NCBI Conserved Domain Search

Monocarboxylate transporter-homologous (Mch) 1 protein and similar transporters of the Major Facilitator Superfamily of transporters; Yeast monocarboxylate transporter-homologous (Mch) proteins are putative transporters that do not transport monocarboxylic acids across the plasma membrane, and may play roles distinct from their mammalian counterparts. Their function has not been determined. The Mch1p-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

Pssm-ID: 340912 [Multi-domain] Cd Length: 385 Bit Score: 412.42 E-value: 5.23e-135

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  546 RWLVFVCAMWIQSVAGVGYLFGgSMSPAIKTSLGYNQKQIALLGVAKNLGDAIGFVSGALSEVSPSWVVLLVGATQNLVG 625
Cdd:cd17354      2 RWLSFVAALWSQLSAGSIYLFS-LYSPPLKSTLGYSQQQNNLLSVAKDLGYLVGPLLGLLSDRLGPWLLLLIGAILFFPG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  626 YGVVWLVVTGQLPNLPLWMLFVAIFVGTNGETYYNTASLVSCIHNFPESRGPVVGILKGFSGLSGAILTQVYLMFNPSHD 705
Cdd:cd17354     81 YGVLWLVVTGLISDLSFWLMCLCFFLIGNSTSSLYTAALVTCAKNFPESRGLAIGIPKGCYGLSGAIGSQLYKALFFHDS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  706 SSVILMVALGPPVVVLALLFIVRPVERSCRmnlrsddlrflaiygfcvvlavyllgllvlqslvdmtqtiittsgailvi 785
Cdd:cd17354    161 ARVFLFLAVLPAVVGLLAWFSVRIVSIEEG-------------------------------------------------- 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  786 fmvvpvlvpfssvfisgnnvtlvkpeegtsnvdqnevktliersdippekkrapcigedftllQALGQADFWLIFMSLVL 865
Cdd:cd17354    191 ---------------------------------------------------------------EFLKDIDFWLLFISLFL 207

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  866 GVGSGITVIDNLGQICYSL-GYNNTKIFVSLISISNFLGRVAGGYFSELIIRKLSLPRTLAMSVVQAIMSLGLIYYAIDW 944
Cdd:cd17354    208 GVGPGEMFINNLGQIGQSLtGPSNTSTLVSLFSIFSFLGRLLSGLLSDLFVRKFRLPRPSRMVLLLLILSLGHLLQAFGL 287

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  945 P-GKIYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSFVFSGVIASNIYDYyarkqAGPTTETESL 1023
Cdd:cd17354    288 PsGALYVASALIGFGYGGLFSIAPTIVSELFGLKNFGTNYGFLMLAPAIGSLIFSVIYAGVYYDN-----GGEGAGSDDL 362


                   ....*.
gi 1901200332 1024 VCTGSD 1029
Cdd:cd17354    363 SCIGPH 368

Nodulin-like; This family represents a conserved region within plant nodulin-like proteins.

Pssm-ID: 284279 Cd Length: 250 Bit Score: 358.58 E-value: 1.92e-116

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  546 RWLVFVCAMWIQSVAGVGYLFGgSMSPAIKTSLGYNQKQIALLGVAKNLGDAIGFVSGALSEVSPSWVVLLVGATQNLVG 625
Cdd:pfam06813    1 RWLVLVAAIWIQSIAGANYDFS-AYSSALKSSLGYSQVQLNLLGVAKDLGKNFGWLSGLASEYLPPWVVLLVGAAMGLVG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  626 YGVVWLVVTGQLPNLPLWMLFVAIFVGTNGETYYNTASLVSCIHNFPESRGPVVGILKGFSGLSGAILTQVYLMFNPSHD 705
Cdd:pfam06813   80 YGVQWLVVTGRIPGLPYWLMFLCICLAGNSICWFNTASLVTCIRNFPESRGVVLGLLKGYAGLSGAIYTQLYTAIYGSDA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  706 SSVILMVALGPPVVVLALLFIVRPVERSC-RMNLRSDDLRFLAIYGFCVVLAVYLLGLLVLQSLVDMTQTIITTSGAILV 784
Cdd:pfam06813  160 KSLLLLNALVPLVVSLVALYFVRPCPPSPsVGERRSEDRVFLVLNVISVLLAVYLLVMSILSKFSDLSSARIYASAAILV 239

                          250
                   ....*....|.
gi 1901200332  785 IFMVVPVLVPF 795
Cdd:pfam06813  240 LLLLVPLAVPI 250

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: 183.94 E-value: 4.35e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd17781      3 PALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSATDA 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1901200332  150 LQKMVQGKFRHLPVVE-NGEVIALLDIAKCLYDAIA 184
Cdd:cd17781     83 LDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118

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: 161.26 E-value: 3.85e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVM-VENKLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAIV 315
Cdd:cd17782      1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMdNSGKVIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTIL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1901200332  316 EALHIMHNGKFLHLPVLDKDGDVVAVIDVIHITHAAVT 353
Cdd:cd17782     81 DALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ 118

The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

Pssm-ID: 99730 Cd Length: 86 Bit Score: 136.29 E-value: 8.20e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  414 FAFKLQDKKGRMHRFMCE-TQSLTTLITAILQRMGDDIEPDNLPQIMYEDEDNDKVVLASDNDLGAAVEHAKSIGWKGLK 492
Cdd:cd06409      1 FAFKFKDPKGRVHRFRLRpSESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80


                   ....*.
gi 1901200332  493 LHLDYT 498
Cdd:cd06409     81 LHLHYP 86

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 123.40 E-value: 6.64e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:COG2905      8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEA 87

                           90       100
                   ....*....|....*....|....*.
gi 1901200332  150 LQKMVQGKFRHLPVVENGEVIALLDI 175
Cdd:COG2905     88 LELMEEHRIRHLPVVDDGKLVGIVSI 113

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: 108.66 E-value: 7.51e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQ 151
Cdd:cd04623      5 VTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMA 84

                           90       100
                   ....*....|....*....|....
gi 1901200332  152 KMVQGKFRHLPVVENGEVIALLDI 175
Cdd:cd04623     85 LMTERRIRHLPVVEDGKLVGIVSI 108

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: 107.51 E-value: 1.81e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALlCGILTDRDIATKVIAKQLNLEeTPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd04587      5 PPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRL-VGIVTDRDLRNRVVAEGLDPD-TPVSEIMTPPPVTIDADALVFEA 82

                           90       100
                   ....*....|....*....|.
gi 1901200332  150 LQKMVQGKFRHLPVVENGEVI 170
Cdd:cd04587     83 LLLMLERNIHHLPVVDDGRVV 103

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: 106.95 E-value: 4.11e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd17782      3 PPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTILDA 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1901200332  150 LQKMVQGKFRHLPVVEN-GEVIALLDIAKCLYDAIA 184
Cdd:cd17782     83 LHKMHEGKFLNLPVVDDeGEIVGLVDVLQLTYATLQ 118

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: 105.75 E-value: 9.66e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  228 PSLSTIIPENTkvlkvgldeTVLGVTMKMVEYQSSAAMVMVEN-KLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPE 306
Cdd:cd17781      1 PSPALTVPETT---------TVAEAAQLMAAKRTDAVLVVDDDgGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPL 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1901200332  307 SATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVIDV 344
Cdd:cd17781     72 CVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVLDI 109

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 102.25 E-value: 2.19e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   62 TVKRLRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVL 141
Cdd:COG0517      2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVS 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1901200332  142 SDTIAVEALQKMVQGKFRHLPVVENGE----VIALLDIAKCLYDAIA 184
Cdd:COG0517     82 PDTSLEEAAELMEEHKIRRLPVVDDDGrlvgIITIKDLLKALLEPLA 128

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: 94.79 E-value: 5.78e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALlCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:cd04622      7 TVSPDTTLREAARLMRDLDIGALPVCEGDRL-VGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARL 85

                           90       100
                   ....*....|....*....|....*...
gi 1901200332  153 MVQGKFRHLPVVENGE----VIALLDIA 176
Cdd:cd04622     86 MAEHQVRRLPVVDDDGrlvgIVSLGDLA 113

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: 92.59 E-value: 3.82e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIaTKVIAKQLNLEeTPVSKVMTKNPVFVLSDTIAVEALQ 151
Cdd:cd09836      6 VTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI-VRAVAEGIDLD-TPVEEIMTKNLVTVSPDESIYEAAE 83

                           90       100       110
                   ....*....|....*....|....*....|
gi 1901200332  152 KMVQGKFRHLPVVENGE----VIALLDIAK 177
Cdd:cd09836     84 LMREHNIRHLPVVDGGGklvgVISIRDLAR 113

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 91.08 E-value: 1.71e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVEN-KLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAIV 315
Cdd:COG0517      8 TTDVVTVSPDATVREALELMSEKRIGGLPVVDEDgKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLE 87

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1901200332  316 EALHIMHNGKFLHLPVLDKDGDVVAVIDVIHITHAAV 352
Cdd:COG0517     88 EAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

