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Conserved domains on  [gi|327439232|dbj|BAK15597|]
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predicted transcriptional regulator containing CBS domains [Solibacillus silvestris StLB046]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
198-305 5.21e-55

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 178.05  E-value: 5.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 198 MEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMI 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80
                         90       100
                 ....*....|....*....|....*...
gi 327439232 278 WEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108
DRTGG pfam07085
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ...
76-178 2.32e-33

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).


:

Pssm-ID: 429285 [Multi-domain]  Cd Length: 105  Bit Score: 121.07  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232   76 EIVNIIDGQVLGGKSGLHKTLTKFVIGAMKLDDMMRYTDAGSLLIV-GNRTQAHEYALKTG-AAVLITGGFDTTESTKDL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80
                          90       100
                  ....*....|....*....|....*
gi 327439232  154 ADELDLPIISTTYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
335-430 8.58e-08

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


:

Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 49.78  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 335 IEVEFTVTPQMTNQFGAISYGAFTILLSEVGAFALKR--RKRGEAVVENMNIYFIKPVQMESVLTVRPRILDMSRKFVKM 412
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlgGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80
                         90
                 ....*....|....*....
gi 327439232 413 DFEVYSATN-LVGKAMMTF 430
Cdd:cd03440   81 EVEVRNEDGkLVATATATF 99
HTH_ARSR super family cl46857
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
6-59 2.26e-06

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


The actual alignment was detected with superfamily member cd07377:

Pssm-ID: 481197 [Multi-domain]  Cd Length: 66  Bit Score: 44.75  E-value: 2.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 327439232   6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTI 59
Cdd:cd07377    8 DQLREAILSgeLKPGDRLpSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTF 64
 
Name Accession Description Interval E-value
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
198-305 5.21e-55

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 178.05  E-value: 5.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 198 MEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMI 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80
                         90       100
                 ....*....|....*....|....*...
gi 327439232 278 WEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
161-309 2.95e-52

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 171.63  E-value: 2.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 161 IISTTYDTFtvatminraiydqlikKDILLIEDVYVpMEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITS 240
Cdd:COG4109    4 IISTSYDTF----------------KEILLVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTS 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327439232 241 KDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQLA 309
Cdd:COG4109   67 KDILGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQKI 135
DRTGG pfam07085
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ...
76-178 2.32e-33

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).


Pssm-ID: 429285 [Multi-domain]  Cd Length: 105  Bit Score: 121.07  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232   76 EIVNIIDGQVLGGKSGLHKTLTKFVIGAMKLDDMMRYTDAGSLLIV-GNRTQAHEYALKTG-AAVLITGGFDTTESTKDL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80
                          90       100
                  ....*....|....*....|....*
gi 327439232  154 ADELDLPIISTTYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
73-244 1.39e-21

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 97.21  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  73 TFAEIVNIIDGQVL-GGKSGLHKTLtKFVIGAMKLDDMMRYTDAGSLLIVGNRTQAHEYALKTGAAVLI-TGGFDTTEST 150
Cdd:PRK14869 139 SLENIIRTLDGEVLvGAEEDKVEEG-KVVVAAMAPESLLERIEEGDIVIVGDREDIQLAAIEAGVRLLIiTGGAPVSEDV 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 151 KDLADELDLPIISTTYDTFTVATMINRAIYDQLI--KKDILliedvyvpmedtaVLKNNDTIADFHRQNRRTTHGAFPVV 228
Cdd:PRK14869 218 LELAKENGVTVISTPYDTFTTARLINQSIPVSYImtTEDLV-------------TFSKDDYLEDVKEVMLKSRYRSYPVV 284
                        170
                 ....*....|....*.
gi 327439232 229 TGQNRLVGMITSKDVI 244
Cdd:PRK14869 285 DEDGKVVGVISRYHLL 300
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
75-178 5.16e-15

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 77.18  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  75 AEIVNIIDGQVLGGKSGLHKTLTKFVIGAMKLDDMMRYTDAGSLLIV-GNRT-------QAHEYALKTGAAVLITGGFDT 146
Cdd:COG0857  217 RDLAEALGAEVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITpGDRSdillaalLAALSGTPSIAGLILTGGLPP 296
                         90       100       110
                 ....*....|....*....|....*....|....
gi 327439232 147 TESTKDLADELD--LPIISTTYDTFTVATMINRA 178
Cdd:COG0857  297 DPAVLRLAEGLGqtLPILSVELDTYTTAERLERV 330
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
203-307 1.57e-12

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: 68.95  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  203 VLKNNDTIADFHRQNRRTTHGAFPVVTGqNRLVGMITSKDV-IGKEESEPIDKVMTK-NPIAASMKTSVASAGHRMIWEG 280
Cdd:pfam00478  92 TLSPDATVADALALMERYGISGVPVVDD-GKLVGIVTNRDLrFETDLSQPVSEVMTKeNLVTAPEGTTLEEAKEILHKHK 170
                          90       100
                  ....*....|....*....|....*..
gi 327439232  281 IDLLPVIDEEGLLKGVISRQDVLKAIQ 307
Cdd:pfam00478 171 IEKLPVVDDNGRLVGLITIKDIEKAKE 197
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
200-305 4.57e-09

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 58.38  E-value: 4.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 200 DTAV-LKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIW 278
Cdd:PRK07807  97 DTPVtLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEADCAGVDRFTQVRDVMSTDLVTLPAGTDPREAFDLLEA 176
                         90       100
                 ....*....|....*....|....*..
gi 327439232 279 EGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:PRK07807 177 ARVKLAPVVDADGRLVGVLTRTGALRA 203
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
335-430 8.58e-08

