NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1054581769|ref|WP_066350512|]
View 

diguanylate cyclase [Aliarcobacter skirrowii]

Protein Classification

CBS_pair and GGDEF domain-containing protein( domain architecture ID 10115349)

CBS_pair and GGDEF domain-containing protein

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 ...
 273-443 5.86e-65

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: 209.83  E-value: 5.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 273 SKLQSKTTQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVV 352
Cdd:COG2199   101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRE-GRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 353 KNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIK---NISCSFGVTKFNK-SDSMQSILARADK 428
Cdd:COG2199   180 RASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGkelRVTVSIGVALYPEdGDSAEELLRRADL 259

                         170
                  ....*....|....*
gi 1054581769 429 AMYKAKNNGKNRVEI 443
Cdd:COG2199   260 ALYRAKRAGRNRVVV 274
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
128-250 1.36e-14

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


:

Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 72.22  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 128 LMLEKQTLSDmLLSSFVKKADINDLTKDVIELMDDTIYDCVIIFDKSNSVGILTTKDIIKLFGESKDL-NLPVSNYMRSP 206
Cdd:COG2524    81 GLVLKMKVKD-IMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRDLlDAPVSDIMTRD 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1054581769 207 LVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:COG2524   160 VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDIL 203
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 12-121 1.34e-11

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: 61.11  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  12 TKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR-LKSDNIDFNTKLKDIKYDKIFSTHYKTSIPD 90
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRaLVEGGLALDTPVAEVMTPDVITVSPDTDLEE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1054581769  91 AIEE-IGFNGNSLCLVDDDDKLCGFVSYHDII 121
Cdd:cd02205    81 ALELmLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 273-443 5.86e-65

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: 209.83  E-value: 5.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 273 SKLQSKTTQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVV 352
Cdd:COG2199   101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRE-GRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 353 KNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIK---NISCSFGVTKFNK-SDSMQSILARADK 428
Cdd:COG2199   180 RASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGkelRVTVSIGVALYPEdGDSAEELLRRADL 259

                         170
                  ....*....|....*
gi 1054581769 429 AMYKAKNNGKNRVEI 443
Cdd:COG2199   260 ALYRAKRAGRNRVVV 274
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 288-441 3.31e-60

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: 193.54  E-value: 3.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 288 TDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRWGG 367
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRS-GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054581769 368 EEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIK--NISCSFGVTKFN-KSDSMQSILARADKAMYKAKNNGKNRV 441
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQeiRVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 286-440 3.21e-52

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: 172.82  E-value: 3.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 286 ASTDNLTSLYNRAKFEQKLKYEISRATRyENQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRW 365
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALR-EGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 366 GGEEFFIIYPSTNLKQAFEASEKLRILINKLEF-----DDIKNISCSFGVTKFNKS-DSMQSILARADKAMYKAKNNGKN 439
Cdd:pfam00990  80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKIphtvsGLPLYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 1054581769 440 R 440
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 285-442 5.18e-49

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: 164.82  E-value: 5.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 285 LASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACR 364
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRF-QRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 365 WGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF----DDIKNISCSFGVTKF-NKSDSMQSILARADKAMYKAKNNGKN 439
Cdd:TIGR00254  80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIevagSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGRN 159


                  ...
gi 1054581769 440 RVE 442
Cdd:TIGR00254 160 RVV 162
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 284-443 1.42e-46

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 158.18  E-value: 1.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  284 QLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFAC 363
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQ-GSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  364 RWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF-DDIK-NISCSFGVTKFNKS-DSMQSILARADKAMYKAKNNGKNR 440
Cdd:smart00267  80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIiHGIPlYLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQ 159


                   ...
gi 1054581769  441 VEI 443
Cdd:smart00267 160 VAV 162
pleD PRK09581
response regulator PleD; Reviewed
 244-441 4.13e-46

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 165.46  E-value: 4.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 244 ITQKELLARVYS-----KWADFLRDKTVHlsSINsklqskttqleqLASTDNLTSLYNRAKFEQKLKYEISRATRyENQE 318
Cdd:PRK09581  259 IDKNELLARVRTqirrkRYQDALRNNLEQ--SIE------------MAVTDGLTGLHNRRYFDMHLKNLIERANE-RGKP 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 319 FSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF 398
Cdd:PRK09581  324 LSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPF 403

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1054581769 399 ---DDIK--NISCSFGVTKFNKS-DSMQSILARADKAMYKAKNNGKNRV 441
Cdd:PRK09581  404 iisDGKErlNVTVSIGVAELRPSgDTIEALIKRADKALYEAKNTGRNRV 452
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
243-441 8.88e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 148.59  E-value: 8.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 243 QITQKELLARVYSKWADFLRDktvhLSSinsklqskttQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIV 322
Cdd:NF038266   65 QLRRLEKIVRISDRYQRMMRD----LNE----------ALREASTRDPLTGLPNRRLLMERLREEVERARRS-GRPFTLA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 323 LFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF---D 399
Cdd:NF038266  130 MLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVrvgD 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1054581769 400 DIKNISCSFGVTKFNK-SDSMQSILARADKAMYKAKNNGKNRV 441
Cdd:NF038266  210 DVLSVTASAGLAEHRPpEEGLSATLSRADQALYQAKRAGRDRV 252
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
128-250 1.36e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 72.22  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 128 LMLEKQTLSDmLLSSFVKKADINDLTKDVIELMDDTIYDCVIIFDKSNSVGILTTKDIIKLFGESKDL-NLPVSNYMRSP 206
Cdd:COG2524    81 GLVLKMKVKD-IMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRDLlDAPVSDIMTRD 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1054581769 207 LVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:COG2524   160 VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDIL 203
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 144-251 1.44e-14

