Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 317 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVFEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 396
Cdd:cd04590    1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 335334953 397 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 446
Cdd:cd04590   78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 317 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVFEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 396
Cdd:cd04590    1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 335334953 397 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 446
Cdd:cd04590   78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119

magnesium/cobalt transporter CorC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 291 RERVLELARGGG-----DPYS-DLSKGVLRY--RTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERSN 362
Cdd:PRK15094  34 RDELLALIRDSEqndliDEDTrDMLEGVMDIadQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 363 IVDMLYLKDLAFVDPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 440
Cdd:PRK15094 113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                        170       180
                 ....*....|....*....|....*..
gi 335334953 441 LEDVIEEIIrSEILDESEDYSDTKVKK 467
Cdd:PRK15094 181 IEDILELIV-GEIEDEYDEEDDIDFRQ 206

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 335334953  386 ITRFYNHPLHFVFNDTKLDAVLEEF-KRGKSHLAIVqkvNNEGEgdpfyeVLGLVTLEDVIEEIIR 450
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMrEHGISRLPVV---DEDGK------LVGIVTLKDLLRALLG 57

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 317 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVFEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 396
Cdd:cd04590    1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 335334953 397 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 446
Cdd:cd04590   78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119

Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 235 LVFlvGEVLP----AAVSGRWALALAP--RAL---------GLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELAR 299
Cdd:COG4536  106 LIF--AEVTPktlaALYPEKIALPVSPplRPLlkllyplvwLVNLIVRGLLRLFGVKPDADASDLLSEEELRTVVDLGEA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 300 GGGDP--YSDLSKGV--LRYRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERSNIVDMLYLKD-LAF 374
Cdd:COG4536  184 GGVIPkeHRDMLLNIldLEDVTVEDIMVPRNEIEGIDLDDPWE-EILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDlLRA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 375 VDPEDCTP--LSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIEEIIrSE 452
Cdd:COG4536  263 LRKGDLSKedLRKIAR----EPYFIPETTPLSTQLQNFQKRKRRFALV--VDEYG------DVQGLVTLEDILEEIV-GE 329

                 ....
gi 335334953 453 ILDE 456
Cdd:COG4536  330 ITDE 333

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 233 AGLVFLVGEVLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSKGV 312
Cdd:COG2524    3 VLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 313 LRYRTVEDVLTPleDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERsnIVDMLYLKDLAFVDPEDCTPLS-TITRFYN 391
Cdd:COG2524   83 VLKMKVKDIMTK--DVITVSPDTTLE-EALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDaPVSDIMT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 335334953 392 HPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGEgdpfyeVLGLVTLEDVIEEI 448
Cdd:COG2524  158 RDVVTVSEDDSLEEALRLMLEHGIGRLPV--VDDDGK------LVGIITRTDILRAL 206

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 317 TVEDVLTPleDCFMLDSG-TVLDfsVLASIMQSGHTRIPVFEEERsNIVDMLYLKDLAF-VDPEDCTPLST-ITRFYNHP 393
Cdd:COG0517    2 KVKDIMTT--DVVTVSPDaTVRE--ALELMSEKRIGGLPVVDEDG-KLVGIVTDRDLRRaLAAEGKDLLDTpVSEVMTRP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 335334953 394 LHFVFNDTKLDAVLEEFKRGK-SHLAIVqkvnnEGEGdpfyEVLGLVTLEDVIEEIIR 450
Cdd:COG0517   77 PVTVSPDTSLEEAAELMEEHKiRRLPVV-----DDDG----RLVGIITIKDLLKALLE 125

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335334953 341 VLASIMQSGHTRIPVFEEErSNIVDMLYLKDLAFVDPEDCTPLSTITRFY-NHPLHFVFNDTKLDAVLEEFKRGK-SHLA 418
Cdd:cd02205   16 ALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPVAEVmTPDVITVSPDTDLEEALELMLEHGiRRLP 94

                         90       100
                 ....*....|....*....|....*..
gi 335334953 419 IVqkvNNEGEgdpfyeVLGLVTLEDVI 445
Cdd:cd02205   95 VV---DDDGK------LVGIVTRRDIL 112