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Conserved domains on  [gi|489826438|ref|WP_003730209|]
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MULTISPECIES: cyclic di-AMP binding protein CbpA [Listeria]

Protein Classification

CBS domain-containing protein( domain architecture ID 17609527)

CBS (cystathione beta synthase) domain-containing protein; CBS domains may act as regulatory units

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_CbpA NF038387
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ...
 1-209 9.52e-138

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: 383.90  E-value: 9.52e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGEKFLGNIYKMHIYKHAANGGSLSDPVMSLIKNATKH 80
Cdd:NF038387   1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPVTHLLKNATKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  81 ICVNASFFEVFFTIKELPYIAVLNEQGNFYGILTHGKLLGLLQDGWNVKTTSYVLTIATGEVQGALTKITKIIDRYSSIA 160
Cdd:NF038387  81 ISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489826438 161 SLITLDNQTEDFIRRVLVSLPVGVTEEKKNEIVSHLERKGLRVVETEKI 209
Cdd:NF038387 161 SCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL 209
 
Name Accession Description Interval E-value
CBS_CbpA NF038387
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ...
 1-209 9.52e-138

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: 383.90  E-value: 9.52e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGEKFLGNIYKMHIYKHAANGGSLSDPVMSLIKNATKH 80
Cdd:NF038387   1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPVTHLLKNATKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  81 ICVNASFFEVFFTIKELPYIAVLNEQGNFYGILTHGKLLGLLQDGWNVKTTSYVLTIATGEVQGALTKITKIIDRYSSIA 160
Cdd:NF038387  81 ISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489826438 161 SLITLDNQTEDFIRRVLVSLPVGVTEEKKNEIVSHLERKGLRVVETEKI 209
Cdd:NF038387 161 SCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL 209
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 12-119 6.36e-16

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: 70.74  E-value: 6.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  12 NLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGGSLSD-PVMSLIKNATKHICVNASFFEV 90
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDDG-KLVGIVTERDILRALVEGGLALDtPVAEVMTPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489826438  91 FFTIKE--LPYIAVLNEQGNFYGILTHGKLL 119
Cdd:cd02205   82 LELMLEhgIRRLPVVDDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-127 7.09e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 68.35  E-value: 7.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPkiNLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGGS-------LSDPVMSL 73
Cdd:COG3448    2 MTVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDG-RLVGIVTERDLLRALLPDRLdeleerlLDLPVEDV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489826438  74 IKNATKHICVNASFFEVFFTIKE--LPYIAVLNEQGNFYGILTHGKLLGLLQDGWN 127
Cdd:COG3448   79 MTRPVVTVTPDTPLEEAAELMLEhgIHRLPVVDDDGRLVGIVTRTDLLRALARLLE 134
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 8-62 5.26e-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: 42.59  E-value: 5.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489826438    8 IPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAAN 62
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDG-KLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 12-53 3.17e-04

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 37.49  E-value: 3.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 489826438    12 NLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYK 53
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEG-RLVGIVTR 41
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
5-56 7.37e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 39.81  E-value: 7.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489826438   5 NLCIP------KINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHI 56
Cdd:PRK14869 243 NQSIPvsyimtTEDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDG-KVVGVISRYHL 299
 
Name Accession Description Interval E-value
CBS_CbpA NF038387
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ...
 1-209 9.52e-138

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: 383.90  E-value: 9.52e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGEKFLGNIYKMHIYKHAANGGSLSDPVMSLIKNATKH 80
Cdd:NF038387   1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPVTHLLKNATKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  81 ICVNASFFEVFFTIKELPYIAVLNEQGNFYGILTHGKLLGLLQDGWNVKTTSYVLTIATGEVQGALTKITKIIDRYSSIA 160
Cdd:NF038387  81 ISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489826438 161 SLITLDNQTEDFIRRVLVSLPVGVTEEKKNEIVSHLERKGLRVVETEKI 209
Cdd:NF038387 161 SCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL 209
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 12-119 6.36e-16