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 49.78  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 335 IEVEFTVTPQMTNQFGAISYGAFTILLSEVGAFALKR--RKRGEAVVENMNIYFIKPVQMESVLTVRPRILDMSRKFVKM 412
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlgGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80
                         90
                 ....*....|....*....
gi 327439232 413 DFEVYSATN-LVGKAMMTF 430
Cdd:cd03440   81 EVEVRNEDGkLVATATATF 99
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
326-435 6.44e-07

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 48.40  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 326 EMRVMGEEDIEVEFTVTPQMTNQFGAISYGAFTILLSEVGAFALKRRKRGE--AVVENMNIYFIKPVQMESVLTVRPRIL 403
Cdd:COG2050   24 ELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGrrAVTIELNINFLRPARLGDRLTAEARVV 103
                         90       100       110
                 ....*....|....*....|....*....|...
gi 327439232 404 DMSRKFVKMDFEVYSAT-NLVGKAMMTFQLLER 435
Cdd:COG2050  104 RRGRRLAVVEVEVTDEDgKLVATATGTFAVLPK 136
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
349-425 1.87e-06

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 45.32  E-value: 1.87e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327439232  349 FGAISYGAFTILLSEVGAFALKRRKRGE--AVVENMNIYFIKPVQMESVLTVRPRILDMSRKFVKMDFEVYSATNLVGK 425
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
6-59 2.26e-06

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 44.75  E-value: 2.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 327439232   6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTI 59
Cdd:cd07377    8 DQLREAILSgeLKPGDRLpSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTF 64
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
6-78 1.49e-05

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 46.01  E-value: 1.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327439232   6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTIRIEKKKKENIERLT-FAEIV 78
Cdd:COG2188   12 DALRERIESgeLPPGDRLpSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPKIEYPLSRLTsFTEEL 88
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
200-248 9.28e-05

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: 39.80  E-value: 9.28e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 327439232   200 DTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEE 248
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
6-58 2.31e-03

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 36.01  E-value: 2.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 327439232     6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGT 58
Cdd:smart00345   3 ERLREDIVSgeLRPGDKLpSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGT 58
cas_HTH TIGR01884
CRISPR locus-related DNA-binding protein; Most but not all examples of this family are ...
7-64 2.58e-03

CRISPR locus-related DNA-binding protein; Most but not all examples of this family are associated with CRISPR loci, a combination of DNA repeats and characteristic proteins encoded near the repeat cluster. The C-terminal region of this protein is homologous to DNA-binding helix-turn-helix domains with predicted transcriptional regulatory activity. [Regulatory functions, DNA interactions, , ]


Pssm-ID: 273852 [Multi-domain]  Cd Length: 203  Bit Score: 38.88  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 327439232    7 KILQYIESLPvgdKISVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTIRIEKK 64
Cdd:TIGR01884 147 KILEVLKATG---EKSVKNIAKKLGKSLSTISRHLAELEKKGLVEQKGRKGKRYSLTK 201
 
Name Accession Description Interval E-value
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
198-305 5.21e-55

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 178.05  E-value: 5.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 198 MEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMI 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80
                         90       100
                 ....*....|....*....|....*...
gi 327439232 278 WEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
161-309 2.95e-52

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 171.63  E-value: 2.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 161 IISTTYDTFtvatminraiydqlikKDILLIEDVYVpMEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITS 240
Cdd:COG4109    4 IISTSYDTF----------------KEILLVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTS 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327439232 241 KDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQLA 309
Cdd:COG4109   67 KDILGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQKI 135
DRTGG pfam07085
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ...
76-178 2.32e-33

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).


Pssm-ID: 429285 [Multi-domain]  Cd Length: 105  Bit Score: 121.07  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232   76 EIVNIIDGQVLGGKSGLHKTLTKFVIGAMKLDDMMRYTDAGSLLIV-GNRTQAHEYALKTG-AAVLITGGFDTTESTKDL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80
                          90       100
                  ....*....|....*....|....*
gi 327439232  154 ADELDLPIISTTYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
73-244 1.39e-21

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 97.21  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  73 TFAEIVNIIDGQVL-GGKSGLHKTLtKFVIGAMKLDDMMRYTDAGSLLIVGNRTQAHEYALKTGAAVLI-TGGFDTTEST 150
Cdd:PRK14869 139 SLENIIRTLDGEVLvGAEEDKVEEG-KVVVAAMAPESLLERIEEGDIVIVGDREDIQLAAIEAGVRLLIiTGGAPVSEDV 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 151 KDLADELDLPIISTTYDTFTVATMINRAIYDQLI--KKDILliedvyvpmedtaVLKNNDTIADFHRQNRRTTHGAFPVV 228
Cdd:PRK14869 218 LELAKENGVTVISTPYDTFTTARLINQSIPVSYImtTEDLV-------------TFSKDDYLEDVKEVMLKSRYRSYPVV 284
                        170
                 ....*....|....*.
gi 327439232 229 TGQNRLVGMITSKDVI 244
Cdd:PRK14869 285 DEDGKVVGVISRYHLL 300
CBS COG0517
CBS domain [Signal transduction mechanisms];
207-307 1.21e-18

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 81.45  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 207 NDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEESE-------PIDKVMTKNPIAASMKTSVASAGHRMIWE 279
Cdd:COG0517   17 DATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEgkdlldtPVSEVMTRPPVTVSPDTSLEEAAELMEEH 96
                         90       100
                 ....*....|....*....|....*...
gi 327439232 280 GIDLLPVIDEEGLLKGVISRQDVLKAIQ 307
Cdd:COG0517   97 KIRRLPVVDDDGRLVGIITIKDLLKALL 124
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
198-304 4.89e-18

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: 79.21  E-value: 4.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 198 MEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVI------GKEESEPIDKVMTKNPIAASMKTSVAS 271
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILralvegGLALDTPVAEVMTPDVITVSPDTDLEE 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 327439232 272 AGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLK 304
Cdd:cd02205   81 ALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
208-304 2.94e-17