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: 88.84 E-value: 6.35e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEeTPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd02205      3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALD-TPVAEVMTPDVITVSPDTDLEEA 81

                           90       100
                   ....*....|....*....|....*
gi 1901200332  150 LQKMVQGKFRHLPVV-ENGEVIALL 173
Cdd:cd02205     82 LELMLEHGIRRLPVVdDDGKLVGIV 106

Oxalate:formate antiporter (OFA) and similar proteins of the Major Facilitator Superfamily of transporters; This subfamily is composed of Oxalobacter formigenes oxalate:formate antiporter (OFA or OxlT) and similar proteins. O. formigenes, a commensal found in the gut of animals and humans, plays an important role in clearing dietary oxalate from the intestinal tract, which is carried out by OFA/OxlT, an anion transporter that facilitates the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation. This exchange generates an electrochemical proton gradient and is the source of energy for ATP synthesis in this cell. The OFA-like subfamily belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

Pssm-ID: 340911 [Multi-domain] Cd Length: 389 Bit Score: 96.14 E-value: 7.62e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  546 RWLVFVCAMWIQSVAGVGYLFGgSMSPAIKTSLGYNQKQIAL-LGVAKNLGDAIGFVSGALSE-VSPSWVVLLVGAtqnL 623
Cdd:cd17353      2 RWLVLLGAVLMHLILGYQYAWS-VFNPPLSSALGWSLASVALaFTLTIVFLAISAPFAGRLVDrGGPRKAILIGGI---L 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  624 VGYGvvwLVVTGQLPNLPLWMLFVAIFVGT-NGETYyntASLVSCIHN-FPESRGPVVGILKGFSGLSGAIltqvylmFN 701
Cdd:cd17353     78 FGLG---FILSAFAISLPLLFLGYGVLGGIgAGIGY---ITPVSTAVKwFPDKRGLATGIVIAGFGLGSLI-------FS 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  702 PshdssviLMVALGPPVVVLALLFIvrpverscrmnlrsddlrfLAIYGFCVVLavyllgllvlqslvdmtqtiittsga 781
Cdd:cd17353    145 P-------LIAYLINTVGVPTTFLI-------------------LGIIFLIIIV-------------------------- 172

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  782 ILVIFMVVPVlvpfssvfisgnnvTLVKPEEGTSNVDQNEVKTliersdippekkrapcigEDFTLLQALGQADFWLIFM 861
Cdd:cd17353    173 IGAFLIRDPP--------------KGWVPPGVDPLANNAENSP------------------RDYTPREMLRTPTFWLLWL 220

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  862 SLVLGVGSGITVIDNLGQICYSLGYNNTKI---FVSLISISNFLGRVAGGYFSELIIRKLSLprtLAMSVVQAIMSLGLI 938
Cdd:cd17353    221 MFFLNATAGLMLIGQAKPIGQEFAGLDAGIaalAVSILSIFNGGGRPFWGWLSDKIGRKNTL---SIAFLIQGVAMFLLP 297

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  939 YYAIDwPGKIYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSFVfsGVIASNIYDY 1008
Cdd:cd17353    298 FIGSV-AVLFVLGVALIGFCYGGGFALFPALTADFFGTKNAGTNYGLLYTAKGVGGLI--GPIIAAYVLY 364

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 89.12 E-value: 8.20e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVEN-KLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAIV 315
Cdd:COG2905      6 SRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLA 85

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1901200332  316 EALHIMHNGKFLHLPVLDkDGDVVAVIDVIHITHA 350
Cdd:COG2905     86 EALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRA 119

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 86.86 E-value: 4.17e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  195 AIAAAVEGVEKNWGTSIAGPNTFMETLRERIFKPSLSTIIpeNTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVG 274
Cdd:COG2524     53 AGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIM--TKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVG 130

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901200332  275 ILTSKDILmRVISQNLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVIDVIHITHA 350
Cdd:COG2524    131 IITERDLL-KALAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRA 205

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: 82.20 E-value: 1.64e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:cd17775      7 TASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEALER 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1901200332  153 MVQGKFRHLPVV-ENGE---VIALLDIAKCL 179
Cdd:cd17775     87 MREKGVRRLPVVdDDGElvgIVTLDDILELL 117

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 84.55 E-value: 2.27e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIAtKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:COG2524     98 TVSPDTTLEEALELMLEKGISGLPVVDDGKLV-GIITERDLL-KALAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRL 175

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1901200332  153 MVQGKFRHLPVVE-NGEVIALL---DIAKCL 179
Cdd:COG2524    176 MLEHGIGRLPVVDdDGKLVGIItrtDILRAL 206

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 82.22 E-value: 2.34e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLN-----LEETPVSKVMTKNPVFVLSDTIAV 147
Cdd:COG3448     14 TVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerLLDLPVEDVMTRPVVTVTPDTPLE 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1901200332  148 EALQKMVQGKFRHLPVV-ENGEVIALL---DIAKCLYDAIAR 185
Cdd:COG3448     94 EAAELMLEHGIHRLPVVdDDGRLVGIVtrtDLLRALARLLEE 135

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: 79.60 E-value: 1.16e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVEN-KLVGILTSKDILMRVISQNLPQETTtVEKVMTPNPESATVDMAIV 315
Cdd:cd02205      1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDgKLVGIVTERDILRALVEGGLALDTP-VAEVMTPDVITVSPDTDLE 79

                           90       100
                   ....*....|....*....|....*..
gi 1901200332  316 EALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd02205     80 EALELMLEHGIRRLPVVDDDGKLVGIV 106

PB1 domain;

Pssm-ID: 395447 Cd Length: 84 Bit Score: 78.10 E-value: 1.69e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  413 TFAFKLQDKKGRMH-RFMCETQSLTTLITAILQRMGDDiepDNLPQIMYEDEDNDKVVLASDNDLGAAVEHAKSIGWKGL 491
Cdd:pfam00564    1 TVRLKLRYGGGIRRfLSVSRGISFEELRALVEQRFGLD---DVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSL 77


                   ....*..
gi 1901200332  492 KLHLDYT 498
Cdd:pfam00564   78 RLHVFPT 84

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 78.75 E-value: 3.84e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVM-VENKLVGILTSKDILMRVISQNLPQ-----ETTTVEKVMTPNPESATV 310
Cdd:COG3448      9 TRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDRLDEleerlLDLPVEDVMTRPVVTVTP 88

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1901200332  311 DMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI---DVIH 346
Cdd:COG3448     89 DTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVtrtDLLR 127

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: 77.07 E-value: 7.95e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVM-VENKLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAIV 315
Cdd:cd04623      1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVdDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVE 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1901200332  316 EALHIMHNGKFLHLPVLDkDGDVVAVI---DVI 345
Cdd:cd04623     81 ECMALMTERRIRHLPVVE-DGKLVGIVsigDVV 112

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: 77.07 E-value: 9.89e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAIVE 316
Cdd:cd04622      2 TRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEE 81

                           90       100
                   ....*....|....*....|....*.
gi 1901200332  317 ALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd04622     82 AARLMAEHQVRRLPVVDDDGRLVGIV 107

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: 76.31 E-value: 1.80e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  243 VGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDILMRVISQNLPQEtTTVEKVMTPNPESATVDMAIVEALHIM- 321
Cdd:cd04587      9 VPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPD-TPVSEIMTPPPVTIDADALVFEALLLMl 87

                           90       100
                   ....*....|....*....|..
gi 1901200332  322 -HNgkFLHLPVLDkDGDVVAVI 342
Cdd:cd04587     88 eRN--IHHLPVVD-DGRVVGVV 106

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: 75.27 E-value: 3.93e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSsAAMVMVEN--KLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAI 314
Cdd:cd17775      2 RREVVTASPDTSVLEAARLMRDHHV-GSVVVVEEdgKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGL 80

                           90       100
                   ....*....|....*....|....*...
gi 1901200332  315 VEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd17775     81 FEALERMREKGVRRLPVVDDDGELVGIV 108

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: 73.33 E-value: 1.83e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  238 TKVLKVGLDETVLGVTMKMVEYQ-SSAAMVMVENKLVGILTSKDILmRVISQNLPQETTtVEKVMTPNPESATVDMAIVE 316
Cdd:cd09836      3 KPVVTVPPETTIREAAKLMAENNiGSVVVVDDDGKPVGIVTERDIV-RAVAEGIDLDTP-VEEIMTKNLVTVSPDESIYE 80

                           90       100
                   ....*....|....*....|....*.
gi 1901200332  317 ALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd09836     81 AAELMREHNIRHLPVVDGGGKLVGVI 106

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.