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: 70.74  E-value: 6.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  12 NLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGGSLSD-PVMSLIKNATKHICVNASFFEV 90
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDDG-KLVGIVTERDILRALVEGGLALDtPVAEVMTPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489826438  91 FFTIKE--LPYIAVLNEQGNFYGILTHGKLL 119
Cdd:cd02205   82 LELMLEhgIRRLPVVDDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-127 7.09e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 68.35  E-value: 7.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPkiNLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGGS-------LSDPVMSL 73
Cdd:COG3448    2 MTVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDG-RLVGIVTERDLLRALLPDRLdeleerlLDLPVEDV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489826438  74 IKNATKHICVNASFFEVFFTIKE--LPYIAVLNEQGNFYGILTHGKLLGLLQDGWN 127
Cdd:COG3448   79 MTRPVVTVTPDTPLEEAAELMLEhgIHRLPVVDDDGRLVGIVTRTDLLRALARLLE 134
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-124 3.00e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 61.42  E-value: 3.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPkiNLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGG--SLSDPVMSLIKNAT 78
Cdd:COG0517    1 MKVKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPVVDEDG-KLVGIVTDRDLRRALAAEGkdLLDTPVSEVMTRPP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489826438  79 KHICVNASFFEVF--FTIKELPYIAVLNEQGNFYGILTHGKLLGLLQD 124
Cdd:COG0517   78 VTVSPDTSLEEAAelMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-119 8.85e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.05  E-value: 8.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNLCIPkiNLTTVPGDATLQEAIHLLEESGYRCVPVLDekGEKFLGNIYKMHIYKHAANGGSLSD-PVMSLIKNATK 79
Cdd:COG2524   86 MKVKDIMTK--DVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLDaPVSDIMTRDVV 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489826438  80 HICVNASFFEVF--FTIKELPYIAVLNEQGNFYGILTHGKLL 119
Cdd:COG2524  162 TVSEDDSLEEALrlMLEHGIGRLPVVDDDGKLVGIITRTDIL 203
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
1-123 2.20e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 45.29  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   1 MLIKNlCIPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANggSLSDPVMSliknaTKH 80
Cdd:COG4109   16 LLVED-IMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDD--TPIEDVMT-----KNP 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489826438  81 ICVNA--SFFEVF--FTIKELPYIAVLNEQGNFYGILTHGKLLGLLQ 123
Cdd:COG4109   87 ITVTPdtSLASAAhkMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 8-62 5.26e-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: 42.59  E-value: 5.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489826438    8 IPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAAN 62
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDG-KLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 12-53 3.17e-04

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 37.49  E-value: 3.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 489826438    12 NLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYK 53
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEG-RLVGIVTR 41
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 5-119 5.87e-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: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   5 NLCIPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGGSLSDPVMS--LIKNATKH-- 80
Cdd:cd04643    1 DFLIPAEKVAHVQDTNNLEHALLVLTKSGYSRIPVLDKDY-KLVGLISLSMILDAILGLERIEFEKLSelKVEEVMNTdv 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489826438  81 --ICVNASFFEVFFTIKELPYIAVLNEQGNFYGILTHGKLL 119
Cdd:cd04643   80 ptVSPDDDLEEVLHLLVDHPFLCVVDEDGYFLGIITRREIL 120
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 12-45 6.25e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.27  E-value: 6.25e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489826438  12 NLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGE 45
Cdd:COG2905    8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGR 41
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 8-114 6.68e-04

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: 38.25  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438   8 IPKINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGEKFLGNIYKMHIYKHAANGGSLSDpvmsLIKNATKHICVNAS- 86
Cdd:cd04590    7 TPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLD----LRALLRPPLFVPETt 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489826438  87 ----FFEVFftIKELPYIA-VLNEQGNFYGILT 114
Cdd:cd04590   83 plddLLEEF--RKERSHMAiVVDEYGGTAGIVT 113
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
5-56 7.37e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 39.81  E-value: 7.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489826438   5 NLCIP------KINLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHI 56
Cdd:PRK14869 243 NQSIPvsyimtTEDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDG-KVVGVISRYHL 299
CBS_pair_bac cd09834
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 19-114 1.87e-03

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: 36.71  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  19 DATLQEAIHLLEESGYRCVPVLDEKGeKFLGNIYKMHIYKHAANGGSLSD------PVMSLIKNAT-KHICVNASFFEVF 91
Cdd:cd09834   10 DSTLRQALEKMEYHRYTAIPILNRDG-KYVGTITEGDLLWYIKNKPNLDLkdaekiSIKDIPRRRDnKPVNINANMEDLL 88

                         90       100
                 ....*....|....*....|...
gi 489826438  92 FTIKELPYIAVLNEQGNFYGILT 114
Cdd:cd09834   89 DLAMNQNFVPVVDDRGVFIGIVT 111
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 15-114 1.92e-03

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 36.74  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826438  15 TVPGDATLQEAIHLLEESGYRCVPVLDEKGEK----FLGNIYKmHIYKHAAnggSLSDPVMSLIKNATKHICVNASFFEV 90
Cdd:cd04608   14 TVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVvgmvTEGNLLS-SLLAGRA---QPSDPVSKAMYKQFKQVDLDTPLGAL 89

                         90       100
                 ....*....|....*....|....
gi 489826438  91 FFTIKELPYIAVLNEQGNFYGILT 114
Cdd:cd04608   90 SRILERDHFALVVDGQGKVLGIVT 113
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 12-45 3.33e-03

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: 35.88  E-value: 3.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489826438  12 NLTTVPGDATLQEAIHLLEESGYRCVPVLDEKGE 45
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGR 37
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 15-44 7.13e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. 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: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 35.48  E-value: 7.13e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489826438  15 TVPGDATLQEAIHLLEESGYRCVPVLDEKG 44
Cdd:cd04586    7 TVTPDTSVREAARLLLEHRISGLPVVDDDG 36
 
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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