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Conserved domains on  [gi|917142797|ref|WP_051749509|]
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hemolysin family protein [Ureaplasma diversum]

Protein Classification

hemolysin family protein( domain architecture ID 11441338)

hemolysin family protein containing tandem repeats of the cystathionine beta-synthase (CBS pair) domain and a transporter-associated domain, similar to Methanoculleus thermophilus hemolysin

Gene Ontology:  GO:0016020|GO:0005886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 37-408 4.19e-77

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 246.95  E-value: 4.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  37 LIIGLAFLtLFLILLASFFSCTETALTSI--TKVKWKSESGNIKSKKIVNIVYKmINNY--TMTLGSNLIGSALVNTASS 112
Cdd:COG1253    3 LLLELLLI-LLLILLNGFFSASEFALVSLrrSRLEQLAEEGDKGARRALKLLED-PDRFlsTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 113 TVAGLLFSGVVRYVGAGSHAEAIGTGVATGVMTLLILIFGEFLPKNFAKKNPIKLLTWFGYPIYFFYLVFWPFTWLLNRI 192
Cdd:COG1253   81 ALAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 193 FNR---------KEKTTKTTIEELKSLVDVIKYEGTLDSQEALIINKAILFDEILIKQKMVGWDKVVKVNENDLVKDVIP 263
Cdd:COG1253  161 TNLllrllgiepAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 264 TFLETGFSRLVVINED-QEVVGIAHIKVVIKAYLNDQNTPIDSIMHSPMLITKNDTLYDGLRMMQIQQIHLAIVVDN--L 340
Cdd:COG1253  241 LILESGHSRIPVYEGDlDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEygG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917142797 341 TEknpvGIITLENITEELTGNVFDETDlsDANEWVQEVNEYTWKLDAKANAKKFlTEKINASIEVADD 408
Cdd:COG1253  321 TA----GLVTLEDILEEIVGEIRDEYD--EEEPEIVKLDDGSYLVDGRLPIDEL-NELLGLDLPEEED 381
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 37-408 4.19e-77

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 246.95  E-value: 4.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  37 LIIGLAFLtLFLILLASFFSCTETALTSI--TKVKWKSESGNIKSKKIVNIVYKmINNY--TMTLGSNLIGSALVNTASS 112
Cdd:COG1253    3 LLLELLLI-LLLILLNGFFSASEFALVSLrrSRLEQLAEEGDKGARRALKLLED-PDRFlsTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 113 TVAGLLFSGVVRYVGAGSHAEAIGTGVATGVMTLLILIFGEFLPKNFAKKNPIKLLTWFGYPIYFFYLVFWPFTWLLNRI 192
Cdd:COG1253   81 ALAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 193 FNR---------KEKTTKTTIEELKSLVDVIKYEGTLDSQEALIINKAILFDEILIKQKMVGWDKVVKVNENDLVKDVIP 263
Cdd:COG1253  161 TNLllrllgiepAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 264 TFLETGFSRLVVINED-QEVVGIAHIKVVIKAYLNDQNTPIDSIMHSPMLITKNDTLYDGLRMMQIQQIHLAIVVDN--L 340
Cdd:COG1253  241 LILESGHSRIPVYEGDlDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEygG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917142797 341 TEknpvGIITLENITEELTGNVFDETDlsDANEWVQEVNEYTWKLDAKANAKKFlTEKINASIEVADD 408
Cdd:COG1253  321 TA----GLVTLEDILEEIVGEIRDEYD--EEEPEIVKLDDGSYLVDGRLPIDEL-NELLGLDLPEEED 381
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 43-224 4.85e-41

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.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 144.67  E-value: 4.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797   43 FLTLFLILLASFFSCTETALTSITKVKWKS--ESGNIKSKKivniVYKMINNYTMTLGSNLIGSALVNTASSTVAGLLFS 120
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEElaEKGNKGAKR----LLKLLANPDRLLSTLLIGNTLANILLGALATALFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  121 GVVryvgagSHAEAIGTGVATGVMTLLILIFGEFLPKNFAKKNPIKLLTWFGYPIYFFYLVFWPFTWLLNRIFNR----- 195
Cdd:pfam01595  77 ELL------APLGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLilrlf 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 917142797  196 ----KEKTTKTTIEELKSLVDVIKYEGTLDSQE 224
Cdd:pfam01595 151 gvkgGESEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 243-356 5.67e-19