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: 76.98  E-value: 2.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 208 DTIADFHRQNRRTTHGAFPVVTGqNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVI 287
Cdd:cd04610   12 DTVKDVIKLIKETGHDGFPVVDD-GKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITDAARVIFRSGISKLPVV 90
                         90
                 ....*....|....*..
gi 327439232 288 DEEGLLKGVISRQDVLK 304
Cdd:cd04610   91 DDEGNLVGIITNMDVIR 107
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
189-306 1.03e-16

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 76.44  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 189 LLIEDVYVPmeDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVI------------GKEESEPIDKVM 256
Cdd:COG3448    2 MTVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLrallpdrldeleERLLDLPVEDVM 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 327439232 257 TKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:COG3448   80 TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRAL 129
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
207-306 4.57e-16

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 76.46  E-value: 4.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 207 NDTIADFHRQNRRTTHGAFPVVTGqNRLVGMITSKDVI------GKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEG 280
Cdd:COG2524  102 DTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLkalaegRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHG 180
                         90       100
                 ....*....|....*....|....*.
gi 327439232 281 IDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:COG2524  181 IGRLPVVDDDGKLVGIITRTDILRAL 206
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
75-178 5.16e-15

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 77.18  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  75 AEIVNIIDGQVLGGKSGLHKTLTKFVIGAMKLDDMMRYTDAGSLLIV-GNRT-------QAHEYALKTGAAVLITGGFDT 146
Cdd:COG0857  217 RDLAEALGAEVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITpGDRSdillaalLAALSGTPSIAGLILTGGLPP 296
                         90       100       110
                 ....*....|....*....|....*....|....
gi 327439232 147 TESTKDLADELD--LPIISTTYDTFTVATMINRA 178
Cdd:COG0857  297 DPAVLRLAEGLGqtLPILSVELDTYTTAERLERV 330
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
199-304 8.88e-14

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: 67.05  E-value: 8.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 199 EDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDV-IGKEESEPIDKVMTKN--PIAASMKTSVASAgHR 275
Cdd:cd04601    2 TDPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIrFETDLSTPVSEVMTPDerLVTAPEGITLEEA-KE 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 327439232 276 MIWEG-IDLLPVIDEEGLLKGVISRQDVLK 304
Cdd:cd04601   81 ILHKHkIEKLPIVDDNGELVGLITRKDIEK 110
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
223-306 7.10e-13

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 65.24  E-value: 7.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQNRLVGMITSKDVIGK-------EESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDeEGLLKG 295
Cdd:COG2905   31 GSLVVVDDDGRLVGIITDRDLRRRvlaegldPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVG 109
                         90
                 ....*....|.
gi 327439232 296 VISRQDVLKAI 306
Cdd:COG2905  110 IVSITDLLRAL 120
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
207-305 7.60e-13

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. 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: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 64.44  E-value: 7.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 207 NDTIADFHRQNRRTTHGAFPVVTGqNRLVGMITSKDV----IGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGID 282
Cdd:cd04595   10 DTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDVdkakHHGLGHAPVKGYMSTNVITIDPDTSLEEAQELMVEHDIG 88
                         90       100
                 ....*....|....*....|...
gi 327439232 283 LLPVIdEEGLLKGVISRQDVLKA 305
Cdd:cd04595   89 RLPVV-EEGKLVGIVTRSDVLRY 110
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
203-307 1.57e-12

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: 68.95  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  203 VLKNNDTIADFHRQNRRTTHGAFPVVTGqNRLVGMITSKDV-IGKEESEPIDKVMTK-NPIAASMKTSVASAGHRMIWEG 280
Cdd:pfam00478  92 TLSPDATVADALALMERYGISGVPVVDD-GKLVGIVTNRDLrFETDLSQPVSEVMTKeNLVTAPEGTTLEEAKEILHKHK 170
                          90       100
                  ....*....|....*....|....*..
gi 327439232  281 IDLLPVIDEEGLLKGVISRQDVLKAIQ 307
Cdd:pfam00478 171 IEKLPVVDDNGRLVGLITIKDIEKAKE 197
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
223-306 2.71e-12

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: 63.31  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQNRLVGMITSKDVI-----GKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVI 297
Cdd:cd09836   27 GSVVVVDDDGKPVGIVTERDIVravaeGIDLDTPVEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVI 106

                 ....*....
gi 327439232 298 SRQDVLKAI 306
Cdd:cd09836  107 SIRDLAREL 115
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
223-305 3.57e-12

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: 63.60  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQNRLVGMITSKDVIGKEESEPIDK-----------------------------VMTKNPIAASMKTSVASAG 273
Cdd:cd04586   27 SGLPVVDDDGKLVGIVSEGDLLRREEPGTEPRrvwwldallesperlaeeyvkahgrtvgdVMTRPVVTVSPDTPLEEAA 106
                         90       100       110
                 ....*....|....*....|....*....|..
gi 327439232 274 HRMIWEGIDLLPVIDeEGLLKGVISRQDVLKA 305
Cdd:cd04586  107 RLMERHRIKRLPVVD-DGKLVGIVSRADLLRA 137
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
219-305 5.36e-12

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: 62.20  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 219 RTTHGAFPVVTGqNRLVGMITSKDVIGKEESE----PIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDeEGLLK 294
Cdd:cd04801   25 EEKHLGYPVVEN-GRLVGIVTLEDIRKVPEVEreatRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVE-DGELV 102
                         90
                 ....*....|.
gi 327439232 295 GVISRQDVLKA 305
Cdd:cd04801  103 GIISRTDLMRA 113
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
223-305 1.75e-11

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: 60.91  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAfPVVTGQNRLVGMITSKDVIGK--------EESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIdEEGLLK 294
Cdd:cd04629   28 GA-PVVDEQGRLVGFLSEQDCLKAlleasyhcEPGGTVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVV-EDGKLV 105
                         90
                 ....*....|.
gi 327439232 295 GVISRQDVLKA 305
Cdd:cd04629  106 GQISRRDVLRA 116
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
73-177 1.03e-10