Pssm-ID: 214770 Cd Length: 81 Bit Score: 69.54 E-value: 1.47e-14

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   413 TFAFKLQDKkGRMHRFMCE-TQSLTTLITAILQRMGDDIEPdnlPQIMYEDEDNDKVVLASDNDLGAAVEHAKSIGWKGL 491
Cdd:smart00666    1 TVDVKLRYG-GETRRLSVPrDISFEDLRSKVAKRFGLDNQS---FTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKL 76


                    ....*
gi 1901200332   492 KLHLD 496
Cdd:smart00666   77 RLHVF 81

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: 70.43 E-value: 2.29e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   75 PDsTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEeTPVSKVMTKNPVFVLSDTIAVEALQKMV 154
Cdd:cd17771     11 PD-TPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLD-APISEVMTPDPVRLPPSASAFEAALLMA 88

                           90
                   ....*....|....*....
gi 1901200332  155 QGKFRHLPVVENGEVIALL 173
Cdd:cd17771     89 EHGFRHVCVVDNGRLVGVV 107

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341389 [Multi-domain] Cd Length: 136 Bit Score: 71.03 E-value: 2.51e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  250 LGVTMKMVEYQSSAAMVMVENKLVGILTSKDILmRVISQNLPQETTTVEKVMTPNP----ESATVDmaIVEALHIMHNGK 325
Cdd:cd04620     35 LSEDSIITEARSSCVLVVENQQLVGIFTERDVV-RLTASGIDLSGVTIAEVMTQPVitlkESEFQD--IFTVLSLLRQHQ 111

                           90
                   ....*....|....*..
gi 1901200332  326 FLHLPVLDKDGDVVAVI 342
Cdd:cd04620    112 IRHLPIVDDQGQLVGLI 128

Nitrate/nitrite transporter NarK [Inorganic ion transport and metabolism];

Pssm-ID: 441825 [Multi-domain] Cd Length: 392 Bit Score: 74.53 E-value: 8.53e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  832 PPEKKRAPCIGEDFTLLQALGQADFWLIFMSLVLGVGSGITVIDNLGQIC---YSLGYNNTKIFVSLISISNFLGRVAGG 908
Cdd:COG2223    183 PPAGAAAAAKASLRDQLEALRDPRFWLLSLLYFGTFGSFIGFSSWLPPYLvdqFGLSAATAGLLAALFALLGALGRPLGG 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  909 YFSELIIRKLSlprTLAMSVVQAIMSLGLIYYAIDWPGkIYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQIT 988
Cdd:COG2223    263 WLSDRIGGRRV---LLIVFALMALGLLLLALALGSLWL-FLVLFLLLGLALGGGNGAVFALVPDIFPTKNAGAVYGLVGA 338

                          170       180
                   ....*....|....*....|.
gi 1901200332  989 TLPIGSFVFsGVIASNIYDYY 1009
Cdd:COG2223    339 AGGLGGFLG-PLLFGALLDAT 358

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: 65.14 E-value: 1.93e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDI-------ATKVIAKQLN--LEETPVSKVMTKNPVFVLSD 143
Cdd:cd04584     12 TVTPDTSLAEARELMKEHKIRHLPVVDDGKLV-GIVTDRDLlraspskATSLSIYELNylLSKIPVKDIMTKDVITVSPD 90

                           90       100
                   ....*....|....*....|....*..
gi 1901200332  144 TIAVEALQKMVQGKFRHLPVVENGEVI 170
Cdd:cd04584     91 DTVEEAALLMLENKIGCLPVVDGGKLV 117

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: 64.71 E-value: 2.48e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   74 VPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIAtKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQKM 153
Cdd:cd04604     18 VSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLR-RALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELM 96

                           90       100
                   ....*....|....*....|...
gi 1901200332  154 VQGKFRHLPVV-ENGEVIALLDI 175
Cdd:cd04604     97 EEHKITVLPVVdEDGKPVGILHL 119

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: 64.00 E-value: 3.57e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVI-AKQLNLEETPVSKVMTKNPVFVLSDTIAVE 148
Cdd:cd04629      4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLeASYHCEPGGTVADYMSTEVLTVSPDTSIVD 83

                           90       100
                   ....*....|....*....|....*
gi 1901200332  149 ALQKMVQGKFRHLPVVENGEVIALL 173
Cdd:cd04629     84 LAQLFLKNKPRRYPVVEDGKLVGQI 108

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: 341393 [Multi-domain] Cd Length: 120 Bit Score: 64.16 E-value: 3.83e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLC-GILTDRDIATKVIAKQLNLEETPVSKVMTKnPVFVLSDTIAVE-A 149
Cdd:cd04630     10 VTIDGLATVREALQLMKEHNVKSLIVEKRHEHDAyGIVTYTDILKKVIAEDRDPDLVNVYEIMTK-PAISVSPDLDIKyA 88

                           90       100
                   ....*....|....*....|....
gi 1901200332  150 LQKMVQGKFRHLPVVENGEVIALL 173
Cdd:cd04630     89 ARLMARFNLKRAPVIENNELIGIV 112

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: 63.17 E-value: 8.41e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  265 MVMV---ENKLVGILTSKDiLMRVISQNLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAV 341
Cdd:cd04604     38 CTAVvdeDGRLVGIITDGD-LRRALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGI 116


                   ....*
gi 1901200332  342 IDvIH 346
Cdd:cd04604    117 LH-LH 120

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 63.39 E-value: 1.06e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  269 ENKLVGILTSKDILMRvisqnlpQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI---DVI 345
Cdd:COG4109     57 NGRLVGIVTSKDILGK-------DDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIIsrqDVL 129

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: 63.13 E-value: 1.29e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   71 ALTVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIA--------TKVIAK--QLN----LEETPVSKVMTKN 136
Cdd:cd17777     12 VLSISPSAPILSAFEKMNRRGIRRLVVVDENKLE-GILSARDLVsylgggclFKIVESrhQGDlysaLNREVVETIMTPN 90

                           90       100
                   ....*....|....*....|....*...
gi 1901200332  137 PVFVLSDTIAVEALQKMVQGKFRHLPVV 164
Cdd:cd17777     91 PVYVYEDSDLIEALTIMVTRGIGSLPVV 118

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: 62.15 E-value: 1.39e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIatkviakQLNLEE-TPVSKVMTKNPVFVLSDTIAVE 148
Cdd:cd04583      3 NPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDI-------NRNYRKaKKVGEIMERDVFTVKEDSLLRD 75

                           90
                   ....*....|....*...
gi 1901200332  149 ALQKMVQGKFRHLPVVEN 166
Cdd:cd04583     76 TVDRILKRGLKYVPVVDE 93

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: 61.69 E-value: 1.99e-11

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1901200332  269 ENKLVGILTSKDIlMRVISQNLPQETTtVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVV 339
Cdd:cd04607     34 NRKLLGTVTDGDI-RRGLLKGLSLDAP-VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVV 102

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

Pssm-ID: 99716 [Multi-domain] Cd Length: 81 Bit Score: 60.37 E-value: 2.41e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  414 FAFKLQDKkGRMHRFMCETQSLT--TLITAILQRMGDDIEPdnlPQIMYEDEDNDKVVLASDNDLGAAVEHAKSIGWKGL 491
Cdd:cd05992      1 VRVKVKYG-GEIRRFVVVSRSISfeDLRSKIAEKFGLDAVS---FKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKL 76


                   ....*
gi 1901200332  492 KLHLD 496
Cdd:cd05992     77 RLFVF 81

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: 61.67 E-value: 3.39e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  129 VSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVENGEVIALL---DIAKclydaiarmersvekgkaiAAAvegvek 205
Cdd:cd04584      2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVtdrDLLR-------------------ASP------ 56

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901200332  206 nwgtSIAGPNTFMEtLRERIFKPSLSTIIpeNTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDIL 282
Cdd:cd04584     57 ----SKATSLSIYE-LNYLLSKIPVKDIM--TKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDIL 126

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: 61.58 E-value: 3.71e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  128 PVSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVENGEVIALLDIAkclyDAIARMERSVEKGKAIAAAVEgveknw 207
Cdd:cd17778      1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAM----DIVKYFGSHEAKKRLTTGDID------ 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901200332  208 gtsiagpnTFMETLRERIFKPSLSTIIPentkvlkvglDETVLGVTMKMVEY-QSSAAMVMVENKLVGILTSKDILMR 284
Cdd:cd17778     71 --------EAYSTPVEEIMSKEVVTIEP----------DADIAEAARLMIKKnVGSLLVVDDEGELKGIITERDVLIA 130

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: 62.30 E-value: 3.84e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKV------------IAKQ------------------- 121
Cdd:cd04614      8 PVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDVSriveseeesgmsIADDedewswegirdvmslyypt 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1901200332  122 --LNLEETPVSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVE-NGEVIALL 173
Cdd:cd04614     88 snVELPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSgEGDLAGML 142

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341389 [Multi-domain] Cd Length: 136 Bit Score: 61.79 E-value: 4.31e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMA-ARRVDALLLTDSNAL--------------LCGILTDRDIaTKVIAKQLNLEETPVSKVMTKN 136
Cdd:cd04620     10 LTVSPDTPVIEAIALMSqTRSSCCLLSEDSIITearsscvlvvenqqLVGIFTERDV-VRLTASGIDLSGVTIAEVMTQP 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1901200332  137 PVFV----LSDTIAVEALqkMVQGKFRHLPVV-ENGEVIALL 173
Cdd:cd04620     89 VITLkeseFQDIFTVLSL--LRQHQIRHLPIVdDQGQLVGLI 128

