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Conserved domains on  [gi|88196782|ref|NP_444416|]
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metal transporter CNNM3 isoform 1 precursor [Mus musculus]

Protein Classification

CBS_pair_CorC_HlyC_assoc domain-containing protein( domain architecture ID 10140050)

CBS_pair_CorC_HlyC_assoc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 319-448 2.38e-37

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: 135.32  E-value: 2.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 319 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAIVEPEDCTPlsTITRFYNHPLHF 398
Cdd:cd04590   1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 88196782 399 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 448
Cdd:cd04590  78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
COG3903 super family cl43979
Predicted ATPase [General function prediction only];
11-304 5.51e-04

Predicted ATPase [General function prediction only];


The actual alignment was detected with superfamily member COG3903:

Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  11 WLGWVLA-------AFCLGSTAGEAAPAPGAGLLNFCTEEDSAPGAGSLRGRAAPEATLCLRLFCSGLANSSWTWVAAEG 83
Cdd:COG3903 567 WLERALAaageaaaALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAA 646

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  84 AGCPEGGRATEPEEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAPPWALGLGAAGLLALAAVARGLQLS 163
Cdd:COG3903 647 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAA 726

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 164 ALALAPAEVQVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAAGQRAVPAVLGCAGLVFLVGE 243
Cdd:COG3903 727 LLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAA 806

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196782 244 VLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGG 304
Cdd:COG3903 807 AAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAA 867
 
Name Accession Description Interval E-value
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 319-448 2.38e-37

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: 135.32  E-value: 2.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 319 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAIVEPEDCTPlsTITRFYNHPLHF 398
Cdd:cd04590   1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 88196782 399 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 448
Cdd:cd04590  78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 237-461 1.71e-27

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 115.99  E-value: 1.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 237 LVFLVGEVLP----AAVSGRWALALAPRALGLSRLAvlltlpvaLPVGQLLELAAR---------PGRLRERV------- 296
Cdd:COG1253 115 LSLVFGELVPkrlaLQNPERVALLVAPPLRLFSRLF--------RPLVWLLNGSTNlllrllgiePAEEEPAVteeelra 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 297 -LELARGGG--DPY-SDLSKGVLR--SRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVYEEERSNIVDMLY 370
Cdd:COG1253 187 lVEESEESGviEEEeREMIENVFEfgDRTVREVMTPRTDVVALDLDDTLE-EALELILESGHSRIPVYEGDLDDIVGVVH 265

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 371 LKDL--AIVEPEDcTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVnnegegDPFYEVLGLVTLEDVIE 448
Cdd:COG1253 266 VKDLlrALLEGEP-FDLRDLLR----PPLFVPETKPLDDLLEEFRRERVHMAIV--V------DEYGGTAGLVTLEDILE 332

                       250
                ....*....|...
gi 88196782 449 EIIkSEILDESED 461
Cdd:COG1253 333 EIV-GEIRDEYDE 344
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
293-493 6.41e-14

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 72.92  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  293 RERVLELARGGG-----DPYS-DLSKGVL--RSRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVYEEERSN 364
Cdd:PRK15094  34 RDELLALIRDSEqndliDEDTrDMLEGVMdiADQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  365 IVDMLYLKDLAIVEPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 442
Cdd:PRK15094 113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 88196782  443 LEDVIEEIIkSEILDESEDYSDTKVRK-----KTVALGAPLKRKEEFSLFKVSDDE 493
Cdd:PRK15094 181 IEDILELIV-GEIEDEYDEEDDIDFRQlsrhtWTVRALASIEDFNEAFGTHFSDEE 235
COG3903 COG3903
Predicted ATPase [General function prediction only];
11-304 5.51e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  11 WLGWVLA-------AFCLGSTAGEAAPAPGAGLLNFCTEEDSAPGAGSLRGRAAPEATLCLRLFCSGLANSSWTWVAAEG 83
Cdd:COG3903 567 WLERALAaageaaaALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAA 646