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 63.63  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232  73 TFAEIVNIIDGQVLGGKSGLHKTLTKFVIGAMKLDDMMRYTDAGSLLIV-GNRT-------QAHEYALKTgAAVLITGGF 144
Cdd:PRK05632 203 RVIDIAKHLGATVLNEGDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTpGDRSdvilaalLAAMNGPPI-AGLLLTGGY 281
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 327439232 145 DTTESTKDL---ADELDLPIISTTYDTFTVATMINR 177
Cdd:PRK05632 282 EPDPRIAKLcegAFETGLPVLSVDTNTYQTALRLQS 317
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
204-304 2.99e-10

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: 57.16  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 204 LKNNDTIAD-FHRQNRRTTHGAfPVVTGqNRLVGMITSKDvIGK-----EESEPIDKVMTKNPIAASMKTSVASAGHRMI 277
Cdd:cd04588    7 LKPDATIKDaAKLLSENNIHGA-PVVDD-GKLVGIVTLTD-IAKalaegKENAKVKDIMTKDVITIDKDEKIYDAIRLMN 83
                         90       100
                 ....*....|....*....|....*..
gi 327439232 278 WEGIDLLPVIDEEGLLKGVISRQDVLK 304
Cdd:cd04588   84 KHNIGRLIVVDDNGKPVGIITRTDILK 110
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
226-306 3.05e-10

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: 57.73  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVTGqNRLVGMITSKDVI---GKEE--------------SEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVID 288
Cdd:cd17778   35 PVVSG-GKLVGIVTAMDIVkyfGSHEakkrlttgdideaySTPVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVD 113
                         90
                 ....*....|....*...
gi 327439232 289 EEGLLKGVISRQDVLKAI 306
Cdd:cd17778  114 DEGELKGIITERDVLIAL 131
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
223-303 1.17e-09

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 55.42  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQnRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIdEEGLLKGVISRQDV 302
Cdd:cd04599   27 GGLPVVENG-KLVGIITSRDVRRAHPNRLVADAMSRNVVTISPEASLWEAKELMEEHGIERLVVV-EEGRLVGIITKSTL 104

                 .
gi 327439232 303 L 303
Cdd:cd04599  105 Y 105
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
224-305 1.18e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). 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: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 56.52  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 224 AFPVVTGQNRLVGMITSKDVIGK---EESE-------------------------------------PIDKVMTKNPIAA 263
Cdd:cd04614   29 AAPVLDSEGKLVGIVTERDLIDVsriVESEeesgmsiaddedewswegirdvmslyyptsnvelpdkPVKDVMTKDVVTA 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 327439232 264 SMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04614  109 FPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLLKA 150
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
190-302 1.67e-09

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: 55.32  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 190 LIEDVYvpMEDTAVLKNNDTIADFHRQ--NRRTTHgaFPVVTGQNRLVGMITSKDvIGK---EESEPIDKVMTKNPIAAS 264
Cdd:cd04605    1 LVEDIM--SKDVATIREDISIEEAAKImiDKNVTH--LPVVSEDGKLIGIVTSWD-ISKavaLKKDSLEEIMTRNVITAR 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 327439232 265 MKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDV 302
Cdd:cd04605   76 PDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
200-305 4.57e-09

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 58.38  E-value: 4.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 200 DTAV-LKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIW 278
Cdd:PRK07807  97 DTPVtLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEADCAGVDRFTQVRDVMSTDLVTLPAGTDPREAFDLLEA 176
                         90       100
                 ....*....|....*....|....*..
gi 327439232 279 EGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:PRK07807 177 ARVKLAPVVDADGRLVGVLTRTGALRA 203
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
199-306 5.56e-09

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: 53.70  E-value: 5.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 199 EDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKD----VIGKE---ESEPIDKVMTKNPIAASMKTSVAS 271
Cdd:cd17775    3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDivveVVAKGldpKDVTVGDIMSADLITAREDDGLFE 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 327439232 272 AGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd17775   83 ALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
218-305 7.05e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; 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: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 53.12  E-value: 7.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 218 RRTTHGAFPVVTGQN-RLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLkGV 296
Cdd:cd04638   22 KKKAISGVPVVKKETgKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDKLV-GI 100

                 ....*....
gi 327439232 297 ISRQDVLKA 305
Cdd:cd04638  101 VTVADLVRA 109
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
252-328 7.97e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 53.72  E-value: 7.97e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327439232 252 IDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQLAQRQPQHGETIDDLVKNEMR 328
Cdd:COG3448    4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVEDVMT 80
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
197-305 1.28e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. 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: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 52.96  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 197 PMEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIG--KEES----EPIDKVMTKNPIAASMKTSVA 270
Cdd:cd04613    1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGvlFEEElwdlVVVKDLATTDVITVTPDDDLY 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 327439232 271 SAGHRMIWEGIDLLPVIDEE--GLLKGVISRQDVLKA 305
Cdd:cd04613   81 TALLKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVIAA 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
252-306 1.42e-08

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: 50.67  E-value: 1.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 327439232  252 IDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRAL 55
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
223-304 2.97e-08

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: 51.65  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQNRLVGMITSKDVI------GKE-ESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLkG 295
Cdd:cd04623   26 GALVVVDDGGRLVGILSERDYVrklalrGASsLDTPVSEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVEDGKLV-G 104

                 ....*....
gi 327439232 296 VISRQDVLK 304
Cdd:cd04623  105 IVSIGDVVK 113
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
227-304 3.16e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) 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: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 51.29  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMITSKDV---I--GKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQD 301
Cdd:cd04607   30 VVDENRKLLGTVTDGDIrrgLlkGLSLDAPVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDD 109