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 61.47 E-value: 4.64e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKviakqlnLEETPVSKVMTKNPVFV-LSDTIAvE 148
Cdd:COG4109     26 DVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK-------DDDTPIEDVMTKNPITVtPDTSLA-S 97

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1901200332  149 ALQKMVQGKFRHLPVV-ENGEVIALL---DIAKCL 179
Cdd:COG4109     98 AAHKMIWEGIELLPVVdDDGRLLGIIsrqDVLKAL 132

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: 59.77 E-value: 9.22e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDsTTLFEACRRM--AARRVdALLLTDSNALLcGILTDRDI--AtkvIAKQLNLEeTPVSKVMTKNPVFVLSDTI 145
Cdd:cd04607      4 KVLVSPD-TTIREAIEVIdkGALQI-ALVVDENRKLL-GTVTDGDIrrG---LLKGLSLD-APVEEVMNKNPITASPSTS 76

                           90       100
                   ....*....|....*....|....*...
gi 1901200332  146 AVEALQKMVQGKFRHLPVV-ENGEVIAL 172
Cdd:cd04607     77 REELLALMRAKKILQLPIVdEQGRVVGL 104

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: 341365 [Multi-domain] Cd Length: 113 Bit Score: 59.51 E-value: 1.42e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNaLLCGILTDRDIATKVIAKQLNLeETPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd04589      4 PPLFVDAETSIREATRLMKENGADSLLVRDGD-GRVGIVTRTDLRDAVVLDGQPV-DTPVGEIATFPLISVEPDDFLFNA 81

                           90       100
                   ....*....|....*....|....*
gi 1901200332  150 LQKMVQGKFRHLPVVENGEVIALLD 174
Cdd:cd04589     82 LLLMTRHRVKRVVVREGEEIVGVLE 106

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: 57.33 E-value: 6.61e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  238 TKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDILmrvisqnLPQETTTVEKVMTPNPESATVDMAIVEA 317
Cdd:cd04610      3 RDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLL-------GKDDDEKVSEIMSRDTVVADPDMDITDA 75

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1901200332  318 LHIMHNGKFLHLPVLDKDGDVVAVI---DVI 345
Cdd:cd04610     76 ARVIFRSGISKLPVVDDEGNLVGIItnmDVI 106

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: 56.35 E-value: 1.64e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIatkVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:cd04595      6 TVSPDTTIEEARKIMLRYGHTGLPVVEDGKLV-GIISRRDV---DKAKHHGLGHAPVKGYMSTNVITIDPDTSLEEAQEL 81

                           90
                   ....*....|....*...
gi 1901200332  153 MVQGKFRHLPVVENGEVI 170
Cdd:cd04595     82 MVEHDIGRLPVVEEGKLV 99

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: 57.05 E-value: 1.65e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI---------------------ATKVIAKQLN-LEET 127
Cdd:cd04586      4 DVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLlrreepgteprrvwwldalleSPERLAEEYVkAHGR 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1901200332  128 PVSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVENGEVI 170
Cdd:cd04586     84 TVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLV 126

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: 341408 [Multi-domain] Cd Length: 112 Bit Score: 56.04 E-value: 1.81e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   71 ALTVPDSTTLFEACRRMAARRVDALLLTDSN-ALLCGILTdRDIATKVIAkqLNLEETPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd17772      4 VISVEPDTTIAEAAELMTRYNINALPVVDGGtGRLVGIIT-RQVAEKAIY--HGLGDLPVSEYMTTEFATVTPDAPLSEI 80

                           90       100
                   ....*....|....*....|.
gi 1901200332  150 LQKMVQGKFRHLPVVENGEVI 170
Cdd:cd17772     81 QEIIVEQRQRLVPVVEDGRLV 101

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: 55.94 E-value: 1.85e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  269 ENKLVGILTSKDILMRvisqnlpQETTTVEKVMTPNPESATVDMAIVEALHIM-HNGKFLhLPVLDKDGDVVAVI---DV 344
Cdd:cd04596     34 ENRVVGIVTAKDVIGK-------EDDTPIEKVMTKNPITVKPKTSVASAAHMMiWEGIEL-LPVVDENRKLLGVIsrqDV 105


                   .
gi 1901200332  345 I 345
Cdd:cd04596    106 L 106

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: 55.23 E-value: 3.43e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  262 SAAMVMVENKLVGILTSKDIlMRVISQNLpqETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAV 341
Cdd:cd04588     26 HGAPVVDDGKLVGIVTLTDI-AKALAEGK--ENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGI 102


                   ....*...
gi 1901200332  342 I---DVIH 346
Cdd:cd04588    103 ItrtDILK 110

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: 341368 [Multi-domain] Cd Length: 128 Bit Score: 55.45 E-value: 4.55e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI---ATKVIAKQLNLEETPVSKVMTKN------PVFVLS 142
Cdd:cd04592      6 ITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIqrfLKRAKADNEDPKTILVSSICTRNggycrgLWTCTP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1901200332  143 DTIAVEALQKMVQGKFRHLPVVENGE------VIALLDiakclYDAI 183
Cdd:cd04592     86 DMDLLTAKMLMEARGINQLPVVKRGGeerrrrVVGLLD-----RDSI 127

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: 54.11 E-value: 1.17e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIATkviAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:cd04801      9 TVTPEMTVSELLDRMFEEKHLGYPVVENGRLV-GIVTLEDIRK---VPEVEREATRVRDVMTKDVITVSPDADAMEALKL 84

                           90       100
                   ....*....|....*....|.
gi 1901200332  153 MVQGKFRHLPVVENGEVIALL 173
Cdd:cd04801     85 MSQNNIGRLPVVEDGELVGII 105

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: 54.35 E-value: 1.42e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  266 VMVENKLVGILTSKDILMRVISQ---------NLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDkDG 336
Cdd:cd04584     36 VVDDGKLVGIVTDRDLLRASPSKatslsiyelNYLLSKIPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVD-GG 114


                   ....*.
gi 1901200332  337 DVVAVI 342
Cdd:cd04584    115 KLVGII 120

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: 54.36 E-value: 1.43e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVM-VENKLVGILTSKDILMRVISQNLPQ----------------------E 293
Cdd:cd04586      2 TTDVVTVTPDTSVREAARLLLEHRISGLPVVdDDGKLVGIVSEGDLLRREEPGTEPRrvwwldallesperlaeeyvkaH 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1901200332  294 TTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDkDGDVVAVI---DVIH 346
Cdd:cd04586     82 GRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVsraDLLR 136

Monocarboxylate transporter (MCT) family and similar transporters of the Major Facilitator Superfamily; The group is composed of the Monocarboxylate transporter (MCT) family in animals and similar transporters from fungi, plants, archaea, and bacteria. MCT is also called Solute carrier family 16 (SLC16 or SLC16A). It is composed of 14 members, MCT1-14. MCTs play an integral role in cellular metabolism via lactate transport and have been implicated in metabolic synergy in tumors. MCTs have been found to facilitate the transport across the plasma membrane not only of monocarboxylates (MCT1-4), but also thyroid hormones (MCT8/10), and aromatic acids (MCT10). Yeast MCT homologous (Mch) proteins are not involved in the uptake of monocarboxylates; their substrates are not known. The MCT-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

Pssm-ID: 340872 [Multi-domain] Cd Length: 385 Bit Score: 57.42 E-value: 2.31e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  842 GEDFTLLQALGQADFWLIFMSLVLGVGSGITVIDNLGQICYSLGYNNTK---IFVSLISISNFLGRVAGGYFSELIIRKL 918
Cdd:cd17314    194 KKTQTMGEIFRDKVFWILFIAIFLVLIGGFLFIANMASLVRSLQLDAPSfvtKLMSIYGLFNAFGRLLWGIVADFFGGRL 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  919 SLprtlaMSVVQAIMSLGL--IYYAIDWPGKIYVVTIVI-GMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSf 995
Cdd:cd17314    274 ST-----LSILLTILGLGLcaFLFLLKMTPVGLVLTGSLlGFSYGGLFTVYPATVSTVFGTESFATLYGILLFAPAIGS- 347

                          170
                   ....*....|..
gi 1901200332  996 VFSGVIASNIYD 1007
Cdd:cd17314    348 ILGPMLGAKFYD 359

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: 53.26 E-value: 2.74e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   71 ALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQlNLEETPVSKVMTKNP--VFVLSDTIAVE 148
Cdd:cd04617      6 PVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQ-DLEKTPVSMIMTRMPniVTVTPDDSVLE 84

                           90       100
                   ....*....|....*....|
gi 1901200332  149 ALQKMVQGKFRHLPVVENGE 168
Cdd:cd04617     85 AARKLIEHEIDSLPVVEKED 104

