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Conserved domains on  [gi|1055036525|ref|WP_066787350|]
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cyclic di-AMP binding protein CbpA [Rummeliibacillus stabekisii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_CbpA super family cl45816
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ...
 1-207 6.25e-52

cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain.


The actual alignment was detected with superfamily member NF038387:

Pssm-ID: 439679  Cd Length: 209  Bit Score: 166.64  E-value: 6.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQKYVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDKEEKFVGNAFKVAILEYKLEHGnDEDIPIRDLAADPDG 80
Cdd:NF038387    1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGG-DMSLPVTHLLKNATK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  81 TIGMESSFYEVFFTIKRLPYLTVLDENDNFAGILTHSRVFELLEEAWGYKTGSCALTIALPDQEGILARTLSVIRKKWPV 160
Cdd:NF038387   80 FISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1055036525 161 HCVFSID-DDDWYLRRVIVTLAKGATDQTVKEIEGILHKAGARLVDVE 207
Cdd:NF038387  160 ASCITLDeQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIE 207
 
Name Accession Description Interval E-value
CBS_CbpA NF038387
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ...
 1-207 6.25e-52

cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain.


Pssm-ID: 439679  Cd Length: 209  Bit Score: 166.64  E-value: 6.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQKYVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDKEEKFVGNAFKVAILEYKLEHGnDEDIPIRDLAADPDG 80
Cdd:NF038387    1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGG-DMSLPVTHLLKNATK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  81 TIGMESSFYEVFFTIKRLPYLTVLDENDNFAGILTHSRVFELLEEAWGYKTGSCALTIALPDQEGILARTLSVIRKKWPV 160
Cdd:NF038387   80 FISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1055036525 161 HCVFSID-DDDWYLRRVIVTLAKGATDQTVKEIEGILHKAGARLVDVE 207
Cdd:NF038387  160 ASCITLDeQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIE 207
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 10-120 1.02e-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: 59.57  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  10 KHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVGNAFKVAILEYKLEHGNDEDIPIRDLAADPDGTIGMESSFY 89
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLE 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1055036525  90 EVFFTI--KRLPYLTVLDENDNFAGILTHSRVF 120
Cdd:cd02205    80 EALELMleHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-123 2.65e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 52.19  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQkyVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkeEKFVGNAFKVAILEYKLEHGNDEDIPIRDLAADPDG 80
Cdd:COG2524    86 MKVKD--IMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVV 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1055036525  81 TIGMESSFYEVF--FTIKRLPYLTVLDENDNFAGILTHSRVFELL 123
Cdd:COG2524   162 TVSEDDSLEEALrlMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 8-49 4.72e-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: 34.50  E-value: 4.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1055036525   8 VNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVG 49
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVG 44
 
Name Accession Description Interval E-value
CBS_CbpA NF038387
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ...
 1-207 6.25e-52

cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain.


Pssm-ID: 439679  Cd Length: 209  Bit Score: 166.64  E-value: 6.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQKYVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDKEEKFVGNAFKVAILEYKLEHGnDEDIPIRDLAADPDG 80
Cdd:NF038387    1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGG-DMSLPVTHLLKNATK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  81 TIGMESSFYEVFFTIKRLPYLTVLDENDNFAGILTHSRVFELLEEAWGYKTGSCALTIALPDQEGILARTLSVIRKKWPV 160
Cdd:NF038387   80 FISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1055036525 161 HCVFSID-DDDWYLRRVIVTLAKGATDQTVKEIEGILHKAGARLVDVE 207
Cdd:NF038387  160 ASCITLDeQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIE 207
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 10-120 1.02e-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: 59.57  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  10 KHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVGNAFKVAILEYKLEHGNDEDIPIRDLAADPDGTIGMESSFY 89
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLE 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1055036525  90 EVFFTI--KRLPYLTVLDENDNFAGILTHSRVF 120
Cdd:cd02205    80 EALELMleHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-123 2.65e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 52.19  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQkyVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkeEKFVGNAFKVAILEYKLEHGNDEDIPIRDLAADPDG 80
Cdd:COG2524    86 MKVKD--IMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVV 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1055036525  81 TIGMESSFYEVF--FTIKRLPYLTVLDENDNFAGILTHSRVFELL 123
Cdd:COG2524   162 TVSEDDSLEEALrlMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
1-121 3.02e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 50.68  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQK-YVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILdDKEEKFVGnafkvaILEYKLEHGNDEDIPIRDLAADPD 79
Cdd:COG4109    14 EILLVEdIMTLEDVATLSEDDTVEDALELLEKTGHSRFPVV-DENGRLVG------IVTSKDILGKDDDTPIEDVMTKNP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1055036525  80 GTIGMESSFYEVF--FTIKRLPYLTVLDENDNFAGILTHSRVFE 121
Cdd:COG4109    87 ITVTPDTSLASAAhkMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
11-128 2.07e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  11 HDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVG----NAFKVAILEYKLEHGNDE--DIPIRDLAADPDGTIGM 84
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGivteRDLLRALLPDRLDELEERllDLPVEDVMTRPVVTVTP 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1055036525  85 ESSFYEVFFT-----IKRLPyltVLDENDNFAGILTHSRVFELLEEAWG 128
Cdd:COG3448    89 DTPLEEAAELmlehgIHRLP---VVDDDGRLVGIVTRTDLLRALARLLE 134
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-125 4.22e-06