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  84 AGCPEGGRATEPEEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAPPWALGLGAAGLLALAAVARGLQLS 163
Cdd:COG3903 647 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAA 726

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 164 ALALAPAEVQVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAAGQRAVPAVLGCAGLVFLVGE 243
Cdd:COG3903 727 LLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAA 806

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196782 244 VLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGG 304
Cdd:COG3903 807 AAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAA 867
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 388-452 8.60e-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: 35.27  E-value: 8.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196782   388 ITRFYNHPLHFVFNDTKLDAVLEEF-KRGKSHLAIVqkvNNEGEgdpfyeVLGLVTLEDVIEEIIK 452
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMrEHGISRLPVV---DEDGK------LVGIVTLKDLLRALLG 57
 
Name Accession Description Interval E-value
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 319-448 2.38e-37

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: 135.32  E-value: 2.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 319 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAIVEPEDCTPlsTITRFYNHPLHF 398
Cdd:cd04590   1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 88196782 399 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 448
Cdd:cd04590  78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 237-461 1.71e-27

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 115.99  E-value: 1.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 237 LVFLVGEVLP----AAVSGRWALALAPRALGLSRLAvlltlpvaLPVGQLLELAAR---------PGRLRERV------- 296
Cdd:COG1253 115 LSLVFGELVPkrlaLQNPERVALLVAPPLRLFSRLF--------RPLVWLLNGSTNlllrllgiePAEEEPAVteeelra 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 297 -LELARGGG--DPY-SDLSKGVLR--SRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVYEEERSNIVDMLY 370
Cdd:COG1253 187 lVEESEESGviEEEeREMIENVFEfgDRTVREVMTPRTDVVALDLDDTLE-EALELILESGHSRIPVYEGDLDDIVGVVH 265

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 371 LKDL--AIVEPEDcTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVnnegegDPFYEVLGLVTLEDVIE 448
Cdd:COG1253 266 VKDLlrALLEGEP-FDLRDLLR----PPLFVPETKPLDDLLEEFRRERVHMAIV--V------DEYGGTAGLVTLEDILE 332

                       250
                ....*....|...
gi 88196782 449 EIIkSEILDESED 461
Cdd:COG1253 333 EIV-GEIRDEYDE 344
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 237-469 4.40e-22

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: 99.38  E-value: 4.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 237 LVFlvGEVLP----AAVSGRWALALAP--RAL---------GLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELAR 301
Cdd:COG4536 106 LIF--AEVTPktlaALYPEKIALPVSPplRPLlkllyplvwLVNLIVRGLLRLFGVKPDADASDLLSEEELRTVVDLGEA 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 302 GGGDP--YSDLSKGV--LRSRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVYEEERSNIVDMLYLKDL--A 375
Cdd:COG4536 184 GGVIPkeHRDMLLNIldLEDVTVEDIMVPRNEIEGIDLDDPWE-EILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLlrA 262

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 376 IVEPE-DCTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIEEIIkSE 454
Cdd:COG4536 263 LRKGDlSKEDLRKIAR----EPYFIPETTPLSTQLQNFQKRKRRFALV--VDEYG------DVQGLVTLEDILEEIV-GE 329

                       250
                ....*....|....*
gi 88196782 455 ILDESeDYSDTKVRK 469
Cdd:COG4536 330 ITDEH-DPDAEEIRP 343
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
293-493 6.41e-14