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: 52.80 E-value: 2.85e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATkviakqLNLEETPVSKVMTKN--PVFVLSDTIAVEAL 150
Cdd:cd04601      6 TLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRF------ETDLSTPVSEVMTPDerLVTAPEGITLEEAK 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1901200332  151 QKMVQGKFRHLPVV-ENGEVIALL---DIAK 177
Cdd:cd04601     80 EILHKHKIEKLPIVdDNGELVGLItrkDIEK 110

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: 52.80 E-value: 2.88e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  261 SSAAMVMVENKLVGILTSKDIlmrvisQNLPQETTTVEKVMTPNPESATVDMAIV--EALHIMHNGKFLHLPVLDKDGDV 338
Cdd:cd04601     26 SGVPVTEDGGKLVGIVTSRDI------RFETDLSTPVSEVMTPDERLVTAPEGITleEAKEILHKHKIEKLPIVDDNGEL 99


                   ....
gi 1901200332  339 VAVI 342
Cdd:cd04601    100 VGLI 103

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

Pssm-ID: 341403 [Multi-domain] Cd Length: 116 Bit Score: 52.61 E-value: 4.25e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDiatkviAKQLNLEE-----TPVSKVMTkNPVFVL-SDTI 145
Cdd:cd09833      8 LTCSPDTPLADAAARMAERRCSSILIVENGEIV-GIWTERD------ALKLDFSDpdafrRPISEVMS-SPVLTIpQDTT 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1901200332  146 AVEALQKMVQGKFRHLPVVENGE----VIALLDIAK 177
Cdd:cd09833     80 LGEAAVRFRQEGVRHLLVVDDDGrpvgIVSQTDVVL 115

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: 52.41 E-value: 4.27e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALlCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:cd17776      7 TVDADASLEDAAERMLRNRVGSVVVTDDGTP-AGILTETDALHAGYATDDPFSEIPVRAVASRPLVTISPTATLREAAER 85

                           90       100
                   ....*....|....*....|.
gi 1901200332  153 MVQGKFRHLPVVENGEVIALL 173
Cdd:cd17776     86 MVDEGVKKLPVVDGLDLVGIL 106

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: 53.11 E-value: 4.62e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  233 IIPENTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDIL-------MRVISQNLPQ-------ETTTVE 298
Cdd:cd17777      5 MIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLVsylgggcLFKIVESRHQgdlysalNREVVE 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1901200332  299 KVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd17777     85 TIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIV 128

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: 51.65 E-value: 9.20e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEeTPVSKVMTKNPVFVLSDTIAVEALQ 151
Cdd:cd17784      5 ITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKYELG-TTVEEVMVKDVATVHPDETLLEAIK 83

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1901200332  152 KM-----VQGKFRHLPVVENGEVIALL---DIAKCL 179
Cdd:cd17784     84 KMdsnapDEEIINQLPVVDDGKLVGIIsdgDIIRAI 119

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: 50.90 E-value: 1.38e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  255 KMVEYQSSAAMVMVEN-KLVGILTSKDILMRVIS---QNlpQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLP 330
Cdd:cd04629     20 LLLEHKISGAPVVDEQgRLVGFLSEQDCLKALLEasyHC--EPGGTVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYP 97

                           90
                   ....*....|..
gi 1901200332  331 VLDkDGDVVAVI 342
Cdd:cd04629     98 VVE-DGKLVGQI 108

MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of transporters; This group is composed of uncharacterized bacterial MFS-type transporters including Bacillus subtilis YcxA and YbfB. YcxA has been shown to facilitate the export of surfactin in B. subtilis. The YcxA-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

Pssm-ID: 340913 [Multi-domain] Cd Length: 386 Bit Score: 54.58 E-value: 1.92e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  846 TLLQALGQADFWLIFMSLVLGVGSGITVIDNLGQICYSLGYNNTK--IFVSLISISNFLGRVAGGYFSeliiRKLSLPRT 923
Cdd:cd17355    202 TLKEALRSASFWLLALAFFLCGFAVVGLIVHLVPYLADRGISPAAaaVALALIGLFNIVGRLLSGWLG----DRYSPRRL 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  924 LAMSVvqAIMSLGLIYYAI-DWPGK-IYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSFvFSGVI 1001
Cdd:cd17355    278 LAASY--ALRALGLALLLLlPFPPLaLLLFAALFGLGWGATVPLTAALAARYFGARSYGTLFGLVFAPHQLGSA-LGPWL 354


                   ....*...
gi 1901200332 1002 ASNIYDYY 1009
Cdd:cd17355    355 GGLLYDRT 362

inosine-5'-monophosphate dehydrogenase; Provisional

Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 54.98 E-value: 1.93e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901200332  267 MVENKLVGILTSKDILmrvisqNLPQETTTVEKVMTPNpESATV---DMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:PTZ00314   137 KVGGKLLGIVTSRDID------FVKDKSTPVSEVMTPR-EKLVVgntPISLEEANEVLRESRKGKLPIVNDNGELVALV 208

Bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4, and similar proteins; This family is composed of bacterial L-fucose permease (FucP), eukaryotic Major facilitator superfamily domain-containing protein 4 (MFSD4) proteins, and similar proteins. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. The MFSD4 subfamily consists of two vertebrate members: MFSD4A and MFSD4B. The function of MFSD4A is unknown. MFSD4B is more commonly know as Sodium-dependent glucose transporter 1 (NaGLT1), a primary fructose transporter in rat renal brush-border membranes that also facilitates sodium-independent urea uptake. The FucP/MFSD4 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

Pssm-ID: 340891 [Multi-domain] Cd Length: 372 Bit Score: 53.86 E-value: 2.64e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  857 WLIFMSLVLGVGSGITVIDNLGQIcYSLGYNNtkifVSLISISNFLGRVAGGYFSELIIRKLSLPRTLAMSvvQAIMSLG 936
Cdd:cd17333      2 YISFFSNGLTDALLGILGPSLEEA-FNLNVAD----VSVIFSSQNAGYLIGSLLAGFLMKRLGRRRTLILG--LLLISLA 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901200332  937 LIYYAIDWPGKIYVVTIVI-GMGYGAHWAIAPASVSDIFGlKSFGSLYNFQITTLPIGSFVF 997
Cdd:cd17333     75 LALIFATPSIYLFVVLMFLaGLGAGILDTGANTFVGALFE-ESSATRLNVLHGFFGLGALIG 135

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: 54.32 E-value: 2.88e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  243 VGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDIlmrvisQNLPQETTTVEKVMTP-NPESATVDMAIVEALHIM 321
Cdd:pfam00478   93 LSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDL------RFETDLSQPVSEVMTKeNLVTAPEGTTLEEAKEIL 166

                           90       100
                   ....*....|....*....|.
gi 1901200332  322 HNGKFLHLPVLDKDGDVVAVI 342
Cdd:pfam00478  167 HKHKIEKLPVVDDNGRLVGLI 187

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: 47.59 E-value: 4.48e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1901200332  297 VEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVIDVIHITHA 350
Cdd:pfam00571    1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54

Monocarboxylate transporter (MCT) family of the Major Facilitator Superfamily of transporters; The animal Monocarboxylate transporter (MCT) family is also called Solute carrier family 16 (SLC16 or SLC16A). It is composed of 14 members, MCT1-14. MCTs play an integral role in cellular metabolism via lactate transport and have been implicated in metabolic synergy in tumors. MCT1-4 are proton-coupled transporters that facilitate the transport across the plasma membrane of monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and ketone bodies such as acetoacetate, beta-hydroxybutyrate and acetate. MCT8 and MCT10 are transporters which stimulate the cellular uptake of thyroid hormones such as thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine (T2). MCT10 also functions as a sodium-independent transporter that mediates the uptake or efflux of aromatic acids. Many members are orphan transporters whose substrates are yet to be determined. The MCT family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

Pssm-ID: 340910 [Multi-domain] Cd Length: 361 Bit Score: 52.94 E-value: 6.05e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  847 LLQALGQADFWLIFMSLVLGVGSGITVIDNLGQICYSLGYNNTKIF--VSLISISNFLGRVAGGYFSELiiRKLSLPRTL 924
Cdd:cd17352    176 LLRLLKDPTFVLLALGVSFAMLGFFVPFVYLPSYAKSLGIDESDAAflLSIIGISDIVGRILLGLLADK--PRIGRLYLY 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  925 AMSVVQAIMSLGLIYYAIDWPGkIYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSFVFsGVIASN 1004
Cdd:cd17352    254 IFTLLILGLSLLAFPLATTYVG-LIVFSVLFGFCSGSYSSLTPVILADLVGLEKLSNAYGLVLLFQGLAALVG-PPIAGL 331


                   ....*
gi 1901200332 1005 IYDYY 1009
Cdd:cd17352    332 LRDYT 336

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 49.48 E-value: 7.06e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1901200332  296 TVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:COG3448      3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIV 49