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 82.16  E-value: 5.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 243 MVGWDKVVKVNENDLVKDVIPTFLETGFSRLVVINED-QEVVGIAHIKVVIKAYLNDQ-NTPIDSIMHSPMLITKNDTLY 320
Cdd:cd04590    6 MTPRTDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDLLAALLEGReKLDLRALLRPPLFVPETTPLD 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 917142797 321 DGLRMMQIQQIHLAIVVDnltEKN-PVGIITLENITE 356
Cdd:cd04590   86 DLLEEFRKERSHMAIVVD---EYGgTAGIVTLEDILE 119
PRK11573 PRK11573
hypothetical protein; Provisional
 48-275 1.01e-09

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 60.15  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  48 LILLASFFSCTETALTSITKVKWK--SESGNIKSKKivniVYKMINNYTMTLGSNLIGSALVNTASSTVAGLlfsgvvry 125
Cdd:PRK11573   1 MVVISAYFSGSETGMMTLNRYRLRhmAKQGNRSAKR----VEKLLRKPDRLISLVLIGNNLVNILASALGTI-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 126 VGAGSHAEAiGTGVATGVMTLLILIFGEFLPKNFAKKNPIKlltwFGYPIYFFY----LVFWPFTWLLN-------RIFN 194
Cdd:PRK11573  69 VGMRLYGDA-GVAIATGVLTFVVLVFAEVLPKTIAALYPEK----VAYPSSFLLaplqILMMPLVWLLNtitrllmRLMG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 195 RKEKTTKT---TIEELKSLVDVIKYEGTLDSQEALIinkAIL-FDEILIKQKMVGWDKVVKVNENDLVKDVIPTFLETGF 270
Cdd:PRK11573 144 IKTDIVVSgalSKEELRTIVHESRSQISRRNQDMLL---SVLdLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPH 220


                 ....*
gi 917142797 271 SRLVV 275
Cdd:PRK11573 221 GRIVL 225
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 249-294 1.73e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 39.03  E-value: 1.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 917142797   249 VVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKA 294
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 37-408 4.19e-77

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 246.95  E-value: 4.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  37 LIIGLAFLtLFLILLASFFSCTETALTSI--TKVKWKSESGNIKSKKIVNIVYKmINNY--TMTLGSNLIGSALVNTASS 112
Cdd:COG1253    3 LLLELLLI-LLLILLNGFFSASEFALVSLrrSRLEQLAEEGDKGARRALKLLED-PDRFlsTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 113 TVAGLLFSGVVRYVGAGSHAEAIGTGVATGVMTLLILIFGEFLPKNFAKKNPIKLLTWFGYPIYFFYLVFWPFTWLLNRI 192
Cdd:COG1253   81 ALAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 193 FNR---------KEKTTKTTIEELKSLVDVIKYEGTLDSQEALIINKAILFDEILIKQKMVGWDKVVKVNENDLVKDVIP 263
Cdd:COG1253  161 TNLllrllgiepAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 264 TFLETGFSRLVVINED-QEVVGIAHIKVVIKAYLNDQNTPIDSIMHSPMLITKNDTLYDGLRMMQIQQIHLAIVVDN--L 340
Cdd:COG1253  241 LILESGHSRIPVYEGDlDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEygG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917142797 341 TEknpvGIITLENITEELTGNVFDETDlsDANEWVQEVNEYTWKLDAKANAKKFlTEKINASIEVADD 408
Cdd:COG1253  321 TA----GLVTLEDILEEIVGEIRDEYD--EEEPEIVKLDDGSYLVDGRLPIDEL-NELLGLDLPEEED 381
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 31-381 1.43e-57

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


Pssm-ID: 443602 [Multi-domain]  Cd Length: 420  Bit Score: 195.68  E-value: 1.43e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  31 SHWSIGLIIGLAFltlFLILLASFFSCTETALTSITKVKWKS--ESGNiKSKKIVNivyKMINNYTMTLGSNLIGSALVN 108
Cdd:COG4536    2 DDISLSLLIGILV---LLLLLSAFFSGSETALMALNRYRLRHlaKKGH-KGAKRVL---KLLERPDRLIGTILLGNNLVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 109 TASSTVAGLLFsgvVRYVGAGshaeaiGTGVATGVMTLLILIFGEFLPKNFAKKNPIKLLTWFGYPIYFFYLVFWPFTWL 188
Cdd:COG4536   75 ILASSLATVIA---IRLFGDA------GVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 189 LNRIFN----------RKEKTTKTTIEELKSLVDVIKYEGTLDSQEALIINKAILFDEILIKQKMVGWDKVVKVNENDLV 258
Cdd:COG4536  146 VNLIVRgllrlfgvkpDADASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPW 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 259 KDVIPTFLETGFSRLVVINEDQE-VVGIAHIKVVIKAYLNDQNTPID--SIMHSPMLITKNDTLYDGLRMMQIQQIHLAI 335
Cdd:COG4536  226 EEILKQLLTSPHTRLPVYRGDIDnIVGVLHVRDLLRALRKGDLSKEDlrKIAREPYFIPETTPLSTQLQNFQKRKRRFAL 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 917142797 336 VVDnltEKNPV-GIITLENITEELTGNVFDETDLSDANEWVQEVNEY 381
Cdd:COG4536  306 VVD---EYGDVqGLVTLEDILEEIVGEITDEHDPDAEEIRPQEDGSY 349
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 43-224 4.85e-41

