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Conserved domains on  [gi|1543211327|ref|WP_126108038|]
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hemolysin family protein [Corynebacterium amycolatum]

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 ...
 13-341 6.42e-90

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 275.84  E-value: 6.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  13 NAWFVAAEFAMVSARRDQIEPDAVSGSTSAKYALRGIENVSVSLAATQLGITACSLLIGAVGEPAIAHFFEPYMTALGLP 92
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  93 AGTAHVVALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLNPVIWAMNTTSNIVVRkVLRATPKDE 172
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLR-LLGIEPAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 173 vDSSFTASQVQDFVAESGRQGLLDNDELALLHKALGFEHLTAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITD 252
Cdd:COG1253   176 -EPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 253 ADS-SFIGYLHVKDLLSLDdgHRNRPFP-RNLIRTFASVSPDAKLQTVMRLMQREQAHFALVTEEN-STSessvnGIVAL 329
Cdd:COG1253   255 GDLdDIVGVVHVKDLLRAL--LEGEPFDlRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYgGTA-----GLVTL 327

                         330
                  ....*....|..
gi 1543211327 330 EDVLEELVGEVR 341
Cdd:COG1253   328 EDILEEIVGEIR 339
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 13-341 6.42e-90

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 275.84  E-value: 6.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  13 NAWFVAAEFAMVSARRDQIEPDAVSGSTSAKYALRGIENVSVSLAATQLGITACSLLIGAVGEPAIAHFFEPYMTALGLP 92
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  93 AGTAHVVALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLNPVIWAMNTTSNIVVRkVLRATPKDE 172
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLR-LLGIEPAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 173 vDSSFTASQVQDFVAESGRQGLLDNDELALLHKALGFEHLTAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITD 252
Cdd:COG1253   176 -EPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 253 ADS-SFIGYLHVKDLLSLDdgHRNRPFP-RNLIRTFASVSPDAKLQTVMRLMQREQAHFALVTEEN-STSessvnGIVAL 329
Cdd:COG1253   255 GDLdDIVGVVHVKDLLRAL--LEGEPFDlRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYgGTA-----GLVTL 327

                         330
                  ....*....|..
gi 1543211327 330 EDVLEELVGEVR 341
Cdd:COG1253   328 EDILEEIVGEIR 339
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 13-199 4.35e-36

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: 128.87  E-value: 4.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  13 NAWFVAAEFAMVSARRDQIEPDAVSGSTSAKYALRGIENVSVSLAATQLGITACSLLIGAVGEPAIAHFFEPymtalglp 92
Cdd:pfam01595  10 SAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAP-------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  93 agtAHVVALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLNPVIWAMNTTSNIVVRkvLRATPKDE 172
Cdd:pfam01595  82 ---LGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILR--LFGVKGGE 156

                         170       180
                  ....*....|....*....|....*..
gi 1543211327 173 VDSSFTASQVQDFVAESGRQGLLDNDE 199
Cdd:pfam01595 157 SEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 213-334 2.95e-23

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: 92.94  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 213 TAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITDADS-SFIGYLHVKDLLSLDDGHRNRPFPRNLIRTFASVSP 291
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLdNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1543211327 292 DAKLQTVMRLMQREQAHFALVTEENstseSSVNGIVALEDVLE 334
Cdd:cd04590    81 TTPLDDLLEEFRKERSHMAIVVDEY----GGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
184-340 1.23e-07

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 52.50  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 184 DFVAESGRQGLLDNDELALLHKALGFEHLTAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITDADSSFI-GYLH 262
Cdd:PRK15094   39 ALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIeGILM 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543211327 263 VKDLLSLDDGHrNRPFPRNLIRTFASVSPDAK-LQTVMRLMQREQAHFALVTEENStsesSVNGIVALEDVLEELVGEV 340
Cdd:PRK15094  119 AKDLLPFMRSD-AEAFSMDKVLRQAVVVPESKrVDRMLKEFRSQRYHMAIVIDEFG----GVSGLVTIEDILELIVGEI 192
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 224-269 2.13e-03

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: 35.57  E-value: 2.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1543211327  224 LVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSL 269
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 13-341 6.42e-90

