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Conserved domains on  [gi|1958801492|ref|XP_038939147|]
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metal transporter CNNM3 isoform X4 [Rattus norvegicus]

Protein Classification

CBS domain-containing protein( domain architecture ID 10140050)

CBS (cystathione beta synthase) domain-containing protein; the CBS domains may act as regulatory units

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 ...
 317-446 4.66e-39

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: 138.40  E-value: 4.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 317 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVFEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 396
Cdd:cd04590     1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801492 397 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 446
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
COG3903 super family cl43979
Predicted ATPase [General function prediction only];
11-299 1.36e-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: 45.01  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492  11 WLGWVLAAfcLGSTAGEAAPGAGLLSFCTEEDGAPGAGSLRGRAAPEATLCLRLFCPGLANSSWTWVAPEGAGCPEGGRA 90
Cdd:COG3903   567 WLERALAA--AGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAA 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492  91 TEPSEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAAPWALGLGAAGLLALAAVARGLQLSALALAPAEV 170
Cdd:COG3903   645 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAA 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 171 QVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAVGQRAVPAVLGCAGLVFLVGEVLPAAVSGR 250
Cdd:COG3903   725 AALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAA 804

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801492 251 WALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELAR 299
Cdd:COG3903   805 AAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAA 853
 
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 ...
 317-446 4.66e-39

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: 138.40  E-value: 4.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 317 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVFEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 396
Cdd:cd04590     1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801492 397 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 446
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 235-459 2.53e-26

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 111.36  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 235 LVFLVGEVLP----AAVSGRWALALAPRALGLSRLA------------VLLTLPVALPVGQ-----------LLELAARP 287
Cdd:COG1253   115 LSLVFGELVPkrlaLQNPERVALLVAPPLRLFSRLFrplvwllngstnLLLRLLGIEPAEEepavteeelraLVEESEES 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 288 GRLRE-------RVLELarggGDpysdlskgvlryRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEER 360
Cdd:COG1253   195 GVIEEeeremieNVFEF----GD------------RTVREVMTPRTDVVALDLDDTLE-EALELILESGHSRIPVYEGDL 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 361 SNIVDMLYLKDL--AFVDPEDcTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVnnegegDPFYEVLGL 438
Cdd:COG1253   258 DDIVGVVHVKDLlrALLEGEP-FDLRDLLR----PPLFVPETKPLDDLLEEFRRERVHMAIV--V------DEYGGTAGL 324

                         250       260
                  ....*....|....*....|.
gi 1958801492 439 VTLEDVIEEIIrSEILDESED 459
Cdd:COG1253   325 VTLEDILEEIV-GEIRDEYDE 344
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
291-467 4.05e-13

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 69.84  E-value: 4.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 291 RERVLELARGGG-----DPYS-DLSKGVLRY--RTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERSN 362
Cdd:PRK15094   34 RDELLALIRDSEqndliDEDTrDMLEGVMDIadQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 363 IVDMLYLKDLAFVDPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 440
Cdd:PRK15094  113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                         170       180
                  ....*....|....*....|....*..
gi 1958801492 441 LEDVIEEIIrSEILDESEDYSDTKVKK 467
Cdd:PRK15094  181 IEDILELIV-GEIEDEYDEEDDIDFRQ 206
COG3903 COG3903
Predicted ATPase [General function prediction only];
11-299 1.36e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 45.01  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492  11 WLGWVLAAfcLGSTAGEAAPGAGLLSFCTEEDGAPGAGSLRGRAAPEATLCLRLFCPGLANSSWTWVAPEGAGCPEGGRA 90
Cdd:COG3903   567 WLERALAA--AGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAA 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492  91 TEPSEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAAPWALGLGAAGLLALAAVARGLQLSALALAPAEV 170
Cdd:COG3903   645 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAA 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 171 QVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAVGQRAVPAVLGCAGLVFLVGEVLPAAVSGR 250
Cdd:COG3903   725 AALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAA 804

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801492 251 WALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELAR 299
Cdd:COG3903   805 AAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAA 853
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 386-450 7.05e-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: 34.88  E-value: 7.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801492 386 ITRFYNHPLHFVFNDTKLDAVLEEF-KRGKSHLAIVqkvNNEGEgdpfyeVLGLVTLEDVIEEIIR 450
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 ...
 317-446 4.66e-39

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: 138.40  E-value: 4.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 317 TVEDVLTPLEDCFMLDSgTVLDFSVLASIMQSGHTRIPVFEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 396
Cdd:cd04590     1 TVREVMTPRTDVVALDA-DATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801492 397 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 446
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 235-459 2.53e-26

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 111.36  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 235 LVFLVGEVLP----AAVSGRWALALAPRALGLSRLA------------VLLTLPVALPVGQ-----------LLELAARP 287
Cdd:COG1253   115 LSLVFGELVPkrlaLQNPERVALLVAPPLRLFSRLFrplvwllngstnLLLRLLGIEPAEEepavteeelraLVEESEES 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 288 GRLRE-------RVLELarggGDpysdlskgvlryRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEER 360
Cdd:COG1253   195 GVIEEeeremieNVFEF----GD------------RTVREVMTPRTDVVALDLDDTLE-EALELILESGHSRIPVYEGDL 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 361 SNIVDMLYLKDL--AFVDPEDcTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVnnegegDPFYEVLGL 438
Cdd:COG1253   258 DDIVGVVHVKDLlrALLEGEP-FDLRDLLR----PPLFVPETKPLDDLLEEFRRERVHMAIV--V------DEYGGTAGL 324