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: 69.58  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 144 VKKADINDLTKDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIK-LFGESKDLNLPVSNYMRSPLVKVKHTTTVSQALE 221
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKlVGIVTERDILRaLVEGGLALDTPVAEVMTPDVITVSPDTDLEEALE 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769 222 FIQQQKFKRLIIEDFAGNVIGQITQKELLA 251
Cdd:cd02205    84 LMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 12-121 1.34e-11

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: 61.11  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  12 TKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR-LKSDNIDFNTKLKDIKYDKIFSTHYKTSIPD 90
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRaLVEGGLALDTPVAEVMTPDVITVSPDTDLEE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1054581769  91 AIEE-IGFNGNSLCLVDDDDKLCGFVSYHDII 121
Cdd:cd02205    81 ALELmLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
15-123 8.04e-11

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 59.54  E-value: 8.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  15 VTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIrlksdNIDFNTKLKDIKYDKIFSTHYKTSIPDAIEE 94
Cdd:COG4109    27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL-----GKDDDTPIEDVMTKNPITVTPDTSLASAAHK 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769  95 IGFNG-NSLCLVDDDDKLCGFVSYHDIISS 123
Cdd:COG4109   102 MIWEGiELLPVVDDDGRLLGIISRQDVLKA 131
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 154-252 1.20e-08

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 57.01  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNSVGILTTKDIikLFgeSKDLNLPVSNYM-RSPLVKVKHTTTVSQALEFIQQQKFKRLI 232
Cdd:pfam00478 100 ADALALMERYGISGVPVVDDGKLVGIVTNRDL--RF--ETDLSQPVSEVMtKENLVTAPEGTTLEEAKEILHKHKIEKLP 175

                          90       100
                  ....*....|....*....|
gi 1054581769 233 IEDFAGNVIGQITQKELLAR 252
Cdd:pfam00478 176 VVDDNGRLVGLITIKDIEKA 195
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 9-60 2.96e-04

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: 38.73  E-value: 2.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIRL 60
Cdd:pfam00571   3 DIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 273-443 5.86e-65

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: 209.83  E-value: 5.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 273 SKLQSKTTQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVV 352
Cdd:COG2199   101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRE-GRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 353 KNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIK---NISCSFGVTKFNK-SDSMQSILARADK 428
Cdd:COG2199   180 RASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGkelRVTVSIGVALYPEdGDSAEELLRRADL 259

                         170
                  ....*....|....*
gi 1054581769 429 AMYKAKNNGKNRVEI 443
Cdd:COG2199   260 ALYRAKRAGRNRVVV 274
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 288-441 3.31e-60

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: 193.54  E-value: 3.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 288 TDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRWGG 367
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRS-GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054581769 368 EEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIK--NISCSFGVTKFN-KSDSMQSILARADKAMYKAKNNGKNRV 441
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQeiRVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 286-440 3.21e-52

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: 172.82  E-value: 3.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 286 ASTDNLTSLYNRAKFEQKLKYEISRATRyENQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRW 365
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALR-EGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 366 GGEEFFIIYPSTNLKQAFEASEKLRILINKLEF-----DDIKNISCSFGVTKFNKS-DSMQSILARADKAMYKAKNNGKN 439
Cdd:pfam00990  80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKIphtvsGLPLYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 1054581769 440 R 440
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 285-442 5.18e-49

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: 164.82  E-value: 5.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 285 LASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACR 364
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRF-QRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 365 WGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF----DDIKNISCSFGVTKF-NKSDSMQSILARADKAMYKAKNNGKN 439
Cdd:TIGR00254  80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIevagSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGRN 159


                  ...
gi 1054581769 440 RVE 442
Cdd:TIGR00254 160 RVV 162
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 284-443 1.42e-46

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 158.18  E-value: 1.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  284 QLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFAC 363
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQ-GSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  364 RWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF-DDIK-NISCSFGVTKFNKS-DSMQSILARADKAMYKAKNNGKNR 440
Cdd:smart00267  80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIiHGIPlYLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQ 159


                   ...
gi 1054581769  441 VEI 443
Cdd:smart00267 160 VAV 162
pleD PRK09581
response regulator PleD; Reviewed
 244-441 4.13e-46

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 165.46  E-value: 4.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 244 ITQKELLARVYS-----KWADFLRDKTVHlsSINsklqskttqleqLASTDNLTSLYNRAKFEQKLKYEISRATRyENQE 318
Cdd:PRK09581  259 IDKNELLARVRTqirrkRYQDALRNNLEQ--SIE------------MAVTDGLTGLHNRRYFDMHLKNLIERANE-RGKP 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 319 FSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF 398
Cdd:PRK09581  324 LSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPF 403

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1054581769 399 ---DDIK--NISCSFGVTKFNKS-DSMQSILARADKAMYKAKNNGKNRV 441
Cdd:PRK09581  404 iisDGKErlNVTVSIGVAELRPSgDTIEALIKRADKALYEAKNTGRNRV 452
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 257-443 5.48e-42

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: 157.63  E-value: 5.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 257 WADFLRDKTVHLSSINSKLQSKTTQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRyENQEFSIVLFDVDNFKIINDTY 336
Cdd:COG5001   222 LLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARR-SGRRLALLFIDLDRFKEINDTL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 337 GHLAGDMVLKKIADVVKNTIRSTDFACRWGGEEFFIIYPS-TNLKQAFEASEKLR------ILINKLEFddikNISCSFG 409
Cdd:COG5001   301 GHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILaalaepFELDGHEL----YVSASIG 376