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 275.84  E-value: 6.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  13 NAWFVAAEFAMVSARRDQIEPDAVSGSTSAKYALRGIENVSVSLAATQLGITACSLLIGAVGEPAIAHFFEPYMTALGLP 92
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  93 AGTAHVVALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLNPVIWAMNTTSNIVVRkVLRATPKDE 172
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLR-LLGIEPAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 173 vDSSFTASQVQDFVAESGRQGLLDNDELALLHKALGFEHLTAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITD 252
Cdd:COG1253   176 -EPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 253 ADS-SFIGYLHVKDLLSLDdgHRNRPFP-RNLIRTFASVSPDAKLQTVMRLMQREQAHFALVTEEN-STSessvnGIVAL 329
Cdd:COG1253   255 GDLdDIVGVVHVKDLLRAL--LEGEPFDlRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYgGTA-----GLVTL 327

                         330
                  ....*....|..
gi 1543211327 330 EDVLEELVGEVR 341
Cdd:COG1253   328 EDILEEIVGEIR 339
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 13-199 4.35e-36

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: 128.87  E-value: 4.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  13 NAWFVAAEFAMVSARRDQIEPDAVSGSTSAKYALRGIENVSVSLAATQLGITACSLLIGAVGEPAIAHFFEPymtalglp 92
Cdd:pfam01595  10 SAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAP-------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  93 agtAHVVALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLNPVIWAMNTTSNIVVRkvLRATPKDE 172
Cdd:pfam01595  82 ---LGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILR--LFGVKGGE 156

                         170       180
                  ....*....|....*....|....*..
gi 1543211327 173 VDSSFTASQVQDFVAESGRQGLLDNDE 199
Cdd:pfam01595 157 SEPAVTEEELRSLVEESAEEGVIEEEE 183
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 14-339 6.11e-34

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: 129.04  E-value: 6.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  14 AWFVAAEFAMVSARRDQIEPDAVSGSTSAKYALRGIENVSVSLAATQLGITACSllIGAvgePAIAhffepymTALGLPA 93
Cdd:COG4536    21 AFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVN--ILA---SSLA-------TVIAIRL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  94 -GTAhvvALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLNPVIWAMNTTSNIVVRkVLRATPKDE 172
Cdd:COG4536    89 fGDA---GVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLR-LFGVKPDAD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 173 VDSSFTASQVQDFVAESGRQGLLDNDELALLHKALGFEHLTAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITD 252
Cdd:COG4536   165 ASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 253 ADS-SFIGYLHVKDLLSLDdghRNRPFPRNLIRTFAS----VSPDAKLQTVMRLMQREQAHFALVTEENSTsessVNGIV 327
Cdd:COG4536   245 GDIdNIVGVLHVRDLLRAL---RKGDLSKEDLRKIARepyfIPETTPLSTQLQNFQKRKRRFALVVDEYGD----VQGLV 317

                         330
                  ....*....|..
gi 1543211327 328 ALEDVLEELVGE 339
Cdd:COG4536   318 TLEDILEEIVGE 329
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 213-334 2.95e-23

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: 92.94  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 213 TAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITDADS-SFIGYLHVKDLLSLDDGHRNRPFPRNLIRTFASVSP 291
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLdNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1543211327 292 DAKLQTVMRLMQREQAHFALVTEENstseSSVNGIVALEDVLE 334
Cdd:cd04590    81 TTPLDDLLEEFRKERSHMAIVVDEY----GGTAGIVTLEDILE 119
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
210-336 1.43e-14

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 69.56  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 210 EHLTAADVtMQLDTLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSLDDGHR-NRPFPRNLIrtfaS 288
Cdd:COG4109    14 EILLVEDI-MTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPiEDVMTKNPI----T 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1543211327 289 VSPDAKLQTVMRLMQREQAHFALVTEENSTsessVNGIVALEDVLEEL 336
Cdd:COG4109    89 VTPDTSLASAAHKMIWEGIELLPVVDDDGR----LLGIISRQDVLKAL 132
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
211-337 1.71e-08