                 ...
gi 327439232 302 VLK 304
Cdd:cd04607  110 LLA 112
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
227-298 3.48e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 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: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 51.43  E-value: 3.48e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327439232 227 VVTGQNRLVGMITSKD----VIGKE---ESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVIS 298
Cdd:cd17781   30 VVDDDGGLSGIFTDKDlarrVVASGldpRSTLVSSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVLD 108
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
227-306 6.99e-08

CBS pair domains found in archeal proteins, repeat 1; 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: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 51.19  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMITSKDVI-----GKE----------------ESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLP 285
Cdd:cd17777   37 VVVDENKLEGILSARDLVsylggGCLfkivesrhqgdlysalNREVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLP 116
                         90       100
                 ....*....|....*....|.
gi 327439232 286 VIDEEGLLKGVISRQDVLKAI 306
Cdd:cd17777  117 VVDRDGRPVGIVTERDLVLYL 137
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
335-430 8.58e-08

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 49.78  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 335 IEVEFTVTPQMTNQFGAISYGAFTILLSEVGAFALKR--RKRGEAVVENMNIYFIKPVQMESVLTVRPRILDMSRKFVKM 412
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlgGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80
                         90
                 ....*....|....*....
gi 327439232 413 DFEVYSATN-LVGKAMMTF 430
Cdd:cd03440   81 EVEVRNEDGkLVATATATF 99
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
226-306 1.01e-07

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: 50.69  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVtGQNRLVGMITSKDVI---GKEE--------------SEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVID 288
Cdd:cd04631   35 PVV-SDGKLVGIVTSTDIMrylGSGEafeklktgnihevlNVPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVD 113
                         90
                 ....*....|....*...
gi 327439232 289 eEGLLKGVISRQDVLKAI 306
Cdd:cd04631  114 -DGKLVGIITERDILRAI 130
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
218-304 1.06e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 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: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 50.32  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 218 RRTThgAFPVVTGQNRLVGMITSKD----VIGKE---ESEPIDKVMTKNPIAASMKTSVASAGHRMIwEGIDL-LPVIDE 289
Cdd:cd17782   23 NRTT--AVLVMDNSGKVIGIFTSKDvvlrVLAAGldpATTSVVRVMTPNPETAPPSTTILDALHKMH-EGKFLnLPVVDD 99
                         90
                 ....*....|....*
gi 327439232 290 EGLLKGVIsrqDVLK 304
Cdd:cd17782  100 EGEIVGLV---DVLQ 111
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
227-299 1.26e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing 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: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 49.82  E-value: 1.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327439232 227 VVTGQNRLVGMITSKDV-IGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISR 299
Cdd:cd04583   30 VVDKDNVLLGIVDIEDInRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTR 103
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
207-298 1.30e-07

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. 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: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 49.73  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 207 NDTIADFHRQNRRTTHGAFPVVtGQNRLVGMITSKD-VI-----GKE-ESEPIDKVMTKNPIAASMKTSVASAGHRMIWE 279
Cdd:cd04622   11 DTTLREAARLMRDLDIGALPVC-EGDRLVGMVTDRDiVVravaeGKDpNTTTVREVMTGDVVTCSPDDDVEEAARLMAEH 89
                         90
                 ....*....|....*....
gi 327439232 280 GIDLLPVIDEEGLLKGVIS 298
Cdd:cd04622   90 QVRRLPVVDDDGRLVGIVS 108
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 ...
227-305 1.91e-07

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: 49.35  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMITSKD----VI--GKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDeEGLLKGVISRQ 300
Cdd:cd04587   31 LVVDDGRLVGIVTDRDlrnrVVaeGLDPDTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVD-DGRVVGVVTAT 109

                 ....*
gi 327439232 301 DVLKA 305
Cdd:cd04587  110 DLMRL 114
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
199-305 2.30e-07

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 53.05  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 199 EDTAVLKNNDTIADFHRQNRRTTHGAFPV-VTGQ--NRLVGMITSKDVI-GKEESEPIDKVMT--KNPIAASMKTSVASA 272
Cdd:PTZ00314 104 MDPYVLSPNHTVADVLEIKEKKGFSSILItVDGKvgGKLLGIVTSRDIDfVKDKSTPVSEVMTprEKLVVGNTPISLEEA 183
                         90       100       110
                 ....*....|....*....|....*....|...
gi 327439232 273 GHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:PTZ00314 184 NEVLRESRKGKLPIVNDNGELVALVSRSDLKKN 216
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
226-306 4.70e-07

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: 48.77  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVV-TGQNRLVGMITSKDVI----GKEES----------------EPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLL 284
Cdd:cd17779   35 PVAdAGTKRLEGIVTSMDIVdflgGGSKYnlvekkhngnllaainEPVREIMTRDVISVKENASIDDAIELMLEKNVGGL 114
                         90       100
                 ....*....|....*....|..
gi 327439232 285 PVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd17779  115 PIVDKDGKVIGIVTERDFLKFL 136
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
326-435 6.44e-07

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 48.40  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 326 EMRVMGEEDIEVEFTVTPQMTNQFGAISYGAFTILLSEVGAFALKRRKRGE--AVVENMNIYFIKPVQMESVLTVRPRIL 403
Cdd:COG2050   24 ELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGrrAVTIELNINFLRPARLGDRLTAEARVV 103
                         90       100       110
                 ....*....|....*....|....*....|...
gi 327439232 404 DMSRKFVKMDFEVYSAT-NLVGKAMMTFQLLER 435
Cdd:COG2050  104 RRGRRLAVVEVEVTDEDgKLVATATGTFAVLPK 136
PRK07107 PRK07107
IMP dehydrogenase;
204-301 8.73e-07