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1054581769 410 VTKFNK-SDSMQSILARADKAMYKAKNNGKNRVEI 443
Cdd:COG5001   377 IALYPDdGADAEELLRNADLAMYRAKAAGRNRYRF 411
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
243-441 8.88e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 148.59  E-value: 8.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 243 QITQKELLARVYSKWADFLRDktvhLSSinsklqskttQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIV 322
Cdd:NF038266   65 QLRRLEKIVRISDRYQRMMRD----LNE----------ALREASTRDPLTGLPNRRLLMERLREEVERARRS-GRPFTLA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 323 LFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF---D 399
Cdd:NF038266  130 MLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVrvgD 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1054581769 400 DIKNISCSFGVTKFNK-SDSMQSILARADKAMYKAKNNGKNRV 441
Cdd:NF038266  210 DVLSVTASAGLAEHRPpEEGLSATLSRADQALYQAKRAGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 282-441 3.78e-40

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 145.59  E-value: 3.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 282 LEQLASTDNLTSLYNR----AKFEQKLKyeisratRYENQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIR 357
Cdd:PRK09894  125 LTIRSNMDVLTGLPGRrvldESFDHQLR-------NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTR 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 358 STDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILI--NKLEFDDIK-NISCSFGVTKFNKSDSMQSILARADKAMYKAK 434
Cdd:PRK09894  198 DYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIanHAITHSDGRiNITATFGVSRAFPEETLDVVIGRADRAMYEGK 277


                  ....*..
gi 1054581769 435 NNGKNRV 441
Cdd:PRK09894  278 QTGRNRV 284
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
275-441 2.01e-37

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 143.62  E-value: 2.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 275 LQSKttqLEQLASTDNLTSLYNRAKFEQKLKYEISRATRyENQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKN 354
Cdd:PRK15426  390 LQSS---LQWQAWHDPLTRLYNRGALFEKARALAKRCQR-DQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISS 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 355 TIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIKN----ISCSFGVTKFNKS-----DSMQSIlar 425
Cdd:PRK15426  466 SLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSttirISASLGVSSAEEDgdydfEQLQSL--- 542

                         170
                  ....*....|....*.
gi 1054581769 426 ADKAMYKAKNNGKNRV 441
Cdd:PRK15426  543 ADRRLYLAKQAGRNRV 558
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 281-445 2.06e-31

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 127.87  E-value: 2.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  281 QLEQLASTDNLTSLYNRAKFEQKLKyEISRATRYENQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTD 360
Cdd:PRK09776   660 QLSYSASHDALTHLANRASFEKQLR-RLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  361 FACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF---DDIKNISCSFGVTKFNKSDSMQS-ILARADKAMYKAKNN 436
Cdd:PRK09776   739 VLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFpweGRVYRVGASAGITLIDANNHQASeVMSQADIACYAAKNA 818


                   ....*....
gi 1054581769  437 GKNRVEIEE 445
Cdd:PRK09776   819 GRGRVTVYE 827
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 274-443 3.11e-23

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 100.29  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 274 KLQSKTTQLEQLASTDNLTSLYNRAKFEQKLKYEISRATRYeNQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVK 353
Cdd:PRK10245  193 KLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRH-HRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQ 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 354 NTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEFDDIKNI--SCSFGVTKFNKSDS-MQSILARADKAM 430
Cdd:PRK10245  272 ITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVtlRISVGVAPLNPQMShYREWLKSADLAL 351

                         170
                  ....*....|...
gi 1054581769 431 YKAKNNGKNRVEI 443
Cdd:PRK10245  352 YKAKNAGRNRTEV 364
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
282-438 2.69e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 93.59  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 282 LEQLASTDNLTSLYNRAKFEQKLKYEISRATRyenQEFSIVLFDVDNFKIINDTYGHLAGDMVLKKIADVVKNTIRSTDF 361
Cdd:PRK10060  233 LRILANTDSITGLPNRNAIQELIDHAINAADN---NQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 362 ACRWGGEEFFIIYPSTNlKQAFEAS-----EKLR--ILINKLEFddikNISCSFGVTKF-NKSDSMQSILARADKAMYKA 433
Cdd:PRK10060  310 LARLGGDEFLVLASHTS-QAALEAMasrilTRLRlpFRIGLIEV----YTGCSIGIALApEHGDDSESLIRSADTAMYTA 384


                  ....*
gi 1054581769 434 KNNGK 438
Cdd:PRK10060  385 KEGGR 389
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
128-250 1.36e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 72.22  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 128 LMLEKQTLSDmLLSSFVKKADINDLTKDVIELMDDTIYDCVIIFDKSNSVGILTTKDIIKLFGESKDL-NLPVSNYMRSP 206
Cdd:COG2524    81 GLVLKMKVKD-IMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRDLlDAPVSDIMTRD 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1054581769 207 LVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:COG2524   160 VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDIL 203
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 144-251 1.44e-14

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: 69.58  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 144 VKKADINDLTKDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIK-LFGESKDLNLPVSNYMRSPLVKVKHTTTVSQALE 221
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKlVGIVTERDILRaLVEGGLALDTPVAEVMTPDVITVSPDTDLEEALE 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769 222 FIQQQKFKRLIIEDFAGNVIGQITQKELLA 251
Cdd:cd02205    84 LMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 154-250 6.82e-14

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 67.93  E-value: 6.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNS-VGILTTKDII-KLFGESKD-LNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKR 230
Cdd:COG2905    19 REAARLMTEKGVGSLVVVDDDGRlVGIITDRDLRrRVLAEGLDpLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRH 98

                          90       100
                  ....*....|....*....|
gi 1054581769 231 LIIEDfAGNVIGQITQKELL 250
Cdd:COG2905    99 LPVVD-DGKLVGIVSITDLL 117
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 263-439 1.04e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 73.27  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 263 DKTVHLSSINSKLQSKTTQLEQLASTDNLTSLYNRAKFEQKLKYEISRAtryenQEFSIVLFDVDNFKIINDTYGHLAGD 342
Cdd:PRK11359  353 DISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKA-----VSPVVYLIGVDHFQDVIDSLGYAWAD 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 343 MVLKKIADVVKNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINK-LEFDDIK-NISCSFGVTKFNKSDSmQ 420
Cdd:PRK11359  428 QALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKpIMIDDKPfPLTLSIGISYDVGKNR-D 506