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.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 144.67  E-value: 4.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797   43 FLTLFLILLASFFSCTETALTSITKVKWKS--ESGNIKSKKivniVYKMINNYTMTLGSNLIGSALVNTASSTVAGLLFS 120
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEElaEKGNKGAKR----LLKLLANPDRLLSTLLIGNTLANILLGALATALFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  121 GVVryvgagSHAEAIGTGVATGVMTLLILIFGEFLPKNFAKKNPIKLLTWFGYPIYFFYLVFWPFTWLLNRIFNR----- 195
Cdd:pfam01595  77 ELL------APLGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLilrlf 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 917142797  196 ----KEKTTKTTIEELKSLVDVIKYEGTLDSQE 224
Cdd:pfam01595 151 gvkgGESEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 243-356 5.67e-19

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 82.16  E-value: 5.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 243 MVGWDKVVKVNENDLVKDVIPTFLETGFSRLVVINED-QEVVGIAHIKVVIKAYLNDQ-NTPIDSIMHSPMLITKNDTLY 320
Cdd:cd04590    6 MTPRTDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDLLAALLEGReKLDLRALLRPPLFVPETTPLD 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 917142797 321 DGLRMMQIQQIHLAIVVDnltEKN-PVGIITLENITE 356
Cdd:cd04590   86 DLLEEFRKERSHMAIVVD---EYGgTAGIVTLEDILE 119
CBS COG0517
CBS domain [Signal transduction mechanisms];
237-354 9.02e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 67.97  E-value: 9.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 237 ILIKQKMVgwDKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGI---AHI-KVVIKAYLNDQNTPIDSIM-HSPM 311
Cdd:COG0517    1 MKVKDIMT--TDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIvtdRDLrRALAAEGKDLLDTPVSEVMtRPPV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 917142797 312 LITKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENI 354
Cdd:COG0517   79 TVSPDTSLEEAAELMEEHKIRRLPVVDD--DGRLVGIITIKDL 119
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 247-358 1.46e-13

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 67.16  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAH----IKVVIKAYLNDQNTPIDSIMHSPML-ITKNDTLYD 321
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITdrdlRRRVLAEGLDPLDTPVSEVMTRPPItVSPDDSLAE 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 917142797 322 GLRMMQIQQIHLAIVVDNlteKNPVGIITLENITEEL 358
Cdd:COG2905   87 ALELMEEHRIRHLPVVDD---GKLVGIVSITDLLRAL 120
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 247-354 2.82e-13

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: 66.11  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAYLNDQ---NTPIDSIMH-SPMLITKNDTLYDG 322
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGlalDTPVAEVMTpDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 917142797 323 LRMMQIQQIHLAIVVDNltEKNPVGIITLENI 354
Cdd:cd02205   82 LELMLEHGIRRLPVVDD--DGKLVGIVTRRDI 111
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
247-358 2.28e-12

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 64.16  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAylnDQNTPIDSIM-HSPMLITKNDTLYDGLRM 325
Cdd:COG4109   25 EDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK---DDDTPIEDVMtKNPITVTPDTSLASAAHK 101

                         90       100       110
                 ....*....|....*....|....*....|...
gi 917142797 326 MQIQQIHLAIVVDNltEKNPVGIITLENITEEL 358
Cdd:COG4109  102 MIWEGIELLPVVDD--DGRLLGIISRQDVLKAL 132
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
248-354 2.58e-12

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 64.12  E-value: 2.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAYLND---------QNTPIDSIMHSPML-ITKND 317
Cdd:COG3448   11 DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDrldeleerlLDLPVEDVMTRPVVtVTPDT 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 917142797 318 TLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENI 354
Cdd:COG3448   91 PLEEAAELMLEHGIHRLPVVDD--DGRLVGIVTRTDL 125
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
248-358 3.00e-12