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 51.24  E-value: 8.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 204 LKNNDTIADFHRQNRRTTHGAFPVV---TGQNRLVGMITSKDV-IGKEE-SEPIDKVMT--KNPIAASMKTSVASAgHRM 276
Cdd:PRK07107 110 LTPDNTLADVLDLKEKTGHSTVAVTedgTAHGKLLGIVTSRDYrISRMSlDTKVKDFMTpfEKLVTANEGTTLKEA-NDI 188
                         90       100
                 ....*....|....*....|....*.
gi 327439232 277 IWEG-IDLLPVIDEEGLLKGVISRQD 301
Cdd:PRK07107 189 IWDHkLNTLPIVDKNGNLVYLVFRKD 214
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
197-305 9.11e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 48.24  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 197 PMEDTAVLKNNDTIAD---FHRQNRRTthgAFPVVTGQNRLVGMITSKDV------------------------------ 243
Cdd:cd17789    1 PKGKLHVVKPNTTVDEaleLLVENRIT---GLPVIDEDWRLVGVVSDYDLlaldsisgrsqtdnnfppadstwktfnevq 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327439232 244 --IGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd17789   78 klLSKTNGKVVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVRA 141
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
256-306 1.47e-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: 46.66  E-value: 1.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 327439232 256 MTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKAL 51
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
349-425 1.87e-06

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 45.32  E-value: 1.87e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327439232  349 FGAISYGAFTILLSEVGAFALKRRKRGE--AVVENMNIYFIKPVQMESVLTVRPRILDMSRKFVKMDFEVYSATNLVGK 425
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
6-59 2.26e-06

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 44.75  E-value: 2.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 327439232   6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTI 59
Cdd:cd07377    8 DQLREAILSgeLKPGDRLpSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTF 64
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
226-306 2.28e-06

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: 46.65  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVTGqNRLVGMITSKDVI--------GKEESE--------PIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDe 289
Cdd:cd04584   35 PVVDD-GKLVGIVTDRDLLraspskatSLSIYElnyllskiPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVD- 112
                         90
                 ....*....|....*..
gi 327439232 290 EGLLKGVISRQDVLKAI 306
Cdd:cd04584  113 GGKLVGIITETDILRAF 129
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
252-305 3.07e-06

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: 46.26  E-value: 3.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 327439232 252 IDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDeEGLLKGVISRQDVLKA 305
Cdd:cd04584    2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRA 54
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
199-307 3.30e-06

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 48.91  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 199 EDTA---------VLKNNDTIADFHRQNRR------TTHGAFpVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAA 263
Cdd:COG2239  128 EDSAgrlmttefvAVREDWTVGEALRYLRRqaedpeTIYYIY-VVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISV 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 327439232 264 SMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQ 307
Cdd:COG2239  207 PADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVIE 250
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
256-313 3.35e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. 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: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 46.40  E-value: 3.35e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 327439232 256 MTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQLAQRQP 313
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRG 58
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
199-305 3.64e-06

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: 46.17  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 199 EDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVI---------------GKEE----SEPIDKVMTKN 259
Cdd:cd04632    2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVdfvvrpgtktrggdrGGEKermlDLPVYDIMSSP 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 327439232 260 PIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04632   82 VVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
157-308 5.47e-06

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 48.51  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 157 LDLPIISTTYDTFTVATMI--------------NRAIYDQLikkDILLIEDVYVP--MEDTAVLKNNDTIAD-FHRQNRR 219
Cdd:PLN02274  53 LSIPCVSSPMDTVTESDMAiamaalggigivhyNNTAEEQA---AIVRKAKSRRVgfVSDPVVKSPSSTISSlDELKASR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 220 TTHGAFPVVTGQ--NRLVGMITSKDVIG-KEESEPIDKVMTKNP--IAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLK 294
Cdd:PLN02274 130 GFSSVCVTETGTmgSKLLGYVTKRDWDFvNDRETKLSEVMTSDDdlVTAPAGIDLEEAEAVLKDSKKGKLPLVNEDGELV 209
                        170
                 ....*....|....
gi 327439232 295 GVISRQDVLKAIQL 308
Cdd:PLN02274 210 DLVTRTDVKRVKGY 223
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
243-334 6.64e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.80  E-value: 6.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 243 VIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDeEGLLKGVISRQDVLKAiqLAQRQPQHGETIDDL 322
Cdd:COG2524   79 ELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKA--LAEGRDLLDAPVSDI 155
                         90
                 ....*....|..
gi 327439232 323 VKNEMRVMGEED 334
Cdd:COG2524  156 MTRDVVTVSEDD 167
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
190-305 1.10e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. 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: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 44.43  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 190 LIEDVYVPmeDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQ--NRLVGMITSKDV---IGKEESEPIDKvmtkNPIAAS 264
Cdd:cd04591    1 TAEDVMRP--PLTVLARDETVGDIVSVLKTTDHNGFPVVDSTesQTLVGFILRSQLillLEADLRPIMDP----SPFTVT 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 327439232 265 MKTSVASAgHRMIWE-GIDLLPVIDEeGLLKGVISRQDVLKA 305
Cdd:cd04591   75 EETSLEKV-HDLFRLlGLRHLLVTNN-GRLVGIVTRKDLLRA 114
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
226-306 1.37e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 44.25  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVTGQNRLVGMITSKDVIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04606   41 YVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDV 120

                 .
gi 327439232 306 I 306
Cdd:cd04606  121 I 121
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
6-78 1.49e-05

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 46.01  E-value: 1.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327439232   6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTIRIEKKKKENIERLT-FAEIV 78
Cdd:COG2188   12 DALRERIESgeLPPGDRLpSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPKIEYPLSRLTsFTEEL 88
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
227-304 2.56e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 43.52  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMITSKDV------IGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQ 300
Cdd:cd04604   41 VVDEDGRLVGIITDGDLrralekGLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLH 120