                         170
                  ....*....|....*....
gi 1054581769 421 SILARADKAMYKAKNNGKN 439
Cdd:PRK11359  507 YLLSTAHNAMDYIRKNGGN 525
PRK09966 PRK09966
diguanylate cyclase DgcN;
274-440 1.71e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 68.88  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 274 KLQSKTTQLEQLASTDNLTSLYNRAKFEQK----LKYEISRATryenqefSIVLF-DVDNFKIINDTYGHLAGDMVLKKI 348
Cdd:PRK09966  236 RLQAKNAQLLRTALHDPLTGLANRAAFRSGintlMNNSDARKT-------SALLFlDGDNFKYINDTWGHATGDRVLIEI 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 349 ADVVKNTIRSTDFACRWGGEEF-FIIYpstNLKQAFEASEKLRILINklEFD---DIKN-----ISCSFGVTKFNKSDSM 419
Cdd:PRK09966  309 AKRLAEFGGLRHKAYRLGGDEFaMVLY---DVQSESEVQQICSALTQ--IFNlpfDLHNghqttMTLSIGYAMTIEHASA 383

                         170       180
                  ....*....|....*....|.
gi 1054581769 420 QSILARADKAMYKAKNNGKNR 440
Cdd:PRK09966  384 EKLQELADHNMYQAKHQRAEK 404
CBS COG0517
CBS domain [Signal transduction mechanisms];
154-253 6.45e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 62.58  E-value: 6.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIK-LFGESKDL-NLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKR 230
Cdd:COG0517    21 REALELMSEKRIGGLPVVDEDGKlVGIVTDRDLRRaLAAEGKDLlDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRR 100

                          90       100
                  ....*....|....*....|...
gi 1054581769 231 LIIEDFAGNVIGQITQKELLARV 253
Cdd:COG0517   101 LPVVDDDGRLVGIITIKDLLKAL 123
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
154-259 1.18e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.19  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIKLFGES-------KDLNLPVSNYMRSPLVKVKHTTTVSQALEFIQQ 225
Cdd:COG3448    22 REALELMREHGIRGLPVVDEDGRlVGIVTERDLLRALLPDrldeleeRLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLE 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1054581769 226 QKFKRLIIEDFAGNVIGQITQKELLARVYSKWAD 259
Cdd:COG3448   102 HGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEE 135
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 12-121 1.34e-11

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: 61.11  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  12 TKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR-LKSDNIDFNTKLKDIKYDKIFSTHYKTSIPD 90
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRaLVEGGLALDTPVAEVMTPDVITVSPDTDLEE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1054581769  91 AIEE-IGFNGNSLCLVDDDDKLCGFVSYHDII 121
Cdd:cd02205    81 ALELmLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
15-123 8.04e-11

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 59.54  E-value: 8.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  15 VTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIrlksdNIDFNTKLKDIKYDKIFSTHYKTSIPDAIEE 94
Cdd:COG4109    27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL-----GKDDDTPIEDVMTKNPITVTPDTSLASAAHK 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769  95 IGFNG-NSLCLVDDDDKLCGFVSYHDIISS 123
Cdd:COG4109   102 MIWEGiELLPVVDDDGRLLGIISRQDVLKA 131
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 360-434 9.37e-11

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: 60.69  E-value: 9.37e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054581769 360 DFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEFDdikNISCSFGVtkfnksdSMQSILARADkAMYKAK 434
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL---RVTVSIGV-------AGDSLLKRAD-ALYQAR 179
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
9-121 2.92e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 59.90  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKkgF-GIIKANDLIRLKSDNIDF-NTKLKDIKYDKIFSTHYKT 86
Cdd:COG2524    90 DIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK--LvGIITERDLLKALAEGRDLlDAPVSDIMTRDVVTVSEDD 167

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1054581769  87 SIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDII 121
Cdd:COG2524   168 SLEEALRLMLEHGiGRLPVVDDDGKLVGIITRTDIL 203
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 144-251 4.80e-10

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: 56.76  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 144 VKKADINDLTKDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIKLFGESKDLNLPVSNYMRSPLVKVKHTTTVSQALEF 222
Cdd:cd09836     5 VVTVPPETTIREAAKLMAENNIGSVVVVDDDGKpVGIVTERDIVRAVAEGIDLDTPVEEIMTKNLVTVSPDESIYEAAEL 84

                          90       100
                  ....*....|....*....|....*....
gi 1054581769 223 IQQQKFKRLIIEDFAGNVIGQITQKELLA 251
Cdd:cd09836    85 MREHNIRHLPVVDGGGKLVGVISIRDLAR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
9-121 1.01e-09

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 56.41  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR-LKSDNIDF-NTKLKDIKYDKIFSTHYKT 86
Cdd:COG0517     5 DIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRaLAAEGKDLlDTPVSEVMTRPPVTVSPDT 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1054581769  87 SIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDII 121
Cdd:COG0517    85 SLEEAAELMEEHKiRRLPVVDDDGRLVGIITIKDLL 120
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
9-121 1.85e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 55.64  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR--LKSDNIDF-----NTKLKDIKYDKIFS 81
Cdd:COG3448     6 DIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRalLPDRLDELeerllDLPVEDVMTRPVVT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1054581769  82 THYKTSIPDAIEE-IGFNGNSLCLVDDDDKLCGFVSYHDII 121
Cdd:COG3448    86 VTPDTPLEEAAELmLEHGIHRLPVVDDDGRLVGIVTRTDLL 126
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 86-187 6.06e-09