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 52.56  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 211 HLTAADVtMQLDtLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSLDDGHRNRPFPRNLIRTFA--- 287
Cdd:COG3448     1 AMTVRDI-MTRD-VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVedv 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1543211327 288 ------SVSPDAKLQTVMRLMQREQAHFALVTEENSTsessVNGIVALEDVLEELV 337
Cdd:COG3448    79 mtrpvvTVTPDTPLEEAAELMLEHGIHRLPVVDDDGR----LVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 224-333 2.49e-08

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: 51.48  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 224 LVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSLDDgHRNRPFPRN----LIRTFASVSPDAKLQTVM 299
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV-EGGLALDTPvaevMTPDVITVSPDTDLEEAL 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1543211327 300 RLMQREQAHFALVTEENSTsessVNGIVALEDVL 333
Cdd:cd02205    83 ELMLEHGIRRLPVVDDDGK----LVGIVTRRDIL 112
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
184-340 1.23e-07

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 52.50  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 184 DFVAESGRQGLLDNDELALLHKALGFEHLTAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITDADSSFI-GYLH 262
Cdd:PRK15094   39 ALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIeGILM 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543211327 263 VKDLLSLDDGHrNRPFPRNLIRTFASVSPDAK-LQTVMRLMQREQAHFALVTEENStsesSVNGIVALEDVLEELVGEV 340
Cdd:PRK15094  119 AKDLLPFMRSD-AEAFSMDKVLRQAVVVPESKrVDRMLKEFRSQRYHMAIVIDEFG----GVSGLVTIEDILELIVGEI 192
CBS COG0517
CBS domain [Signal transduction mechanisms];
212-341 5.18e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 47.94  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 212 LTAADVtMQLDtLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSLDDgHRNRPFPRNLIRTFAS--- 288
Cdd:COG0517     1 MKVKDI-MTTD-VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALA-AEGKDLLDTPVSEVMTrpp 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1543211327 289 --VSPDAKLQTVMRLMQREQAHFALVTEENSTsessVNGIVALEDVLEELVGEVR 341
Cdd:COG0517    78 vtVSPDTSLEEAAELMEEHKIRRLPVVDDDGR----LVGIITIKDLLKALLEPLA 128
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
68-267 2.19e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 47.96  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327  68 LLIGAVGEPAIAHFFEPYMTALGLPAGTAHVVALALALLIVTFLHMVVGEMVPKNIAIAAPSPTAKFVAIPLYVIVRVLN 147
Cdd:COG2524     1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 148 PVIWAMnTTSNIVVRKVLRATPKDevdssfTASQVQDFVAESGRQGL--LDNDELA----------LLHKALGFEHLTAA 215
Cdd:COG2524    81 GLVLKM-KVKDIMTKDVITVSPDT------TLEEALELMLEKGISGLpvVDDGKLVgiiterdllkALAEGRDLLDAPVS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1543211327 216 DVtMQLDtLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLL 267
Cdd:COG2524   154 DI-MTRD-VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDIL 203
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
224-336 4.98e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.80  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 224 LVTIGSDATVADIEELSARTRFSRFPITDaDSSFIGYLHVKDLLSLDdgHRNRPFPRNLIRTFAS-----VSPDAKLQTV 298
Cdd:COG2524    96 VITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKAL--AEGRDLLDAPVSDIMTrdvvtVSEDDSLEEA 172

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1543211327 299 MRLMQREQAHFALVTEENstseSSVNGIVALEDVLEEL 336
Cdd:COG2524   173 LRLMLEHGIGRLPVVDDD----GKLVGIITRTDILRAL 206
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 225-304 9.09e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 43.94  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 225 VTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSLDDghRNRPF-----PRNLIRTfasVSPDAKLQTVM 299
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFETD--LSTPVsevmtPDERLVT---APEGITLEEAK 79


                  ....*
gi 1543211327 300 RLMQR 304
Cdd:cd04601    80 EILHK 84
PRK11573 PRK11573
hypothetical protein; Provisional
 101-339 9.95e-06