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 65.68  E-value: 3.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVInEDQEVVGIAHIKVVIKAYLNDQ---NTPIDSIMHSPML-ITKNDTLYDGL 323
Cdd:COG2524   95 DVITVSPDTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLLKALAEGRdllDAPVSDIMTRDVVtVSEDDSLEEAL 173

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 917142797 324 RMMQIQQIHLAIVVDNltEKNPVGIITLENITEEL 358
Cdd:COG2524  174 RLMLEHGIGRLPVVDD--DGKLVGIITRTDILRAL 206
PRK11573 PRK11573
hypothetical protein; Provisional
 48-275 1.01e-09

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 60.15  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797  48 LILLASFFSCTETALTSITKVKWK--SESGNIKSKKivniVYKMINNYTMTLGSNLIGSALVNTASSTVAGLlfsgvvry 125
Cdd:PRK11573   1 MVVISAYFSGSETGMMTLNRYRLRhmAKQGNRSAKR----VEKLLRKPDRLISLVLIGNNLVNILASALGTI-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 126 VGAGSHAEAiGTGVATGVMTLLILIFGEFLPKNFAKKNPIKlltwFGYPIYFFY----LVFWPFTWLLN-------RIFN 194
Cdd:PRK11573  69 VGMRLYGDA-GVAIATGVLTFVVLVFAEVLPKTIAALYPEK----VAYPSSFLLaplqILMMPLVWLLNtitrllmRLMG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 195 RKEKTTKT---TIEELKSLVDVIKYEGTLDSQEALIinkAIL-FDEILIKQKMVGWDKVVKVNENDLVKDVIPTFLETGF 270
Cdd:PRK11573 144 IKTDIVVSgalSKEELRTIVHESRSQISRRNQDMLL---SVLdLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPH 220


                 ....*
gi 917142797 271 SRLVV 275
Cdd:PRK11573 221 GRIVL 225
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
185-394 4.56e-08

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 54.43  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 185 FTWLLNRIFNRKEKTTKTTIE-----ELKSLVDvikyEGTLDSQEALIInkailFDEILIKQKMVGWDKVVKVNENDLVK 259
Cdd:PRK15094  19 FSLLLSQLFHGEPKNRDELLAlirdsEQNDLID----EDTRDMLEGVMD-----IADQRVRDIMIPRSQMITLKRNQTLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 260 DVIPTFLETGFSRLVVINEDQE-VVGIAHIKVVIKAYLNDQNT-PIDSIMHSPMLITKNDTLYDGLRMMQIQQIHLAIVV 337
Cdd:PRK15094  90 ECLDVIIESAHSRFPVISEDKDhIEGILMAKDLLPFMRSDAEAfSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVI 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 917142797 338 DNLTEKNpvGIITLENITEELTGNVFDETDLSDANEwVQEVNEYTWKLDAKANAKKF 394
Cdd:PRK15094 170 DEFGGVS--GLVTIEDILELIVGEIEDEYDEEDDID-FRQLSRHTWTVRALASIEDF 223
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 243-351 5.17e-08

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: 51.23  E-value: 5.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 243 MVGWDKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGI--------AhikvvIKAYLNDQNTPIDSIM-HSPMLI 313
Cdd:cd04604    9 MHTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIitdgdlrrA-----LEKGLDILNLPAKDVMtRNPKTI 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 917142797 314 TKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITL 351
Cdd:cd04604   84 SPDALAAEALELMEEHKITVLPVVDE--DGKPVGILHL 119
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 247-356 2.12e-07

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: 49.01  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAylnDQNTPIDSIMH-SPMLITKNDTLYDGLRM 325
Cdd:cd04596    2 EETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGK---EDDTPIEKVMTkNPITVKPKTSVASAAHM 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 917142797 326 MQIQQIHLAIVVDNltEKNPVGIITLENITE 356
Cdd:cd04596   79 MIWEGIELLPVVDE--NRKLLGVISRQDVLK 107
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 247-358 3.06e-07

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: 48.67  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAH----IKVVikAYLNDQNTPIDSIM-HSPMLITKNDTLYD 321
Cdd:cd09836    3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTerdiVRAV--AEGIDLDTPVEEIMtKNLVTVSPDESIYE 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 917142797 322 GLRMMQIQQIHLAIVVDNltEKNPVGIITLENITEEL 358
Cdd:cd09836   81 AAELMREHNIRHLPVVDG--GGKLVGVISIRDLAREL 115
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 247-356 6.88e-07