                         250       260
                  ....*....|....*....|.
gi 1958801492 439 VTLEDVIEEIIrSEILDESED 459
Cdd:COG1253   325 VTLEDILEEIV-GEIRDEYDE 344
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 235-456 1.21e-21

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: 97.45  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 235 LVFlvGEVLP----AAVSGRWALALAP--RAL---------GLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELAR 299
Cdd:COG4536   106 LIF--AEVTPktlaALYPEKIALPVSPplRPLlkllyplvwLVNLIVRGLLRLFGVKPDADASDLLSEEELRTVVDLGEA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 300 GGGDP--YSDLSKGV--LRYRTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERSNIVDMLYLKD-LAF 374
Cdd:COG4536   184 GGVIPkeHRDMLLNIldLEDVTVEDIMVPRNEIEGIDLDDPWE-EILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDlLRA 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 375 VDPEDCTP--LSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIEEIIrSE 452
Cdd:COG4536   263 LRKGDLSKedLRKIAR----EPYFIPETTPLSTQLQNFQKRKRRFALV--VDEYG------DVQGLVTLEDILEEIV-GE 329


                  ....
gi 1958801492 453 ILDE 456
Cdd:COG4536   330 ITDE 333
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
291-467 4.05e-13

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 69.84  E-value: 4.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 291 RERVLELARGGG-----DPYS-DLSKGVLRY--RTVEDVLTPLEDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERSN 362
Cdd:PRK15094   34 RDELLALIRDSEqndliDEDTrDMLEGVMDIadQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 363 IVDMLYLKDLAFVDPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 440
Cdd:PRK15094  113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                         170       180
                  ....*....|....*....|....*..
gi 1958801492 441 LEDVIEEIIrSEILDESEDYSDTKVKK 467
Cdd:PRK15094  181 IEDILELIV-GEIEDEYDEEDDIDFRQ 206
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
233-448 1.48e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 52.19  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 233 AGLVFLVGEVLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSKGV 312
Cdd:COG2524     3 VLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 313 LRYRTVEDVLTPleDCFMLDSGTVLDfSVLASIMQSGHTRIPVFEEERsnIVDMLYLKDLAFVDPEDCTPLS-TITRFYN 391
Cdd:COG2524    83 VLKMKVKDIMTK--DVITVSPDTTLE-EALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDaPVSDIMT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801492 392 HPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGEgdpfyeVLGLVTLEDVIEEI 448
Cdd:COG2524   158 RDVVTVSEDDSLEEALRLMLEHGIGRLPV--VDDDGK------LVGIITRTDILRAL 206
COG3903 COG3903
Predicted ATPase [General function prediction only];
11-299 1.36e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 45.01  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492  11 WLGWVLAAfcLGSTAGEAAPGAGLLSFCTEEDGAPGAGSLRGRAAPEATLCLRLFCPGLANSSWTWVAPEGAGCPEGGRA 90
Cdd:COG3903   567 WLERALAA--AGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAA 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492  91 TEPSEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAAPWALGLGAAGLLALAAVARGLQLSALALAPAEV 170
Cdd:COG3903   645 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAA 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 171 QVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAVGQRAVPAVLGCAGLVFLVGEVLPAAVSGR 250
Cdd:COG3903   725 AALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAA 804

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801492 251 WALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELAR 299
Cdd:COG3903   805 AAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAA 853
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
317-446 2.17e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.44  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 317 TVEDVLTpLEDC-FMLDSGTVLDFsvLASIMQSGHTRIPVFEEERsNIVDMLYLKDLAFVDPEDctplsTITRFYNHPLH 395
Cdd:COG4109    17 LVEDIMT-LEDVaTLSEDDTVEDA--LELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDDT-----PIEDVMTKNPI 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801492 396 FVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIE 446
Cdd:COG4109    88 TVTPDTSLASAAHKMIWEGIELLPV--VDDDG------RLLGIISRQDVLK 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 341-445 2.48e-04

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: 40.69  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 341 VLASIMQSGHTRIPVFEEErSNIVDMLYLKDLAFVDPEDCTPLSTITRFY-NHPLHFVFNDTKLDAVLEEFKRGK-SHLA 418
Cdd:cd02205    16 ALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPVAEVmTPDVITVSPDTDLEEALELMLEHGiRRLP 94

                          90       100
                  ....*....|....*....|....*..
gi 1958801492 419 IVqkvNNEGEgdpfyeVLGLVTLEDVI 445
Cdd:cd02205    95 VV---DDDGK------LVGIVTRRDIL 112
CBS COG0517
CBS domain [Signal transduction mechanisms];
317-450 2.66e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 41.00  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801492 317 TVEDVLTPleDCFMLDSG-TVLDfsVLASIMQSGHTRIPVFEEERsNIVDMLYLKDLAF-VDPEDCTPLST-ITRFYNHP 393
Cdd:COG0517     2 KVKDIMTT--DVVTVSPDaTVRE--ALELMSEKRIGGLPVVDEDG-KLVGIVTDRDLRRaLAAEGKDLLDTpVSEVMTRP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801492 394 LHFVFNDTKLDAVLEEFKRGK-SHLAIVqkvnnEGEGdpfyEVLGLVTLEDVIEEIIR 450
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKiRRLPVV-----DDDG----RLVGIITIKDLLKALLE 125
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 386-450 7.05e-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: 34.88  E-value: 7.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801492 386 ITRFYNHPLHFVFNDTKLDAVLEEF-KRGKSHLAIVqkvNNEGEgdpfyeVLGLVTLEDVIEEIIR 450
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMrEHGISRLPVV---DEDGK------LVGIVTLKDLLRALLG 57
 
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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