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 47.05  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 101 LALALLIVTFLHMVVGEMVPKNIAIAAPSPTA---KFVAIPLYVIvrvLNPVIWAMNTTSNIVVRKVLRATPkDEVDSSF 177
Cdd:PRK11573   79 VAIATGVLTFVVLVFAEVLPKTIAALYPEKVAypsSFLLAPLQIL---MMPLVWLLNTITRLLMRLMGIKTD-IVVSGAL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 178 TASQVQDFVAESGRQGLLDNDElaLLHKALGFEHLTAADVTMQLDTLVTIG-SDATVADIEELS----ARTRFSRFPITD 252
Cdd:PRK11573  155 SKEELRTIVHESRSQISRRNQD--MLLSVLDLEKVTVDDIMVPRNEIVGIDiNDDWKSILRQLThsphGRIVLYRDSLDD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 253 AdssfIGYLHVKDLLSLddGHRNRPF-PRNLIRT-----FASVSPDAKLQTVMrlMQREQAHFALVTEEnstsESSVNGI 326
Cdd:PRK11573  233 A----ISMLRVREAYRL--MTEKKEFtKENMLRAadeiyFVPEGTPLSTQLVK--FQRNKKKVGLVVDE----YGDIQGL 300

                         250
                  ....*....|...
gi 1543211327 327 VALEDVLEELVGE 339
Cdd:PRK11573  301 VTVEDILEEIVGD 313
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 224-336 9.81e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 41.35  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 224 LVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLS--LDDGHRNRPFP------RNLIrtfaSVSPDAKL 295
Cdd:COG2905     9 VVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRrvLAEGLDPLDTPvsevmtRPPI----TVSPDDSL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1543211327 296 QTVMRLMQREQAHFALVTEENstsesSVNGIVALEDVLEEL 336
Cdd:COG2905    85 AEALELMEEHRIRHLPVVDDG-----KLVGIVSITDLLRAL 120
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 224-269 1.63e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 39.12  E-value: 1.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1543211327 224 LVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSL 269
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS COG0517
CBS domain [Signal transduction mechanisms];
186-267 1.63e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 41.00  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 186 VAESGR-QGLLDNDEL--ALLHKALGFEHLTAADVtMQLDtLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLH 262
Cdd:COG0517    38 VDEDGKlVGIVTDRDLrrALAAEGKDLLDTPVSEV-MTRP-PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIIT 115


                  ....*
gi 1543211327 263 VKDLL 267
Cdd:COG0517   116 IKDLL 120
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 229-334 1.90e-04

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: 40.15  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 229 SDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSLDDGHR-NRPFPRNLIrtfaSVSPDAKLQTVMRLMQREQA 307
Cdd:cd04596     9 ETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPiEKVMTKNPI----TVKPKTSVASAAHMMIWEGI 84

                          90       100
                  ....*....|....*....|....*..
gi 1543211327 308 HFALVTEENSTSEssvnGIVALEDVLE 334
Cdd:cd04596    85 ELLPVVDENRKLL----GVISRQDVLK 107
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 221-333 1.66e-03

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 37.90  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543211327 221 LDTLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSL---DDGHRNRPFPRNLIRTFASVSPDAKLQT 297
Cdd:cd04608     9 LGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSllaGRAQPSDPVSKAMYKQFKQVDLDTPLGA 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1543211327 298 VMRLMqrEQAHFALVTEENSTsessVNGIVALEDVL 333
Cdd:cd04608    89 LSRIL--ERDHFALVVDGQGK----VLGIVTRIDLL 118
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 224-269 2.13e-03

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: 35.57  E-value: 2.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1543211327  224 LVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLSL 269
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 213-268 2.52e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 36.94  E-value: 2.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1543211327 213 TAADVTMQLDTLVTIGSDATVADIEELSARTRFSRFPITDADSSFIGYLHVKDLLS 268
Cdd:cd04597    51 RTVDYIMTKDNLIVFKEDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 225-298 7.16e-03

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 38.14  E-value: 7.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1543211327 225 VTIGSDATVADIEELSARTRFSRFPITDaDSSFIGYLHVKDLLslddghrnrpFPRNLIRTFASVSPDAKLQTV 298
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDLR----------FETDLSQPVSEVMTKENLVTA 153
 
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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