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: 53.79  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  86 TSIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDIISSVDPQLMLEKQTLSDmLLSSFVKKADINDLTKDVIELMDDTI 164
Cdd:cd02205    11 TTVREALELMAENGiGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAE-VMTPDVITVSPDTDLEEALELMLEHG 89

                          90       100
                  ....*....|....*....|....
gi 1054581769 165 YDCVIIFDKSNS-VGILTTKDIIK 187
Cdd:cd02205    90 IRRLPVVDDDGKlVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
70-191 9.40e-09

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 53.33  E-value: 9.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  70 KLKDIKYDKIFSTHYKTSIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDIISSVDPQLM-LEKQTLSDmLLSSFVKKA 147
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRiGGLPVVDEDGKLVGIVTDRDLRRALAAEGKdLLDTPVSE-VMTRPPVTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1054581769 148 DINDLTKDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIKLFGE 191
Cdd:COG0517    81 SPDTSLEEAAELMEEHKIRRLPVVDDDGRlVGIITIKDLLKALLE 125
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 154-252 1.20e-08

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 57.01  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNSVGILTTKDIikLFgeSKDLNLPVSNYM-RSPLVKVKHTTTVSQALEFIQQQKFKRLI 232
Cdd:pfam00478 100 ADALALMERYGISGVPVVDDGKLVGIVTNRDL--RF--ETDLSQPVSEVMtKENLVTAPEGTTLEEAKEILHKHKIEKLP 175

                          90       100
                  ....*....|....*....|
gi 1054581769 233 IEDFAGNVIGQITQKELLAR 252
Cdd:pfam00478 176 VVDDNGRLVGLITIKDIEKA 195
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 71-192 1.81e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 52.52  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  71 LKDIKYDKIFSTHYKTSIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDIISSV-DPQLMLEKQTLSDmLLSSFVKKAD 148
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGvGSLVVVDDDGRLVGIITDRDLRRRVlAEGLDPLDTPVSE-VMTRPPITVS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1054581769 149 INDLTKDVIELMDDTIYDCVIIFDKSNSVGILTTKDIIKLFGES 192
Cdd:COG2905    80 PDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 9-128 2.30e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 52.14  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLI-RLKSDNIDF-NTKLKDIKYDKIFSTHYKT 86
Cdd:COG2905     3 DIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRrRVLAEGLDPlDTPVSEVMTRPPITVSPDD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1054581769  87 SIPDAIEEIGFNGNSLCLVDDDDKLCGFVSYHDIISSVDPQL 128
Cdd:COG2905    83 SLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEEL 124
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 144-250 3.00e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; 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: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 51.77  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 144 VKKADINDLTKDVIELMDDTIYDCVIIFDKSNS-VGILTTKDI-IKLFGESKD-LNLPVSNYMRSPLVKVKHTTTVSQAL 220
Cdd:cd17775     5 VVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKpVGIVTDRDIvVEVVAKGLDpKDVTVGDIMSADLITAREDDGLFEAL 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769 221 EFIQQQKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:cd17775    85 ERMREKGVRRLPVVDDDGELVGIVTLDDIL 114
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 154-250 3.92e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 51.26  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIikLFgeSKDLNLPVSNYM--RSPLVKVKHTTTVSQALEFIQQQKFKR 230
Cdd:cd04601    14 ADVLELKAEYGISGVPVTEDGGKlVGIVTSRDI--RF--ETDLSTPVSEVMtpDERLVTAPEGITLEEAKEILHKHKIEK 89

                          90       100
                  ....*....|....*....|
gi 1054581769 231 LIIEDFAGNVIGQITQKELL 250
Cdd:cd04601    90 LPIVDDNGELVGLITRKDIE 109
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 155-250 4.55e-08

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. 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: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 51.77  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 155 DVIELMDDTIYDCVIIFDKSNS--------VGILTTKDIIKLFGESKDL-NLPVSNYMRSPLVKVKHTTTVSQALEFIQQ 225
Cdd:cd17774    18 ELAQLMAEHRVSCVVIVEEDEQqeknklipVGIVTERDIVQFQALGLDLsQTQAQTVMSSPLFSLRPDDSLWTAHQLMQQ 97

                          90       100
                  ....*....|....*....|....*
gi 1054581769 226 QKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:cd17774    98 RRIRRLVVVGEQGELLGIVTQTSLL 122
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 9-121 5.53e-08

signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. 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.


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 51.46  E-value: 5.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIIL-SNTKKGFGIIKANDLIRL-----KSDNIDF----------NTKLK 72
Cdd:cd17779     4 AIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVAdAGTKRLEGIVTSMDIVDFlgggsKYNLVEKkhngnllaaiNEPVR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054581769  73 DIKYDKIFSTHYKTSIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDII 121
Cdd:cd17779    84 EIMTRDVISVKENASIDDAIELMLEKNvGGLPIVDKDGKVIGIVTERDFL 133
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 11-124 7.25e-08

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: 50.60  E-value: 7.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  11 ATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIRLKSDNIDFNTKLKDIKYDKIFSTHYKTSIPD 90
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVEEIMTKNLVTVSPDESIYE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1054581769  91 AIEE-IGFNGNSLCLVDDDDKLCGFVSYHDIISSV 124
Cdd:cd09836    81 AAELmREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 320-410 7.87e-08

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: 50.82  E-value: 7.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 320 SIVLFDVDNFKIINDTYGHLAGDMVLKKIA-DVVKNTIRSTDFACRWGGEEFFIIYPSTNLKQAFEASEKLRILINKLEF 398
Cdd:cd07556     3 TILFADIVGFTSLADALGPDEGDELLNELAgRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ 82

                          90
                  ....*....|..
gi 1054581769 399 DDIKNISCSFGV 410
Cdd:cd07556    83 SEGNPVRVRIGI 94
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 166-250 1.17e-07