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: 46.82 E-value: 8.56e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1901200332  129 VSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVV-ENGEVIALL---DIAKCLYD 181
Cdd:pfam00571    1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVtlkDLLRALLG 57

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: 52.39 E-value: 1.02e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIatkviaKQLNLEETPVSKVMTK-NPVFVLSDTIAVEALQ 151
Cdd:pfam00478   92 TLSPDATVADALALMERYGISGVPVVDDGKLV-GIVTNRDL------RFETDLSQPVSEVMTKeNLVTAPEGTTLEEAKE 164

                           90       100       110
                   ....*....|....*....|....*....|
gi 1901200332  152 KMVQGKFRHLPVV-ENGEVIALL---DIAK 177
Cdd:pfam00478  165 ILHKHKIEKLPVVdDNGRLVGLItikDIEK 194

Sugar phosphate permease [Carbohydrate transport and metabolism];

Pssm-ID: 441872 [Multi-domain] Cd Length: 363 Bit Score: 51.79 E-value: 1.26e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  856 FWLIFMSLVLGVGSGITVIDNLGQICYS-LGYNNTK--IFVSLISISNFLGRVAGGYFSELIIRKlslpRTLAMSVVQAI 932
Cdd:COG2271    182 FWLLALAYFLVYFALYGFLTWLPTYLVEvRGLSLAQagLLLSLPFLAGIVGSLLGGWLSDRLGRR----RKLVLAIGLLL 257

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901200332  933 MSLGLIYYA-IDWPGKIYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSFVFSGVIASnIYDYYA 1010
Cdd:COG2271    258 AALALLLLAlLPSPALAIALLFLAGFGLGGAFGLLWALAAELFPKKARGTASGLVNTFGFLGGALGPLLVGY-LLDATG 335

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: 48.81 E-value: 1.44e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  246 DETVLGVTMKMVEYQSSAAMVMV--ENKLVGILTSKDIL---------------------------MRVISQ-------- 288
Cdd:cd04614     11 DETPLPVALRAMRLANVPAAPVLdsEGKLVGIVTERDLIdvsriveseeesgmsiaddedewswegIRDVMSlyyptsnv 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1901200332  289 NLPQETttVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd04614     91 ELPDKP--VKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGML 142

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

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 45.28 E-value: 3.31e-06

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1901200332   63 VKRLRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVI 118
Cdd:pfam00571    1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56

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: 46.94 E-value: 3.95e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  269 ENKLVGILTSKDILMRvisqnlpQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI---DVI 345
Cdd:cd04606     46 DRRLLGVVSLRDLLLA-------DPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIItvdDVL 118


                   ..
gi 1901200332  346 HI 347
Cdd:cd04606    119 DV 120

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

Pssm-ID: 341384 [Multi-domain] Cd Length: 131 Bit Score: 47.33 E-value: 4.13e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIaTKVIAKqlNLEETPVSKVMTKNPVFVLSDTIAVEALQ 151
Cdd:cd04611     16 LVLPGDASLAEAARRMRSHRADAAVIECPDGGL-GILTERDL-VRFIAR--HPGNTPVGELASRPLLTVGAEDSLIHARD 91

                           90       100
                   ....*....|....*....|....*....
gi 1901200332  152 KMVQGKFRHLPVV-ENGEVIALLDIAKCL 179
Cdd:cd04611     92 LLIDHRIRHLAVVdEDGQVTGLLGFADLL 120

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 47.15 E-value: 4.42e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNA-------LLCGILTDRDIaTKVIAKQLNLEETPVSKVMtKNPVFVLSDTI 145
Cdd:cd17774      9 HAPPTASVLELAQLMAEHRVSCVVIVEEDEqqeknklIPVGIVTERDI-VQFQALGLDLSQTQAQTVM-SSPLFSLRPDD 86

                           90       100
                   ....*....|....*....|....*
gi 1901200332  146 AV-EALQKMVQGKFRHLPVV-ENGE 168
Cdd:cd17774     87 SLwTAHQLMQQRRIRRLVVVgEQGE 111

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: 46.84 E-value: 5.55e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  129 VSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVENGEVIALL---DIAKCLYDaiarmersvekGKAIAAAVEGvek 205
Cdd:cd04631      2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVtstDIMRYLGS-----------GEAFEKLKTG--- 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901200332  206 nwgtsiagpntfmeTLRErIFKPSLSTIIpeNTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDILM 283
Cdd:cd04631     68 --------------NIHE-VLNVPISSIM--KRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILR 128

Major Facilitator Superfamily;

Pssm-ID: 429598 [Multi-domain] Cd Length: 344 Bit Score: 49.72 E-value: 6.06e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  832 PPEKKRAPCIGEDFTLLQALGQADFWLIFMSLVLGVGSGITVIdNLGQICYSLGYNNTK--IFVSLISISNFLGRVAGGY 909
Cdd:pfam07690  179 RPKPAEEARLSLIVAWKALLRDPVLWLLLALLLFGFAFFGLLT-YLPLYQEVLGLSALLagLLLGLGGLLGAIGRLLLGR 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  910 FSELIIRKlslPRTLAMSVVQAIMSLGLIYYA-IDWPGKIYVVTIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQIT 988
Cdd:pfam07690  258 LSDRLGRR---RRLLLALLLLILAALGLLLLSlTLSSLWLLLALLLLGFGFGLVFPALNALVSDLAPKEERGTASGLYNT 334

                          170
                   ....*....|
gi 1901200332  989 TLPIGSFVFS 998
Cdd:pfam07690  335 AGSLGGALGP 344

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: 43.66 E-value: 9.15e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1901200332    73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI 113
Cdd:smart00116    4 TVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44

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: 45.68 E-value: 1.36e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDAL-LLTDSNalLCGILTDRDIATKVIAKQL-------NLEE---TPVSKVMTKNPVFVL 141
Cdd:cd04631     12 TATPGTPIEDVAKIMVRNGFRRLpVVSDGK--LVGIVTSTDIMRYLGSGEAfeklktgNIHEvlnVPISSIMKRDIITTT 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1901200332  142 SDTIAVEALQKMVQGKFRHLPVVENGEVIALL---DIAKCL 179
Cdd:cd04631     90 PDTDLGEAAELMLEKNIGALPVVDDGKLVGIIterDILRAI 130

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: 45.68 E-value: 1.37e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  237 NTKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDILMRVISQNLPQETTT----------VEKVMTPNPE 306
Cdd:cd04631      7 TKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRYLGSGEAFEKLKTgnihevlnvpISSIMKRDII 86

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1901200332  307 SATVDMAIVEALHIMHNGKFLHLPVLDkDGDVVAVI 342
Cdd:cd04631     87 TTTPDTDLGEAAELMLEKNIGALPVVD-DGKLVGII 121

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: 44.77 E-value: 1.86e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1901200332   98 TDSNALLCGILTDRDIATKViakqlnlEETPVSKVMTKNPVFV-LSDTIAvEALQKMVQGKFRHLPVVENG 167
Cdd:cd04596     31 VDEENRVVGIVTAKDVIGKE-------DDTPIEKVMTKNPITVkPKTSVA-SAAHMMIWEGIELLPVVDEN 93

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: 44.45 E-value: 2.34e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLcGILTDRDIAtKVIAKqlNLEETPVSKVMTKNPVFVLSDTIAVEALQ 151
Cdd:cd04588      5 ITLKPDATIKDAAKLLSENNIHGAPVVDDGKLV-GIVTLTDIA-KALAE--GKENAKVKDIMTKDVITIDKDEKIYDAIR 80

                           90       100
                   ....*....|....*....|...
gi 1901200332  152 KMVQGKFRHLPVV-ENGEVIALL 173
Cdd:cd04588     81 LMNKHNIGRLIVVdDNGKPVGII 103

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: 44.54 E-value: 2.63e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   62 TVKRLRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEEtpvskVMTKNPVFVL 141
Cdd:cd04605      1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALKKDSLEE-----IMTRNVITAR 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1901200332  142 SDTIAVEALQKMVQGKFRHLPVV-ENGEVIALL 173
Cdd:cd04605     76 PDEPIELAARKMEKHNISALPVVdDDRRVIGII 108

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: 44.72 E-value: 2.79e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901200332  296 TVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDkDGDVVAVI---DVIHITHAAVTT 354
Cdd:cd04584      1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVtdrDLLRASPSKATS 61

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 47.75 E-value: 2.96e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  269 ENKLVGILTSKDILmrvisqnLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI---DVI 345
Cdd:COG2239    174 DGRLVGVVSLRDLL-------LADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIItvdDVV 246


                   ....*...
gi 1901200332  346 HITHAAVT 353
Cdd:COG2239    247 DVIEEEAT 254

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 44.47 E-value: 3.32e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901200332  296 TVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI---DVIHITHAAVTTAGST 358
Cdd:COG0517      2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVtdrDLRRALAAEGKDLLDT 67