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: 48.10  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIK----VVIKAYLNDQ------------NTPIDSIMHSP 310
Cdd:cd04632    2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYdivdFVVRPGTKTRggdrggekermlDLPVYDIMSSP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 917142797 311 ML-ITKNDTLYDGLRMMQIQQIHLAIVVDNLTEknPVGIITLENITE 356
Cdd:cd04632   82 VVtVTRDATVADAVERMLENDISGLVVTPDDNM--VIGILTKTDVLR 126
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 248-350 1.43e-06

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: 46.76  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVInEDQEVVGIAHIKVVIKAYL-NDQNTPIDSIMhSPMLIT--KNDTLYDGLR 324
Cdd:cd04588    3 DLITLKPDATIKDAAKLLSENNIHGAPVV-DDGKLVGIVTLTDIAKALAeGKENAKVKDIM-TKDVITidKDEKIYDAIR 80

                         90       100
                 ....*....|....*....|....*.
gi 917142797 325 MMQIQQIHLAIVVDNltEKNPVGIIT 350
Cdd:cd04588   81 LMNKHNIGRLIVVDD--NGKPVGIIT 104
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
248-298 4.50e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 46.01  E-value: 4.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAYLND 298
Cdd:COG3448   82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARL 132
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 248-358 1.71e-05

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: 44.07  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAH----IKVVIKAYLNDQNTPIDSIMHSPML-ITKNDTLYDG 322
Cdd:cd17775    4 EVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTdrdiVVEVVAKGLDPKDVTVGDIMSADLItAREDDGLFEA 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 917142797 323 LRMMQIQQIHLAIVVDNltEKNPVGIITLENITEEL 358
Cdd:cd17775   84 LERMREKGVRRLPVVDD--DGELVGIVTLDDILELL 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 247-297 2.06e-05

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: 41.82  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 917142797  247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAYLN 297
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 252-339 5.97e-05

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: 341421 [Multi-domain]  Cd Length: 136  Bit Score: 42.64  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 252 VNENDLVKDVIPTFLETGFSRLV-VINEDQEVVGIAHIKVVIKA-YLND-----------------QNTPIDSIMHSPML 312
Cdd:cd17785   15 VHENTSIRDVIDKMIEDPKTRSVyVVDDDEKLLGIITLMELLKYiGYRFgvtiykgvsfglllrisLKEKAKDIMLSPIY 94

                         90       100
                 ....*....|....*....|....*..
gi 917142797 313 ITKNDTLYDGLRMMQIQQIHLAIVVDN 339
Cdd:cd17785   95 VKKEDTLEEALELMVKNRLQELPVVDE 121
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
227-295 9.23e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 43.33  E-value: 9.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917142797 227 IINKAILFDEILIKQKMVgwDKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAY 295
Cdd:COG2524  140 ALAEGRDLLDAPVSDIMT--RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
248-299 9.93e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 42.16  E-value: 9.93e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAYLNDQ 299
Cdd:COG0517   76 PPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPL 127
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 246-354 1.21e-04

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 41.73  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 246 WDKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIaHIKV-VI-----KAYLNDQNTPIDSIMHSPMLI------ 313
Cdd:cd04641    2 YENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDI-YAKFdVInlaaeKTYNNLDLTVGEALQHRSEDFegvhtc 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 917142797 314 TKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENI 354
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDE--EDRLEGIVSLSDI 119
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 250-355 1.22e-04

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 41.70  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 250 VKVNENDLVKDVIPT-FLE-TGfsRLVVINEDQEVVGIAHIKVVIKAYLNDQN---TPIDSIMhSPM----LITKNDTLY 320
Cdd:cd04617    7 VVVDETTSVYDAIVTlFLEdVG--SLFVVDEEGYLVGVVSRKDLLKATLGGQDlekTPVSMIM-TRMpnivTVTPDDSVL 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 917142797 321 DGLRMMQIQQIH-LAIVVDNLTEKNPVGIITLENIT 355
Cdd:cd04617   84 EAARKLIEHEIDsLPVVEKEDGKLKVVGRITKTNIT 119
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 249-294 1.73e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 39.03  E-value: 1.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 917142797   249 VVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKA 294
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 274-351 2.88e-04