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. 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: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 50.61  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 166 DCVIIFDKSNSVGILTTKDIIKLFGESKDL-NLPVSNYMRSPLVKVKHT--TTVSQALEFIQQQKFKRLIIEDFAGNVIG 242
Cdd:cd04620    47 SCVLVVENQQLVGIFTERDVVRLTASGIDLsGVTIAEVMTQPVITLKESefQDIFTVLSLLRQHQIRHLPIVDDQGQLVG 126


                  ....*...
gi 1054581769 243 QITQKELL 250
Cdd:cd04620   127 LITPESLR 134
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
70-196 3.08e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 49.48  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  70 KLKDIKYDKIFSTHYKTSIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDIISSVDPQLMLE-KQTLSDMLLSSF---- 143
Cdd:COG3448     3 TVRDIMTRDVVTVSPDTTLREALELMREHGiRGLPVVDEDGRLVGIVTERDLLRALLPDRLDElEERLLDLPVEDVmtrp 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054581769 144 VKKADINDLTKDVIELMDDTIYDCVIIFDKSNS-VGILTTKDIIKLFGESKDLN 196
Cdd:COG3448    83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRlVGIVTRTDLLRALARLLEEE 136
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 154-246 4.62e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 48.37  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 154 KDVIELMDDTIYDCVIIFDKSNSVGILTTKDIIKL-FGESKDLNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLI 232
Cdd:cd09833    17 ADAAARMAERRCSSILIVENGEIVGIWTERDALKLdFSDPDAFRRPISEVMSSPVLTIPQDTTLGEAAVRFRQEGVRHLL 96

                          90
                  ....*....|....
gi 1054581769 233 IEDFAGNVIGQITQ 246
Cdd:cd09833    97 VVDDDGRPVGIVSQ 110
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
4-189 5.53e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 49.88  E-value: 5.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   4 LPKLIDIATKAVTTVYDTQSINDAIALMYKEnhREIIILSNTKKGFGIIKANDLIRLKSDNIDFNTKLKDIKYDKIFSTH 83
Cdd:COG2524    23 LLLLAALVLALTAAAAATVLLLAAAAAAAGA--GGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  84 YKTSIPDAIEEIgFNGNSLCL-VDDDDKLCGFVSYHDIISSVDPQLMLEKQTLSDmLLSSFVKKADINDLTKDVIELMDD 162
Cdd:COG2524   101 PDTTLEEALELM-LEKGISGLpVVDDGKLVGIITERDLLKALAEGRDLLDAPVSD-IMTRDVVTVSEDDSLEEALRLMLE 178

                         170       180
                  ....*....|....*....|....*...
gi 1054581769 163 TIYDCVIIFDKSNS-VGILTTKDIIKLF 189
Cdd:COG2524   179 HGIGRLPVVDDDGKlVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
196-266 7.12e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 7.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054581769 196 NLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELLARV----YSKWADFLRDKTV 266
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALlpdrLDELEERLLDLPV 75
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 153-250 9.96e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 47.14  E-value: 9.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 153 TKDVIEL-MDDTIYDCVIIF-----------DKSNSVGILTTKDIIKLFGESKdLNLPVSNYMRSPLVKVKHTTTVSQAL 220
Cdd:cd04588     1 SKDLITLkPDATIKDAAKLLsennihgapvvDDGKLVGIVTLTDIAKALAEGK-ENAKVKDIMTKDVITIDKDEKIYDAI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769 221 EFIQQQKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:cd04588    80 RLMNKHNIGRLIVVDDNGKPVGIITRTDIL 109
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 144-250 1.23e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; 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: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 47.01  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 144 VKKADINDLTKDVIELMDDTIYDCVIIFDKSNSVGILTTKDII-------KLFGEskdlnLPVSNYMRSPLVKVKHTTTV 216
Cdd:cd17776     5 VVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALhagyatdDPFSE-----IPVRAVASRPLVTISPTATL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1054581769 217 SQALEFIQQQKFKRLIIEDfAGNVIGQITQKELL 250
Cdd:cd17776    80 REAAERMVDEGVKKLPVVD-GLDLVGILTATDII 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 199-253 1.36e-06

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: 45.28  E-value: 1.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054581769 199 VSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELLARV 253
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRAL 55
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 9-121 3.51e-06

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. 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.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 46.17  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKgFGIIKANDLI----------RLKSDNID--FNTKLKDIKY 76
Cdd:cd17778     4 EFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKL-VGIVTAMDIVkyfgsheakkRLTTGDIDeaYSTPVEEIMS 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1054581769  77 DKIFSTHYKTSIPDAIEE-IGFNGNSLCLVDDDDKLCGFVSYHDII 121
Cdd:cd17778    83 KEVVTIEPDADIAEAARLmIKKNVGSLLVVDDEGELKGIITERDVL 128
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 177-251 5.76e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present 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: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 45.12  E-value: 5.76e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054581769 177 VGILTTKDIIKLFGESK---DLNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRL-IIEDfaGNVIGQITQKELLA 251
Cdd:cd04629    39 VGFLSEQDCLKALLEASyhcEPGGTVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYpVVED--GKLVGQISRRDVLR 115
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 148-250 1.51e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 44.02  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 148 DINDLTKDVIELMDDTIYDCVIIFDKS--NSVGILTTKDIIKLFGEsKDLNLPVSNYMRSPLVkVKHTTTVSQALEFIQQ 225
Cdd:cd04590    16 DADATLEELLELILESGYSRFPVYEGDldNIIGVLHVKDLLAALLE-GREKLDLRALLRPPLF-VPETTPLDDLLEEFRK 93