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: 43.95 E-value: 4.10e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  238 TKVLKVGLDETVLGVTMKMVEYQSSAAMVM-VENKLVGILTSKDILMRVISQNLPQEtTTVEKVMTPNPESATVDMAIVE 316
Cdd:cd17784      2 KNVITAKPNEGVVEAFEKMLKHKISALPVVdDEGKLIGIVTATDLGHNLILDKYELG-TTVEEVMVKDVATVHPDETLLE 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1901200332  317 ALHIMH-----NGKFLHLPVLDkDGDVVAVI---DVI 345
Cdd:cd17784     81 AIKKMDsnapdEEIINQLPVVD-DGKLVGIIsdgDII 116

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: 43.77 E-value: 4.19e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  269 ENKLVGILTSKDIlmrviSQNLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVIDVIHIT 348
Cdd:cd04605     40 DGKLIGIVTSWDI-----SKAVALKKDSLEEIMTRNVITARPDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDIS 114


                   .
gi 1901200332  349 H 349
Cdd:cd04605    115 R 115

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: 43.72 E-value: 4.66e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLnLEETPVSKVMTKNPVFVLSDTIAVEA 149
Cdd:cd04613      4 KVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEEL-WDLVVVKDLATTDVITVTPDDDLYTA 82

                           90       100
                   ....*....|....*....|....*..
gi 1901200332  150 LQKMVQGKFRHLPVVE---NGEVIALL 173
Cdd:cd04613     83 LLKFTSTNLDQLPVVDdddPGKVLGML 109

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: 43.25 E-value: 6.89e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  240 VLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDIlMRVISQNLPQEttTVEKVMTPNPESATVDMAIVEALH 319
Cdd:cd04595      4 VKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV-DKAKHHGLGHA--PVKGYMSTNVITIDPDTSLEEAQE 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1901200332  320 IM--HN-GkflHLPVLDkDGDVVAVI---DVI 345
Cdd:cd04595     81 LMveHDiG---RLPVVE-EGKLVGIVtrsDVL 108

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: 42.33 E-value: 1.13e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  104 LCGILTDRDIATkviakqlNLEETPVSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVENGEVIALLDIAkclyDAI 183
Cdd:cd04638     39 LVGIVTRKDLLR-------NPDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVA----DLV 107


                   ..
gi 1901200332  184 AR 185
Cdd:cd04638    108 RA 109

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: 42.93 E-value: 1.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  269 ENKLVGILTSKDIL--------------MRVISQNLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDK 334
Cdd:cd04600     35 ARRLVGIVTLADLLkhadldpprglrgrLRRTLGLRRDRPETVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDA 114

                           90
                   ....*....|....
gi 1901200332  335 DGDVVAVI---DVI 345
Cdd:cd04600    115 DGRLVGIVtqsDLI 128

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 42.93 E-value: 1.41e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   56 ERSGERTVKRLRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIAtKVIAKQLNLE 125
Cdd:COG3448     68 ERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLL-RALARLLEEE 136

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: 341368 [Multi-domain] Cd Length: 128 Bit Score: 42.35 E-value: 1.71e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  238 TKVLKVGLDETVLGVTMKMVEYQSSAAMVM-VENKLVGILTSKDI---LMRVISQNLPQETTTVEKVMTPN------PES 307
Cdd:cd04592      3 TRYITVLMSTTLKEAVLLMLEEKQSCALIVdSDDFLIGILTLGDIqrfLKRAKADNEDPKTILVSSICTRNggycrgLWT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1901200332  308 ATVDMAIVEALHIMHNGKFLHLPVLDKDGD-----VVAVID 343
Cdd:cd04592     83 CTPDMDLLTAKMLMEARGINQLPVVKRGGEerrrrVVGLLD 123

Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];

Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 44.89 E-value: 2.15e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  828 RSDIPPEKKRAPcIGEDFTLLqaLGQADF-WLIFMSLVLGVGSGIT-------VIDNLGqicyslgynNTKIFVSLISIS 899
Cdd:COG2211    205 KERPVPEEEKVS-LKESLKAL--LKNRPFlLLLLAYLLFFLALALVaalllyyFKYVLG---------LSAALVGLLLAL 272

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901200332  900 NFLGRVAGGYFSELIIRKLSLPRTLAMS-VVQAIMSLGLIYYAIDWPGKIYVVTIVIGMGYGAHWAIAPASVSDI 973
Cdd:COG2211    273 YFLAALLGAPLWPRLAKRFGKKKAFIIGlLLAALGLLLLFFLGPGNLWLLLVLAALAGIGLGAILVLPWAMLADV 347

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in proteobacteria; 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: 341398 [Multi-domain] Cd Length: 133 Bit Score: 42.17 E-value: 2.25e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1901200332   66 LRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIA-----TKVIAKQLNLEETPVSKVMT 134
Cdd:cd04640      2 FRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILgekplKIVQERGIPREELLVADVMT 75

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.

Pssm-ID: 349949 [Multi-domain] Cd Length: 378 Bit Score: 44.72 E-value: 2.55e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  856 FWLIFMSLVLGVGSGITVIDNLGQI---CYSLGYNNTKIFVSLISISNFLGRVAGGYFSEliiRKLSLPRTLAMSVVqaI 932
Cdd:cd06174    205 LWLLLLAIFLVNLAYYSFSTLLPLFlldLGGLSVAVAGLLLSLFGLAGALGSLLLGLLSD---RLIGRKPLLLIGLL--L 279

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901200332  933 MSLGLIYYAIDWPGKIYVV-TIVIGMGYGAHWAIAPASVSDIFGLKSFGSLYNFQITTLPIGSFVFSGVIASNIYDYYA 1010
Cdd:cd06174    280 MALGLALLLLAPSLLLLLLlLLLLGFGLGGLLPLSFALIAELFPPEIRGTAFGLLNTFGFLGGAIGPLLAGFLLAATFG 358

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: 41.46 E-value: 3.17e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI 113
Cdd:cd02205     71 TVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111

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: 3.73e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  129 VSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVV-ENGEVIALL---DIAKclydaiarmersvekgkaiaaavegve 204
Cdd:cd04605      2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVsEDGKLIGIVtswDISK--------------------------- 54

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901200332  205 knwgtSIAGPNTfmetlrerifkpSLSTIIPENtkVLKVGLDETVLGVTMKMVEYQSSAAMVMVE-NKLVGILTSKDI 281
Cdd:cd04605     55 -----AVALKKD------------SLEEIMTRN--VITARPDEPIELAARKMEKHNISALPVVDDdRRVIGIITSDDI 113

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: 41.55 E-value: 4.16e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   70 KALTVPDSTTLFEACRRMAARRVDALLLTDSNALlCGILTDRDI-------ATKVIAKQLNLEE---TPVSKVMTKNPVF 139
Cdd:cd17778      9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKL-VGIVTAMDIvkyfgshEAKKRLTTGDIDEaysTPVEEIMSKEVVT 87

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1901200332  140 VLSDTIAVEALQKMVQGKFRHLPVVENGEVI 170
Cdd:cd17778     88 IEPDADIAEAARLMIKKNVGSLLVVDDEGEL 118

Sugar phosphate permease [Carbohydrate transport and metabolism];

Pssm-ID: 441872 [Multi-domain] Cd Length: 363 Bit Score: 43.71 E-value: 4.82e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  547 WLVFVCAMwiqSVAGVGYLFGGSMSPAIKTSLGYNQKQIALLGVAKNLGDAIG-FVSGALSE--VSPSWVVLLVGatqnL 623
Cdd:COG2271    183 WLLALAYF---LVYFALYGFLTWLPTYLVEVRGLSLAQAGLLLSLPFLAGIVGsLLGGWLSDrlGRRRKLVLAIG----L 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  624 VGYGVVWLVVtGQLPNLPLWMLFVAIFVGTNGETYYNTASLVSciHNFP-ESRGPVVGILKGFSGLSGAILTQVY-LMFN 701
Cdd:COG2271    256 LLAALALLLL-ALLPSPALAIALLFLAGFGLGGAFGLLWALAA--ELFPkKARGTASGLVNTFGFLGGALGPLLVgYLLD 332

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1901200332  702 PSHDSSVILMVALGPPVVVLALLFIVRPVER 732
Cdd:COG2271    333 ATGYQAAFLLLAALALLAALLALLLLRETRK 363

Sugar phosphate permease [Carbohydrate transport and metabolism];

Pssm-ID: 441872 [Multi-domain] Cd Length: 363 Bit Score: 43.32 E-value: 6.88e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  546 RWLVFVCAMWIQSVAGVGYLFGGSMSPAIKTSLGYNQKQIALLGVAKNLGDAIG-FVSGALSEVSPSWVVLLVGatqnLV 624
Cdd:COG2271      8 RWRILALLFLAYFLNYLDRSNLSVAAPPLQADLGLSAAQLGLLASAFFLGYALGqIPAGLLADRFGRRRVLAIG----LL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  625 GYGVVWLVvTGQLPNLplWMLFVAIFVGTNGETYYNTASLVSCIHNFPES-RGPVVGILKGFSGLsGAILTQVYLMFNPS 703
Cdd:COG2271     84 LWGLATLL-FGFATSF--WQLLLLRFLLGLGEAGFFPAALKLIAEWFPPKeRGRALGIFNAGGPL-GGALAPPLLGWLLA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1901200332  704 HDSSVILMVALGPPVVVLALLFIVrpverscrmnlrsddlrFLAIYGFCVVLAVY 758
Cdd:COG2271    160 AFGWRAAFLILGLPGLLLALLRFW-----------------LLALAYFLVYFALY 197