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: 40.48  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 274 VVINEDQEVVGIahikV-----VIKAY---LNDQNTPIDSIMHSPML-ITKNDTLYDGLRMMQIQQIHLAIVVDNltEKN 344
Cdd:cd04622   29 LPVCEGDRLVGM----VtdrdiVVRAVaegKDPNTTTVREVMTGDVVtCSPDDDVEEAARLMAEHQVRRLPVVDD--DGR 102


                 ....*..
gi 917142797 345 PVGIITL 351
Cdd:cd04622  103 LVGIVSL 109
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 249-350 4.23e-04

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: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 249 VVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIKAYLND---QNTPIDSIMHSPM-LITKNDTLYDGLR 324
Cdd:cd04608   12 PVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGraqPSDPVSKAMYKQFkQVDLDTPLGALSR 91

                         90       100
                 ....*....|....*....|....*.
gi 917142797 325 MMqiQQIHLAIVVDNLTEknPVGIIT 350
Cdd:cd04608   92 IL--ERDHFALVVDGQGK--VLGIVT 113
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 296-354 1.17e-03

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: 39.06  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 296 LNDQNTPIDSIMHSPM-LITKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENI 354
Cdd:cd17774   64 LDLSQTQAQTVMSSPLfSLRPDDSLWTAHQLMQQRRIRRLVVVGE--QGELLGIVTQTSL 121
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 303-350 1.74e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.27  E-value: 1.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 917142797 303 IDSIMHSPML-ITKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIIT 350
Cdd:COG2905    1 VKDIMSRDVVtVSPDATVREAARLMTEKGVGSLVVVDD--DGRLVGIIT 47
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 248-350 2.48e-03

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: 37.69  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVInEDQEVVGIAHIKVVIKAylnDQNTPIDSIMHSPMLITKND-TLYDGLRMM 326
Cdd:cd04610    4 DVITVSPDDTVKDVIKLIKETGHDGFPVV-DDGKVVGYVTAKDLLGK---DDDEKVSEIMSRDTVVADPDmDITDAARVI 79

                         90       100
                 ....*....|....*....|....
gi 917142797 327 QIQQIHLAIVVDNltEKNPVGIIT 350
Cdd:cd04610   80 FRSGISKLPVVDD--EGNLVGIIT 101
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 247-293 2.51e-03

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: 37.61  E-value: 2.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 917142797 247 DKVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAHIKVVIK 293
Cdd:cd02205   67 PDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 307-357 3.56e-03

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: 37.54  E-value: 3.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 917142797 307 MHSPMLITKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENITEE 357
Cdd:cd04640    4 RVPPVTIDPDVSADEALEKMIRRGVRLLLVVDA--NNRVIGLITARDILGE 52
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 303-360 3.68e-03

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: 35.65  E-value: 3.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 917142797  303 IDSIMHSPML-ITKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENITEELTG 360
Cdd:pfam00571   1 VKDIMTKDVVtVSPDTTLEEALELMREHGISRLPVVDE--DGKLVGIVTLKDLLRALLG 57
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 248-350 4.30e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 37.03  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 248 KVVKVNENDLVKDVIPTFLETGFSRLVVINEDQEVVGIAH----IKVVIKA-YLNDQNTPIDSIMHS-PMLITKNDTLYD 321
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSeqdcLKALLEAsYHCEPGGTVADYMSTeVLTVSPDTSIVD 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 917142797 322 GLRMMQIQQIHLAIVVDN--LteknpVGIIT 350
Cdd:cd04629   84 LAQLFLKNKPRRYPVVEDgkL-----VGQIS 109
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
303-378 7.16e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 36.77  E-value: 7.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917142797 303 IDSIMHSPML-ITKNDTLYDGLRMMQIQQIHLAIVVDNltEKNPVGIITLENITEELTGNVFDETDLSDANEWVQEV 378
Cdd:COG3448    4 VRDIMTRDVVtVSPDTTLREALELMREHGIRGLPVVDE--DGRLVGIVTERDLLRALLPDRLDELEERLLDLPVEDV 78
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 273-354 7.20e-03

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: 36.75  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917142797 273 LVVinEDQEVVGIAHIKVVIK---AYLNDQNTPIDSIMHSPmLIT----KNDTLYDGLRMMQIQQI-HLAIVVDnltEKN 344
Cdd:cd04620   50 LVV--ENQQLVGIFTERDVVRltaSGIDLSGVTIAEVMTQP-VITlkesEFQDIFTVLSLLRQHQIrHLPIVDD---QGQ 123

                         90
                 ....*....|
gi 917142797 345 PVGIITLENI 354
Cdd:cd04620  124 LVGLITPESL 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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