                          90       100
                  ....*....|....*....|....*
gi 1054581769 226 QKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:cd04590    94 ERSHMAIVVDEYGGTAGIVTLEDIL 118
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 11-122 1.64e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; 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: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 44.07  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  11 ATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDL-IRLKSDNID-FNTKLKDIKYDKIFSTHYKTSI 88
Cdd:cd17775     1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIvVEVVAKGLDpKDVTVGDIMSADLITAREDDGL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1054581769  89 PDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDIIS 122
Cdd:cd17775    81 FEALERMREKGvRRLPVVDDDGELVGIVTLDDILE 115
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 199-266 3.07e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 43.28  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054581769 199 VSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELLARVYSKWADFLrDKTV 266
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPL-DTPV 67
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 12-123 3.95e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. 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: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 42.69  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  12 TKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKgFGIIKANDLIRLksdniDFNTKLKDIKYDKIFSTHYKTSIPDA 91
Cdd:cd04610     2 TRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKV-VGYVTAKDLLGK-----DDDEKVSEIMSRDTVVADPDMDITDA 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1054581769  92 IEEIGFNGNS-LCLVDDDDKLCGFVSYHDIISS 123
Cdd:cd04610    76 ARVIFRSGISkLPVVDDEGNLVGIITNMDVIRS 108
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 102-187 6.08e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 42.70  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 102 LCLVDDDDKLCGFVSYHDIISSV-----DPQ---LMLEKQTLSD----MLLSSFVKKADINDLTKDVIELMDDtiYDC-- 167
Cdd:cd04632    28 LPVVDDNGKLVGIVTTYDIVDFVvrpgtKTRggdRGGEKERMLDlpvyDIMSSPVVTVTRDATVADAVERMLE--NDIsg 105

                          90       100
                  ....*....|....*....|.
gi 1054581769 168 -VIIFDKSNSVGILTTKDIIK 187
Cdd:cd04632   106 lVVTPDDNMVIGILTKTDVLR 126
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 167-250 8.01e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. 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: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 41.64  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 167 CVIIFDKSNSVGILTTKDI-IKLFGESKDLNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDfAGNVIGQIT 245
Cdd:cd04587    29 SLLVVDDGRLVGIVTDRDLrNRVVAEGLDPDTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVD-DGRVVGVVT 107


                  ....*
gi 1054581769 246 QKELL 250
Cdd:cd04587   108 ATDLM 112
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 156-250 1.24e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 41.55  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 156 VIELM-DDTIYDCVIIFDKSNSVGILTTKDIIK-------------LFGES-KDLNLPVSNYMRSPLVKVKHTTTVSQAL 220
Cdd:cd04632    16 AINLLrEHGISRLPVVDDNGKLVGIVTTYDIVDfvvrpgtktrggdRGGEKeRMLDLPVYDIMSSPVVTVTRDATVADAV 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 1054581769 221 EFIQQQKFKRLIIEDFAGNVIGQITQKELL 250
Cdd:cd04632    96 ERMLENDISGLVVTPDDNMVIGILTKTDVL 125
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 12-124 1.36e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; 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: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 41.25  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769  12 TKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR-LKSDNIDFNTKLKDIKYDKIFSTHYKTSIPD 90
Cdd:cd17784     1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHnLILDKYELGTTVEEVMVKDVATVHPDETLLE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1054581769  91 AIEEIGFNG------NSLCLVdDDDKLCGFVSYHDIISSV 124
Cdd:cd17784    81 AIKKMDSNApdeeiiNQLPVV-DDGKLVGIISDGDIIRAI 119
CBS_pair_Thermoplasmatales cd17786
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 144-249 1.42e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Thermoplasmatales; 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: 341422 [Multi-domain]  Cd Length: 114  Bit Score: 41.37  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 144 VKKADINDLTKDVIELMDDT-IYDCVIIFDKSNSVGILTTKDIIKLF--GESKDLNLPVSNYMRSPLVKVKHTTTVSQAL 220
Cdd:cd17786     4 FKTINWNATVFDAVKIMNENhLYGLVVKDDDGNYVGLISERSIIKRFipRNVKPDEVPVKLVMRKPIPKVKSDYDVKDVA 83

                          90       100
                  ....*....|....*....|....*....
gi 1054581769 221 EFIQQQKFKRLIIEDFAGNVIGQITQKEL 249
Cdd:cd17786    84 AFLSENGLERCAVVDDNGRVVGIVTITDL 112
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 9-120 1.84e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. 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: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 40.68  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDL---IRLKSDNIdfntklkdikyDKIFSTHYK 85
Cdd:cd04605     4 DIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDIskaVALKKDSL-----------EEIMTRNVI 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1054581769  86 TSIPD-AIEEIG-----FNGNSLCLVDDDDKLCGFVSYHDI 120
Cdd:cd04605    73 TARPDePIELAArkmekHNISALPVVDDDRRVIGIITSDDI 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 9-60 2.96e-04

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: 38.73  E-value: 2.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIRL 60
Cdd:pfam00571   3 DIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 199-256 3.24e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. 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: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 40.48  E-value: 3.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054581769 199 VSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDfAGNVIGQITQKELLARVYSK 256
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRASPSK 58
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 272-445 4.76e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 42.62  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 272 NSKLQSKTTQ-LEQLASTDNLTSLYNRAKFEQKLKYEISRATRYENQEFSIVlfdvdNFKIINDTYGHLAG---DMVLKK 347
Cdd:PRK11829  217 NQQLLADAYAdMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVI-----GIETLQEVSGAMSEaqhQQLLLT 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 348 IADVVKNTIRSTDFACRWGGEEFFII-----YPSTNLKQAfeaSEKLRILINKLEFDDIK-NISCSFGVTKFNKS-DSMQ 420
Cdd:PRK11829  292 IVQRIEQCIDDSDLLAQLSKTEFAVLargtrRSFPAMQLA---RRIMSQVTQPLFFDEITlRPSASIGITRYQAQqDTAE 368