                 ....
gi 327439232 301 DVLK 304
Cdd:cd04604  121 DLLR 124
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
252-313 2.71e-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: 2.71e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327439232 252 IDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQLAQRQP 313
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDP 62
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
200-248 9.28e-05

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: 39.80  E-value: 9.28e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 327439232   200 DTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVIGKEE 248
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
227-299 9.36e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; 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: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 41.70  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMITSKD----VIGKE--ESEPIDKVMTKNP--IAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVIS 298
Cdd:cd04617   32 VVDEEGYLVGVVSRKDllkaTLGGQdlEKTPVSMIMTRMPniVTVTPDDSVLEAARKLIEHEIDSLPVVEKEDGKLKVVG 111

                 .
gi 327439232 299 R 299
Cdd:cd04617  112 R 112
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
224-305 1.28e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. 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: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 41.78  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 224 AFPVVTGQNRLVGMITSKDVIGKEESEPIDKV------------MTKNPIAASMKTSVASAGHRM-IWE--------GID 282
Cdd:cd04600   28 ALPVVDRARRLVGIVTLADLLKHADLDPPRGLrgrlrrtlglrrDRPETVGDIMTRPVVTVRPDTpIAElvplfsdgGLH 107
                         90       100
                 ....*....|....*....|...
gi 327439232 283 LLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04600  108 HIPVVDADGRLVGIVTQSDLIAA 130
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
255-308 1.63e-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: 41.07  E-value: 1.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 327439232 255 VMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQL 308
Cdd:cd04605    5 IMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVAL 58
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
256-333 2.17e-04

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: 41.26  E-value: 2.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327439232 256 MTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKaiQLAQRQPQHGETIDDLVKNEMRVMGEE 333
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLR--REEPGTEPRRVWWLDALLESPERLAEE 76
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
223-306 2.49e-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: 40.48  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQNRLVGMITSKDV---IGKEESEP---IDKVMTKNPIAASMKTSVASAGHRMIWEG-----IDLLPVIDEEG 291
Cdd:cd17784   26 SALPVVDDEGKLIGIVTATDLghnLILDKYELgttVEEVMVKDVATVHPDETLLEAIKKMDSNApdeeiINQLPVVDDGK 105
                         90
                 ....*....|....*
gi 327439232 292 LLkGVISRQDVLKAI 306
Cdd:cd17784  106 LV-GIISDGDIIRAI 119
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
227-305 3.42e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing 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: 341402 [Multi-domain]  Cd Length: 116  Bit Score: 40.24  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMIT--SKDVIGKEESEPIDKVMTKNPIAASMKTS-------VASAGhrmiWEgidlLPVIDEEGLLKGVI 297
Cdd:cd09831   35 VVDKKRRFLGVVSvdSLRAALKENAQSLEDAFLTDVETVPADTSlsdilglVASAP----CP----LPVVDEDGRYLGVI 106

                 ....*...
gi 327439232 298 SRQDVLKA 305
Cdd:cd09831  107 SKASLLET 114
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
191-303 3.57e-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: 40.17  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 191 IEDVYVPMEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQ-NRLVGMITSKDVIG----KEESEPIDKVMTKnPIAASM 265
Cdd:cd04590    2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDLLAalleGREKLDLRALLRP-PLFVPE 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 327439232 266 KTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVL 303
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
3-58 3.80e-04

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 42.51  E-value: 3.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327439232   3 TKHEKILQYIES------LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGT 58
Cdd:COG1167   12 PLYLQLADALREailsgrLPPGDRLpSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGT 74
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
257-306 4.44e-04

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: 39.54  E-value: 4.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 327439232 257 TKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRAL 50
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
196-244 5.99e-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: 37.58  E-value: 5.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 327439232  196 VPMEDTAVLKNNDTIADFHRQNRRTTHGAFPVVTGQNRLVGMITSKDVI 244
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLL 52
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
259-307 7.19e-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: 37.11  E-value: 7.19e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 327439232   259 NPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQ 307
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
219-305 8.52e-04

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 41.29  E-value: 8.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 219 RTTHGAFPVVTGQNRLVGMITSKD-----VIGKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLL 293
Cdd:PRK11543 227 RTGLGLVAVCDAQQQVQGVFTDGDlrrwlVGGGALTTPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENGKL 306
                         90
                 ....*....|..
gi 327439232 294 KGVISRQDVLKA 305
Cdd:PRK11543 307 TGAINLQDFYQA 318
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
199-306 1.02e-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: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 38.71  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 199 EDTAVLKNNDTIADF-------HRQNRRtthgaFPVVTGQNRLVGMITSKDVIGKEESE----PIDKVMTknPIAASM-- 265
Cdd:cd04639    5 TEFPIVDADLTLREFaddyligKKSWRE-----FLVTDEAGRLVGLITVDDLRAIPTSQwpdtPVRELMK--PLEEIPtv 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 327439232 266 --KTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd04639   78 aaDQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIELL 120
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
226-306 1.14e-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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 39.02  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVTGQNRLVGMITSKDVIGKE------ESEPIDK-----VMTKNPIAASMKTSVASAGHRMIWEGidLLPVIDEEGLLK 294
Cdd:cd04643   34 PVLDKDYKLVGLISLSMILDAIlgleriEFEKLSElkveeVMNTDVPTVSPDDDLEEVLHLLVDHP--FLCVVDEDGYFL 111
                         90
                 ....*....|..
gi 327439232 295 GVISRQDVLKAI 306
Cdd:cd04643  112 GIITRREILKAV 123
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
256-306 1.19e-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: 38.66  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 327439232 256 MTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAV 51
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
226-304 1.37e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS 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.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 38.10  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVTGQNRLVGMITSKDVigkeeSEPIDKVMTK-NPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLK 304
Cdd:cd04597   32 PVTDDNGKLIGLLSISDI-----ARTVDYIMTKdNLIVFKEDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
257-327 1.99e-03

