PRK09894  91 LAIVEGHWQD--AHFDAFQEGLLSFTAaltdYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLR-NREPQNLYLallDID 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15598454  458 SFKPFNDLYGYARGDEVLLCLAQCLSERIDPgSDFVGHIGGDDFMLVL 505
Cdd:PRK09894 168 RFKLVNDTYGHLIGDVVLRTLATYLASWTRD-YETVYRYGGEEFIICL 214
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 448-509 1.57e-05

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: 44.65  E-value: 1.57e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598454 448 EAVICYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSERIDPGSDFVGHIGGDDFMLVLGPED 509
Cdd:cd07556   1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDH 62
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 297-343 6.22e-05

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.04  E-value: 6.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15598454   297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLR 343
Cdd:pfam00571  12 VSPDTTLEEALELMREH-GISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 301-412 8.76e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 42.13  E-value: 8.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 301 TSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRhalTDaLLRPFACDLFLRKPISRLMSDDFLAVELGQTLQQVSRLLT 380
Cdd:cd09836  12 TTIREAAKLMAEN-NIGSVVVVDDDGKPVGIVTE---RD-IVRAVAEGIDLDTPVEEIMTKNLVTVSPDESIYEAAELMR 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598454 381 SRarqRIEEDFIVTRGGHYAGMGRVIDVLRLI 412
Cdd:cd09836  87 EH---NIRHLPVVDGGGKLVGVISIRDLAREL 115
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
415-505 1.50e-04

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 44.62  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454  415 EKLQ-QARHaNPLTLLPGN--------VPIQQCLErllQQRREAVIcYIDVDSFKPFNDLYGYARGDEVLLCLAQCLSER 485
Cdd:PRK15426 392 SSLQwQAWH-DPLTRLYNRgalfekarALAKRCQR---DQQPFSVI-QLDLDHFKSINDRFGHQAGDRVLSHAAGLISSS 466

                         90       100
                 ....*....|....*....|
gi 15598454  486 IDPGsDFVGHIGGDDFMLVL 505
Cdd:PRK15426 467 LRAQ-DVAGRVGGEEFCVVL 485
CBS COG0517
CBS domain [Signal transduction mechanisms];
297-346 7.73e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.85  E-value: 7.73e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15598454 297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLRPFA 346
Cdd:COG0517  80 VSPDTSLEEAAELMEEH-KIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 286-379 1.06e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 39.05  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598454 286 DLRALLleqrAVDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVhrhALTDALLRPFACDLFLRKPISRLMSDDFLA 365
Cdd:cd04608   8 DLGAPV----TVLPDDTLGEAIEIMREY-GVDQLPVVDEDGRVVGMV---TEGNLLSSLLAGRAQPSDPVSKAMYKQFKQ 79

                        90
                ....*....|....
gi 15598454 366 VELGQTLQQVSRLL 379
Cdd:cd04608  80 VDLDTPLGALSRIL 93
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
297-343 3.56e-03

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.92  E-value: 3.56e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15598454 297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDALLR 343
Cdd:COG3448  86 VTPDTPLEEAAELMLEH-GIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
297-341 9.24e-03

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.94  E-value: 9.24e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15598454 297 VDVRTSTQEVVEIFRRQaNLNSLAILDEEGRPIGIVHRHALTDAL 341
Cdd:COG2524 163 VSEDDSLEEALRLMLEH-GIGRLPVVDDDGKLVGIITRTDILRAL 206
 
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