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 569008110 428 VVEEVLTPLGDCFMLRSDAvLDFATVSEILRSGYTRIPVYEGDqRHNIVDILFVKDLAFVDPDDCTPllTVTRFYNRPLH 507
Cdd:cd04590    1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGD-LDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569008110 508 CVFNDTRLDTVLEEFKKGKSHLAIVQrvnnegegDPFYEVMGIVTL 553
Cdd:cd04590   77 FVPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTL 114

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 569008110 428 VVEEVLTPLGDCFMLRSDAvLDFATVSEILRSGYTRIPVYEGDqRHNIVDILFVKDLAFVDPDDCTPllTVTRFYNRPLH 507
Cdd:cd04590    1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGD-LDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569008110 508 CVFNDTRLDTVLEEFKKGKSHLAIVQrvnnegegDPFYEVMGIVTL 553
Cdd:cd04590   77 FVPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTL 114

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008110  250 DPVELRVLRNSGSAAeqeqARRVQAVRGRGTHLLCTLLLGQAGANAaLAGWLYASLPPGVGDPGEDSGeagvhfPWLPAL 329
Cdd:pfam01595  24 RRSRLEELAEKGNKG----AKRLLKLLANPDRLLSTLLIGNTLANI-LLGALATALFAELLAPLGALG------VAIATV 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569008110  330 VCTGAVFLGAEICPYSVCSRHGLAIASHSVCLTRLLMAAAFPVCYPLGRLLDWALR------QEISTFYTREKL 397
Cdd:pfam01595  93 LVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRlfgvkgGESEPAVTEEEL 166

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008110 451 ATVSE----ILRSGYTRIPVYEGDQrhnIVDILFVKDLAFVDPDDCTPL-LTVTRFYNRPLHCVFNDTRLDTVLEEFKKG 525
Cdd:COG2524  103 TTLEEalelMLEKGISGLPVVDDGK---LVGIITERDLLKALAEGRDLLdAPVSDIMTRDVVTVSEDDSLEEALRLMLEH 179

                         90       100
                 ....*....|....*....|....*..
gi 569008110 526 KSHLAIVqrVNNEGEgdpfyeVMGIVT 552
Cdd:COG2524  180 GIGRLPV--VDDDGK------LVGIIT 198

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 569008110 428 VVEEVLTPLGDCFMLRSDAvLDFATVSEILRSGYTRIPVYEGDqRHNIVDILFVKDLAFVDPDDCTPllTVTRFYNRPLH 507
Cdd:cd04590    1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGD-LDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569008110 508 CVFNDTRLDTVLEEFKKGKSHLAIVQrvnnegegDPFYEVMGIVTL 553
Cdd:cd04590   77 FVPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTL 114

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 569008110 254 LRVLRNSGSAAeqeqARRVQAVRGRGTHLLCTLLLGQAGAN---AALAGWLYASLppgvgdpgedSGEAGVhfpWLPALV 330
Cdd:COG4536   38 LRHLAKKGHKG----AKRVLKLLERPDRLIGTILLGNNLVNilaSSLATVIAIRL----------FGDAGV---AIATLV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008110 331 CTGAVFLGAEICPYSVCSRHGLAIASHSVCLTRLLMAaafpVCYPLGRLLDWA----LR-------QEISTFYTREKLLE 399
Cdd:COG4536  101 LTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLK----LLYPLVWLVNLIvrglLRlfgvkpdADASDLLSEEELRT 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008110 400 TLRAADPYSDLVKEELNIIQGALELRTKVVEEVLTPLGDCFMLrsDAVLDFAT-VSEILRSGYTRIPVYEGDQrHNIVDI 478
Cdd:COG4536  177 VVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGI--DLDDPWEEiLKQLLTSPHTRLPVYRGDI-DNIVGV 253

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569008110 479 LFVKDLAFVDPDDCTPLLTVTRfYNRPLHCVFNDTRLDTVLEEFKKGKSHLAIVqrVNNEGEgdpfyeVMGIVTLED 555
Cdd:COG4536  254 LHVRDLLRALRKGDLSKEDLRK-IAREPYFIPETTPLSTQLQNFQKRKRRFALV--VDEYGD------VQGLVTLED 321

magnesium/cobalt transporter CorC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008110 394 REKLLETLRAADPySDLVKEEL-NIIQGALELRTKVVEEVLTPLGDCFMLRSDAVLDfATVSEILRSGYTRIPVYEGDQR 472
Cdd:PRK15094  34 RDELLALIRDSEQ-NDLIDEDTrDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008110 473 HnIVDILFVKDLAFVDPDDCTPLlTVTRFYnRPLHCVFNDTRLDTVLEEFKKGKSHLAIVQrvnnegegDPFYEVMGIVT 552
Cdd:PRK15094 112 H-IEGILMAKDLLPFMRSDAEAF-SMDKVL-RQAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                 .
gi 569008110 553 L 553
Cdd:PRK15094 181 I 181

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 569008110 451 ATVSEILR----SGYTRIPVYEGDQRhnIVDILFVKDLA-FVDPDDCTPLLTVTRFYNRPLHCVFNDTRLDTVLEEFKKG 525
Cdd:cd02205   11 TTVREALElmaeNGIGALPVVDDDGK--LVGIVTERDILrALVEGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEH 88

                         90       100
                 ....*....|....*....|....*....
gi 569008110 526 K-SHLAIVqrvNNEGEgdpfyeVMGIVTL 553
Cdd:cd02205   89 GiRRLPVV---DDDGK------LVGIVTR 108