                         170       180
                  ....*....|....*....|....*
gi 1054581769 421 SILARADKAMYKAKNNGKNRVEIEE 445
Cdd:PRK11829  369 SMMRNASTAMMAAHHEGRNQIMVFE 393
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 105-188 5.52e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 39.44  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 105 VDDDDKLCGFVSYHDIISSVDPQLMLEKqtlsdmllssfVKKAdindLTKDVIELMDDT-IYDCVIIFDKSN-------- 175
Cdd:cd04588    30 VVDDGKLVGIVTLTDIAKALAEGKENAK-----------VKDI----MTKDVITIDKDEkIYDAIRLMNKHNigrlivvd 94

                          90
                  ....*....|....*..
gi 1054581769 176 ----SVGILTTKDIIKL 188
Cdd:cd04588    95 dngkPVGIITRTDILKV 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
197-266 5.86e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.85  E-value: 5.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 197 LPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQITQKELLARVYSKWADFLrDKTV 266
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLL-DTPV 69
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 160-253 6.18e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341384 [Multi-domain]  Cd Length: 131  Bit Score: 39.63  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 160 MDDTIYDCVIIFDKSNSVGILTTKDIIKLFGeSKDLNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGN 239
Cdd:cd04611    31 MRSHRADAAVIECPDGGLGILTERDLVRFIA-RHPGNTPVGELASRPLLTVGAEDSLIHARDLLIDHRIRHLAVVDEDGQ 109

                          90
                  ....*....|....
gi 1054581769 240 VIGQITQKELLARV 253
Cdd:cd04611   110 VTGLLGFADLLAGV 123
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 148-227 7.25e-04

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 41.64  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 148 DINDLTKDVIELMDDTIYDCVIIFDKS--NSVGILTTKDIIKLFGESKDlnLPVSNYMRSPLVkVKHTTTVSQALEFIQQ 225
Cdd:COG1253   230 DLDDTLEEALELILESGHSRIPVYEGDldDIVGVVHVKDLLRALLEGEP--FDLRDLLRPPLF-VPETKPLDDLLEEFRR 306


                  ..
gi 1054581769 226 QK 227
Cdd:COG1253   307 ER 308
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 71-124 1.17e-03

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: 36.81  E-value: 1.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054581769  71 LKDIKYDKIFSTHYKTSIPDAIEEIGFNG-NSLCLVDDDDKLCGFVSYHDIISSV 124
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGiSRLPVVDEDGKLVGIVTLKDLLRAL 55
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 177-250 1.26e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. 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: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 38.32  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054581769 177 VGILTTKDIIKLFGESKDlNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDfAGNVIGQITQKELL 250
Cdd:cd04801    40 VGIVTLEDIRKVPEVERE-ATRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVE-DGELVGIISRTDLM 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 9-62 1.35e-03

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: 38.27  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIRLKS 62
Cdd:cd09836    63 EIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 177-250 1.48e-03

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. 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.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 38.75  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 177 VGILTTKDIIKLFGeSKD-------------LNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRL-IIEDfaGNVIG 242
Cdd:cd04631    43 VGIVTSTDIMRYLG-SGEafeklktgnihevLNVPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALpVVDD--GKLVG 119


                  ....*...
gi 1054581769 243 QITQKELL 250
Cdd:cd04631   120 IITERDIL 127
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 160-242 1.49e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; 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: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 38.17  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 160 MDDTIYD-----------CVIIFDKSNS-VGILTTKDII-KLFGESKD-LNLPVSNYMRSPLVKVKHTTTVSQALEFIQQ 225
Cdd:cd04623     9 PDATVAEalrllaeknigALVVVDDGGRlVGILSERDYVrKLALRGASsLDTPVSEIMTRDVVTCTPDDTVEECMALMTE 88

                          90
                  ....*....|....*...
gi 1054581769 226 QKFKRL-IIEDfaGNVIG 242
Cdd:cd04623    89 RRIRHLpVVED--GKLVG 104
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 151-245 3.06e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. 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: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 37.30  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 151 DLTKDVIELMDDTIYDCVIIFDKSNSVGILTTKDIIKlfgesKDLNLPVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKR 230
Cdd:cd04610    12 DTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLG-----KDDDEKVSEIMSRDTVVADPDMDITDAARVIFRSGISK 86

                          90
                  ....*....|....*
gi 1054581769 231 LIIEDFAGNVIGQIT 245
Cdd:cd04610    87 LPVVDDEGNLVGIIT 101
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 177-250 3.52e-03

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. 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.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 37.70  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 177 VGILTTKDIIKLFGESKDLNL------------PVSNYMRSPLVKVKHTTTVSQALEFIQQQKFKRLIIEDFAGNVIGQI 244
Cdd:cd17778    43 VGIVTAMDIVKYFGSHEAKKRlttgdideaystPVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGII 122


                  ....*.
gi 1054581769 245 TQKELL 250
Cdd:cd17778   123 TERDVL 128
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
9-60 4.05e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.54  E-value: 4.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054581769   9 DIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIRL 60
Cdd:COG3448    77 DVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRA 128
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 107-189 5.00e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. 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: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 37.02  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581769 107 DDDKLCGFVSYHDIISSVDPQLMLEKQTLSDMLLSSfVKKADIndLTKDVI------------ELMDDTIYDCVIIFDKS 174
Cdd:cd04584    38 DDGKLVGIVTDRDLLRASPSKATSLSIYELNYLLSK-IPVKDI--MTKDVItvspddtveeaaLLMLENKIGCLPVVDGG 114

                          90
                  ....*....|....*
gi 1054581769 175 NSVGILTTKDIIKLF 189
Cdd:cd04584   115 KLVGIITETDILRAF 129
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 6-59 5.32e-03

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: 36.45  E-value: 5.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054581769   6 KLIDIATKAVTTVYDTQSINDAIALMYKENHREIIILSNTKKGFGIIKANDLIR 59
Cdd:cd02205    60 PVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
 
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