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 44.47  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525   1 MIVKQkyVNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVGNAFKVAILEYKLEHGND-EDIPIRDLAADPD 79
Cdd:COG0517     1 MKVKD--IMTTDVVTVSPDATVREALELMSEKRIGGLPVVDE-DGKLVGIVTDRDLRRALAAEGKDlLDTPVSEVMTRPP 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1055036525  80 GTIGMESSFYEVFFT-----IKRLPyltVLDENDNFAGILTHSRVFELLEE 125
Cdd:COG0517    78 VTVSPDTSLEEAAELmeehkIRRLP---VVDDDGRLVGIITIKDLLKALLE 125
CBS_pair_bac cd09834
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 10-121 1.80e-04

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: 341404 [Multi-domain]  Cd Length: 118  Bit Score: 39.79  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  10 KHDVIFCKESDSISSVLKKLYSSGYRCIPILdDKEEKFVGNAFKVAILEYKLEHGND-----EDIPIRDLAADPDG-TIG 83
Cdd:cd09834     1 KSEVAYLYDDSTLRQALEKMEYHRYTAIPIL-NRDGKYVGTITEGDLLWYIKNKPNLdlkdaEKISIKDIPRRRDNkPVN 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1055036525  84 MESSFYEVFFTIKRLPYLTVLDENDNFAGILTHSRVFE 121
Cdd:cd09834    80 INANMEDLLDLAMNQNFVPVVDDRGVFIGIVTRKDIIK 117
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 29-115 5.49e-04

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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 38.64  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  29 LYSSGYRCIPILDdKEEKFVGNAFKVAILEYKLEHgndEDIPIRDLAA-------DPD-GTIGMESSFYEVFFTIKRLPY 100
Cdd:cd04643    25 LTKSGYSRIPVLD-KDYKLVGLISLSMILDAILGL---ERIEFEKLSElkveevmNTDvPTVSPDDDLEEVLHLLVDHPF 100

                          90
                  ....*....|....*
gi 1055036525 101 LTVLDENDNFAGILT 115
Cdd:cd04643   101 LCVVDEDGYFLGIIT 115
CBS_pair_chlorobiales cd09837
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 15-121 2.25e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in chlorobiales; 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: 341406 [Multi-domain]  Cd Length: 111  Bit Score: 36.58  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  15 FCKESDSISSVLKKLYSSGYRCIPILDDkeEKFVGNAfKVAILEYKLEHGNDEDIPIRDLAADPDGTIGMESSFYEVFFT 94
Cdd:cd09837     6 FFTDDAPAAEVLAFMQAKELSCAPVLHD--GRYVAMV-TLADLLPARQGTPTAGLKLGELSLEEVGSIGPHEHLFDLFSR 82

                          90       100
                  ....*....|....*....|....*....
gi 1055036525  95 IKRLPY--LTVLDENDNFAGILTHSRVFE 121
Cdd:cd09837    83 LALFPCsiIPVSDEDGRYIGVVSKKRVLE 111
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 11-125 3.46e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 36.35  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055036525  11 HDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVG----NAFKVAILEyklEHGNDEDIPIRDLAADPDGTIGMES 86
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDD-DGRLVGiitdRDLRRRVLA---EGLDPLDTPVSEVMTRPPITVSPDD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1055036525  87 SFYEVFFT-----IKRLPyltVLDeNDNFAGILTHSRVFELLEE 125
Cdd:COG2905    83 SLAEALELmeehrIRHLP---VVD-DGKLVGIVSITDLLRALSE 122
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 8-49 4.72e-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: 34.50  E-value: 4.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1055036525   8 VNKHDVIFCKESDSISSVLKKLYSSGYRCIPILDDkEEKFVG 49
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVG 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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