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 72.92  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  293 RERVLELARGGG-----DPYS-DLSKGVL--RSRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVYEEERSN 364
Cdd:PRK15094  34 RDELLALIRDSEqndliDEDTrDMLEGVMdiADQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  365 IVDMLYLKDLAIVEPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 442
Cdd:PRK15094 113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 88196782  443 LEDVIEEIIkSEILDESEDYSDTKVRK-----KTVALGAPLKRKEEFSLFKVSDDE 493
Cdd:PRK15094 181 IEDILELIV-GEIEDEYDEEDDIDFRQlsrhtWTVRALASIEDFNEAFGTHFSDEE 235
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
235-450 1.07e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 49.88  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 235 AGLVFLVGEVLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSKGV 314
Cdd:COG2524   3 VLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 315 LRSRTVEDVLTPleDCFMLDSGTVLDfSVLASIMQSGHTRIPVYEEERsnIVDMLYLKDLAIVEPEDCTPLS-TITRFYN 393
Cdd:COG2524  83 VLKMKVKDIMTK--DVITVSPDTTLE-EALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDaPVSDIMT 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 88196782 394 HPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGEgdpfyeVLGLVTLEDVIEEI 450
Cdd:COG2524 158 RDVVTVSEDDSLEEALRLMLEHGIGRLPV--VDDDGK------LVGIITRTDILRAL 206
COG3903 COG3903
Predicted ATPase [General function prediction only];
11-304 5.51e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  11 WLGWVLA-------AFCLGSTAGEAAPAPGAGLLNFCTEEDSAPGAGSLRGRAAPEATLCLRLFCSGLANSSWTWVAAEG 83
Cdd:COG3903 567 WLERALAaageaaaALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAA 646

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782  84 AGCPEGGRATEPEEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAPPWALGLGAAGLLALAAVARGLQLS 163
Cdd:COG3903 647 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAA 726

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 164 ALALAPAEVQVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAAGQRAVPAVLGCAGLVFLVGE 243
Cdd:COG3903 727 LLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAA 806

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196782 244 VLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGG 304
Cdd:COG3903 807 AAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAA 867
CBS COG0517
CBS domain [Signal transduction mechanisms];
319-452 2.02e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 38.69  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 319 TVEDVLTPleDCFMLDSG-TVLDfsVLASIMQSGHTRIPVYEEERsNIVDMLYLKDL--AIVEPEDCTPLSTITRFYNHP 395
Cdd:COG0517   2 KVKDIMTT--DVVTVSPDaTVRE--ALELMSEKRIGGLPVVDEDG-KLVGIVTDRDLrrALAAEGKDLLDTPVSEVMTRP 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 88196782 396 LHFVFNDTKLDAVLEEFKRGK-SHLAIVqkvnnEGEGdpfyEVLGLVTLEDVIEEIIK 452
Cdd:COG0517  77 PVTVSPDTSLEEAAELMEEHKiRRLPVV-----DDDG----RLVGIITIKDLLKALLE 125
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
319-448 6.62e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.58  E-value: 6.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 319 TVEDVLTpLEDC-FMLDSGTVLDFsvLASIMQSGHTRIPVYEEERsNIVDMLYLKDLAIVEPEDctplsTITRFYNHPLH 397
Cdd:COG4109  17 LVEDIMT-LEDVaTLSEDDTVEDA--LELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDDT-----PIEDVMTKNPI 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 88196782 398 FVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIE 448
Cdd:COG4109  88 TVTPDTSLASAAHKMIWEGIELLPV--VDDDG------RLLGIISRQDVLK 130
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 388-452 8.60e-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: 35.27  E-value: 8.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196782   388 ITRFYNHPLHFVFNDTKLDAVLEEF-KRGKSHLAIVqkvNNEGEgdpfyeVLGLVTLEDVIEEIIK 452
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMrEHGISRLPVV---DEDGK------LVGIVTLKDLLRALLG 57
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 343-447 9.70e-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: 36.45  E-value: 9.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196782 343 VLASIMQSGHTRIPVYEEErSNIVDMLYLKDLAIVEPEDCTPLSTITRFY-NHPLHFVFNDTKLDAVLEEFKRGK-SHLA 420
Cdd:cd02205  16 ALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPVAEVmTPDVITVSPDTDLEEALELMLEHGiRRLP 94

                        90       100
                ....*....|....*....|....*..
gi 88196782 421 IVqkvNNEGEgdpfyeVLGLVTLEDVI 447
Cdd:cd02205  95 VV---DDDGK------LVGIVTRRDIL 112
 
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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