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: 40.62 E-value: 7.69e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI--------------ATKVIAKQLNLEETPVSKVMTKNP 137
Cdd:cd04600      6 VTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLlkhadldpprglrgRLRRTLGLRRDRPETVGDIMTRPV 85

                           90       100
                   ....*....|....*....|....*....
gi 1901200332  138 VFVLSDTIAVEALQKMVQGKFRHLPVVEN 166
Cdd:cd04600     86 VTVRPDTPIAELVPLFSDGGLHHIPVVDA 114

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: 40.38 E-value: 7.87e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  265 MVMV--ENKLVGILTSKDILMRVISQNLPQeTTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDkDGDVVAVI 342
Cdd:cd17771     30 MVVVdaNRRPVGIFTLRDLLSRVALPQIDL-DAPISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVD-NGRLVGVV 107

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: 39.81 E-value: 8.54e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1901200332  269 ENKLVGILTSKDIlmrvisQNLPQETTTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd04583     34 DNVLLGIVDIEDI------NRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLV 101

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: 40.02 E-value: 8.61e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   66 LRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKviakqlnleetpVSKVMTK-NPVFVLSDT 144
Cdd:cd04597      2 LEYDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIART------------VDYIMTKdNLIVFKEDD 69

                           90       100
                   ....*....|....*....|..
gi 1901200332  145 IAVEALQKMVQGKFRHLPVVEN 166
Cdd:cd04597     70 YLDEVKEIMLNTNFRNYPVVDE 91

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: 39.91 E-value: 9.35e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1901200332  296 TVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd04605      1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIV 47

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: 39.63 E-value: 1.01e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  101 NALLCGILTDRDiatkVIAKQLNleeTPVSKVMTKNPVFVLSDTIAVEALQKMVQGKFRHLPVVENGEVIALLDIaKCLY 180
Cdd:cd04599     34 NGKLVGIITSRD----VRRAHPN---RLVADAMSRNVVTISPEASLWEAKELMEEHGIERLVVVEEGRLVGIITK-STLY 105

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: 39.73 E-value: 1.06e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1901200332  301 MTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:cd04629      1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFL 42

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

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 39.82 E-value: 1.18e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   62 TVKRLRLCKALTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLeETPVSKVMTKN-PVFV 140
Cdd:cd04608      3 IVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQP-SDPVSKAMYKQfKQVD 81


                   ....*.
gi 1901200332  141 LSDTIA 146
Cdd:cd04608     82 LDTPLG 87

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: 39.45 E-value: 1.34e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI 113
Cdd:cd17775     72 ITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113

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: 39.48 E-value: 1.64e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901200332  269 ENKLVGILTSKDILmRVISQNLPQetTTVEKVMTPNPESATV--DMAIVEALHIMHNGKFLHLPVLDKDGDVVAVID 343
Cdd:cd04639     39 AGRLVGLITVDDLR-AIPTSQWPD--TPVRELMKPLEEIPTVaaDQSLLEVVKLLEEQQLPALAVVSENGTLVGLIE 112

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: 39.31 E-value: 1.65e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  238 TKVLKVGLDETVLGVTMKMVEYQSSAAMVMVENKLVGILTSKDILMRVISQNLPQETTTVEKVMTPNPESATVDMAIVEA 317
Cdd:cd17776      3 TDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALHAGYATDDPFSEIPVRAVASRPLVTISPTATLREA 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1901200332  318 LHIMHNGKFLHLPVLDkDGDVVAVIDVIHITHA 350
Cdd:cd17776     83 AERMVDEGVKKLPVVD-GLDLVGILTATDIIRA 114

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: 1.83e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1901200332   137 PVFVLSDTIAV-EALQKMVQGKFRHLPVV-ENGEVIALL---DIAKCLY 180
Cdd:smart00116    1 DVVTVSPDTTLeEALELLRENGIRRLPVVdEEGRLVGIVtrrDIIKALA 49

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

Pssm-ID: 341422 [Multi-domain] Cd Length: 114 Bit Score: 39.05 E-value: 2.14e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVIAKQLNLEETPVSKVMTKNPVFVLSD 143
Cdd:cd17786      6 TINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIIKRFIPRNVKPDEVPVKLVMRKPIPKVKSD 76

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: 39.24 E-value: 2.73e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1901200332   72 LTVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDI 113
Cdd:cd17778     86 VTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127

arabinose-5-phosphate isomerase KdsD;

Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 40.86 E-value: 2.99e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIaTKVIAKQLNLEETPVSKVMTKNPVFVLSDTIAVEALQK 152
Cdd:PRK10892   216 HVSKTASLRDALLEITRKNLGMTVICDDNMKIEGIFTDGDL-RRVFDMGIDLRQASIADVMTPGGIRVRPGILAVDALNL 294

                           90       100
                   ....*....|....*....|.
gi 1901200332  153 MVQGKFRHLPVVENGEVIALL 173
Cdd:PRK10892   295 MQSRHITSVLVADGDHLLGVL 315

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 38.32 E-value: 3.86e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  266 VMVENKLVGILTSKDIlmrvisQNLPQET---TTVEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDkDGDVVAVI 342
Cdd:cd04801     33 VVENGRLVGIVTLEDI------RKVPEVEreaTRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVE-DGELVGII 105

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: 38.47 E-value: 3.87e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   73 TVPDSTTLFEACRRMAARRVDALLLTDSNALLCGILTDRDIATKVI---------------AKQLNLeetPVSKVMTKNP 137
Cdd:cd04632      6 TVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVrpgtktrggdrggekERMLDL---PVYDIMSSPV 82

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1901200332  138 VFVLSDTIAVEALQKMVQGKFRHLPVV-ENGEVIALL 173
Cdd:cd04632     83 VTVTRDATVADAVERMLENDISGLVVTpDDNMVIGIL 119

hypothetical protein; Provisional

Pssm-ID: 140234 [Multi-domain] Cd Length: 591 Bit Score: 40.58 E-value: 5.41e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901200332  653 TNGETYYNTASLVSCIHNFPESRGPVVGILKGFSGLSGAILTQVYL-MFNPSHDSSVILMVALGPPVVVLALLFIVRP 729
Cdd:PTZ00207   131 TLGCMLFDLGAVVTVLSVFPSNRGAVVAIMKTFTGLGSAILGSIQLaFFSDNTSAYFFFLMSFALVVGILAIVFMRLP 208

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 37.89 E-value: 5.44e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1901200332  297 VEKVMTPNPESATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:COG2905      1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGII 46

inosine-5'-monophosphate dehydrogenase; Provisional

Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 40.34 E-value: 6.00e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901200332  104 LCGILTDRDIatkviaKQLNLEETPVSKVMTKNP-VFVLSDTIAV-EALQKMVQGKFRHLPVV-ENGEVIAL 172
Cdd:PTZ00314   142 LLGIVTSRDI------DFVKDKSTPVSEVMTPREkLVVGNTPISLeEANEVLRESRKGKLPIVnDNGELVAL 207

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: 37.31 E-value: 7.89e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332   72 LTVPDSTTLFEACRRMaaRR-------VDALLLTDSNALLCGILTDRDIatkVIAKqlnlEETPVSKVMTKNPVFVLSDT 144
Cdd:cd04606     12 VAVRPDWTVEEALEYL--RRlapdpetIYYIYVVDEDRRLLGVVSLRDL---LLAD----PDTKVSDIMDTDVISVSADD 82

                           90       100
                   ....*....|....*....|....*.
gi 1901200332  145 IAVEALQKMVQGKFRHLPVVENGEVI 170
Cdd:cd04606     83 DQEEVARLFAKYDLLALPVVDEEGRL 108

IMP dehydrogenase;

Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 40.07 E-value: 8.35e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901200332  226 FKPSLSTIIPENTkvlkvgldetvLGVTMKMVEYQSSAAMVMVEN-----KLVGILTSKDILMRVISQNLPqetttVEKV 300
Cdd:PRK07107   103 FVVSDSNLTPDNT-----------LADVLDLKEKTGHSTVAVTEDgtahgKLLGIVTSRDYRISRMSLDTK-----VKDF 166

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1901200332  301 MTPNPE--SATVDMAIVEALHIMHNGKFLHLPVLDKDGDVVAVI 342
Cdd:PRK07107   167 MTPFEKlvTANEGTTLKEANDIIWDHKLNTLPIVDKNGNLVYLV 210