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: 38.08  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327439232 257 TKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAIQLAQRQPQHGE-------TIDDLVKNEM 327
Cdd:cd04632    1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGGDrggekerMLDLPVYDIM 78
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
223-303 2.00e-03

CBS domain protein; 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 37.68  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 223 GAFPVVTGQNRLVGMITSKDVI------GKEESEPIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDeEGLLKGV 296
Cdd:cd17771   28 GSMVVVDANRRPVGIFTLRDLLsrvalpQIDLDAPISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVD-NGRLVGV 106

                 ....*..
gi 327439232 297 ISRQDVL 303
Cdd:cd17771  107 VSERDLF 113
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
252-306 2.14e-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: 37.90  E-value: 2.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 327439232 252 IDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKAI 306
Cdd:cd04608    4 VRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSL 58
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
260-305 2.21e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; 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: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 37.85  E-value: 2.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 327439232 260 PIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:cd04617    6 PVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKA 51
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
336-421 2.23e-03

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 37.59  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 336 EVEFTVTPQMTNQFGAISYG--------AFTILLSEVGAFALKRRKRGEA-VVENMNIYFIKPVQMESVLTVRPRILDMS 406
Cdd:cd00586    2 TLEIRVRFGDTDAAGHVNNArylryfeeAREEFLRELGLGYDELEEQGLGlVVVELEIDYLRPLRLGDRLTVETRVLRLG 81
                         90
                 ....*....|....*
gi 327439232 407 RKFVKMDFEVYSATN 421
Cdd:cd00586   82 RKSFTFEQEIFREDG 96
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
6-58 2.31e-03

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 36.01  E-value: 2.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 327439232     6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGT 58
Cdd:smart00345   3 ERLREDIVSgeLRPGDKLpSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGT 58
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
330-421 2.51e-03

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 37.96  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 330 MGEEDIEVEFTVTPQMTNQFGAISYGAF--------TILLSEVGAFALKRRKRGEA-VVENMNIYFIKPVQMESVLTVRP 400
Cdd:COG0824    1 MTLFTFETPIRVRFGDTDAMGHVNNANYlryfeearTEFLRALGLSYAELEEEGIGlVVVEAEIDYLRPARYGDELTVET 80
                         90       100
                 ....*....|....*....|.
gi 327439232 401 RILDMSRKFVKMDFEVYSATN 421
Cdd:COG0824   81 RVVRLGGSSLTFEYEIFRADD 101
cas_HTH TIGR01884
CRISPR locus-related DNA-binding protein; Most but not all examples of this family are ...
7-64 2.58e-03

CRISPR locus-related DNA-binding protein; Most but not all examples of this family are associated with CRISPR loci, a combination of DNA repeats and characteristic proteins encoded near the repeat cluster. The C-terminal region of this protein is homologous to DNA-binding helix-turn-helix domains with predicted transcriptional regulatory activity. [Regulatory functions, DNA interactions, , ]


Pssm-ID: 273852 [Multi-domain]  Cd Length: 203  Bit Score: 38.88  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 327439232    7 KILQYIESLPvgdKISVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTIRIEKK 64
Cdd:TIGR01884 147 KILEVLKATG---EKSVKNIAKKLGKSLSTISRHLAELEKKGLVEQKGRKGKRYSLTK 201
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
227-305 2.72e-03

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: 37.38  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 227 VVTGQNRLVGMITSKDVI------GKEESE-PIDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLkGVISR 299
Cdd:cd17776   30 VVTDDGTPAGILTETDALhagyatDDPFSEiPVRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLDLV-GILTA 108

                 ....*.
gi 327439232 300 QDVLKA 305
Cdd:cd17776  109 TDIIRA 114
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
255-305 3.61e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 39.43  E-value: 3.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 327439232 255 VMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDVLKA 305
Cdd:PRK14869  73 LEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARA 123
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
252-304 3.77e-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: 37.21  E-value: 3.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 327439232 252 IDKVMTKNPIAASMKTSVASAGHRMIWEGIDLLPVIdEEGLLKGVISRQDVLK 304
Cdd:cd04631    2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIMR 53
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
264-310 5.54e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. 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: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 36.32  E-value: 5.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 327439232 264 SMKTSVASAGHRMIWEGIDLLPVIDEEGLLkGVISRQDVLKAIQLAQ 310
Cdd:cd04595    8 SPDTTIEEARKIMLRYGHTGLPVVEDGKLV-GIISRRDVDKAKHHGL 53
COG2512 COG2512
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ...
1-73 5.82e-03

Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only];


Pssm-ID: 442002 [Multi-domain]  Cd Length: 80  Bit Score: 35.66  E-value: 5.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327439232   1 MSTKHEKILQYIESlpVGDKISVRQIAKEMQVSEGTAYRAIKEAENRrlvssiervGTIRIEKKKKENIERLT 73
Cdd:COG2512   13 LLEDERRVLELLRE--NGGRMTQSEIVKETGWSKSKVSRLLSRLEER---------GLIEKERVGRENVVELP 74
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
257-302 9.36e-03

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: 36.25  E-value: 9.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 327439232 257 TKNPIAASMKTSVASAGHRMIWEGIDLLPVIDEEGLLKGVISRQDV 302
Cdd:cd17784    1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDL 46
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
226-305 9.79e-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: 35.97  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327439232 226 PVVTGQNRLVGMITSKDVI-----GKEE-SEPIDKVMTKNPIAASMKTSVAsaghrmiwegiDLLP---------VIDEE 290
Cdd:cd04608   37 PVVDEDGRVVGMVTEGNLLssllaGRAQpSDPVSKAMYKQFKQVDLDTPLG-----------ALSRilerdhfalVVDGQ 105
                         90
                 ....*....|....*
gi 327439232 291 GLLKGVISRQDVLKA 305
Cdd:cd04608  106 GKVLGIVTRIDLLNY 120
 
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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