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Conserved domains on  [gi|492232616|ref|WP_005783033|]
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MULTISPECIES: TerC family protein [Pseudomonas syringae group]

Protein Classification

TerC family protein( domain architecture ID 11436733)

TerC family inner membrane protein similar to Escherichia coli YoaE and YegH, which contain a TerC domain, tandem repeats of the cystathionine beta-synthase (CBS pair) domain, and a transporter-associated domain

Gene Ontology:  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 ...
 248-522 7.03e-72

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 235.40  E-value: 7.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 248 RAAHAVMRLLGGRKLESGDV--DEEITDMLEGESSEPVFDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKI 325
Cdd:COG1253  159 GSTNLLLRLLGIEPAEEEPAvtEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEA 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 326 RLKLMHSSYSRLPLIGErGIDEPLGFVHKKELFKELLSGNEPDLKLMSRKAINLLESFTILNALEQMRKESTHIAFVVNE 405
Cdd:COG1253  239 LELILESGHSRIPVYEG-DLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 406 FGDFIGVLSMTDILESIAGQLPDASEVEGPDIVKQGED-FVVSGALNLSLIRERTGFQAKATEDYQTLAGLVMSLLDRLP 484
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGsYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIP 397

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 492232616 485 STGDSLDWQGWNLQVVGVEERRVTRVLLQKQPEVDAGK 522
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
TerC COG0861
Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism];
1-240 2.16e-69

Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism];


:

Pssm-ID: 440622  Cd Length: 225  Bit Score: 221.85  E-value: 2.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   1 MEWIAD-PTAWLGLLTLIVLELVLGIDNLVFIAILADKLPPEQRDKARVIGLSLALIMRLGLLASISWMVTLteplfeif 79
Cdd:COG0861    1 MDLLLFgPEAWLALLTLYLLEIVLSIDNAFVIALIFRKLPPEQQKKALFWGILGALVLRIILIFLGAWLLSF-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616  80 dktfsgrDLIMLFGGVFLLFKATMELHERLEGHVAQRAGNAGYALFWPIVAQIVVLDAVFSLDAVITAVGMVEHLSVMMI 159
Cdd:COG0861   73 -------PWILYLGGLFLLWTAIKLLHEKEEEDEENENGKRAATPLWLAVVQIELADLVFSLDSVPAAFGITQDPFLVFT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 160 AVIFSIGLMMIASKPLTKFVNSRPTVIMLCLGFLMMIGFSLTAEGLGFHIPKGYLYAAIGFSILIevFNQIARKRSKKSA 239
Cdd:COG0861  146 GNIFAILGLRFLAFLLAGLLDRFPYLKYLAAAILGFIGVKLILEDLHFHIPKGYISLAVIFSVLA--LGILASLLKRRKA 223


                 .
gi 492232616 240 H 240
Cdd:COG0861  224 K 224
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 248-522 7.03e-72

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 235.40  E-value: 7.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 248 RAAHAVMRLLGGRKLESGDV--DEEITDMLEGESSEPVFDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKI 325
Cdd:COG1253  159 GSTNLLLRLLGIEPAEEEPAvtEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEA 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 326 RLKLMHSSYSRLPLIGErGIDEPLGFVHKKELFKELLSGNEPDLKLMSRKAINLLESFTILNALEQMRKESTHIAFVVNE 405
Cdd:COG1253  239 LELILESGHSRIPVYEG-DLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 406 FGDFIGVLSMTDILESIAGQLPDASEVEGPDIVKQGED-FVVSGALNLSLIRERTGFQAKATEDYQTLAGLVMSLLDRLP 484
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGsYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIP 397

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 492232616 485 STGDSLDWQGWNLQVVGVEERRVTRVLLQKQPEVDAGK 522
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
TerC COG0861
Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism];
1-240 2.16e-69

Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism];


Pssm-ID: 440622  Cd Length: 225  Bit Score: 221.85  E-value: 2.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   1 MEWIAD-PTAWLGLLTLIVLELVLGIDNLVFIAILADKLPPEQRDKARVIGLSLALIMRLGLLASISWMVTLteplfeif 79
Cdd:COG0861    1 MDLLLFgPEAWLALLTLYLLEIVLSIDNAFVIALIFRKLPPEQQKKALFWGILGALVLRIILIFLGAWLLSF-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616  80 dktfsgrDLIMLFGGVFLLFKATMELHERLEGHVAQRAGNAGYALFWPIVAQIVVLDAVFSLDAVITAVGMVEHLSVMMI 159
Cdd:COG0861   73 -------PWILYLGGLFLLWTAIKLLHEKEEEDEENENGKRAATPLWLAVVQIELADLVFSLDSVPAAFGITQDPFLVFT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 160 AVIFSIGLMMIASKPLTKFVNSRPTVIMLCLGFLMMIGFSLTAEGLGFHIPKGYLYAAIGFSILIevFNQIARKRSKKSA 239
Cdd:COG0861  146 GNIFAILGLRFLAFLLAGLLDRFPYLKYLAAAILGFIGVKLILEDLHFHIPKGYISLAVIFSVLA--LGILASLLKRRKA 223


                 .
gi 492232616 240 H 240
Cdd:COG0861  224 K 224
TerC pfam03741
Integral membrane protein TerC family; This family contains a number of integral membrane ...
 14-204 1.35e-45

Integral membrane protein TerC family; This family contains a number of integral membrane proteins that also contains the TerC protein. TerC has been implicated in resistance to tellurium. This protein may be involved in efflux of tellurium ions. The tellurite-resistant Escherichia coli strain KL53 was found during testing of the group of clinical isolates for antibiotics and heavy metal ion resistance. Determinant of the tellurite resistance of the strain was located on a large conjugative plasmid. Analyses showed, the genes terB, terC, terD and terE are essential for conservation of the resistance. The members of the family contain a number of conserved aspartates that could be involved in binding to metal ions.


Pssm-ID: 461035  Cd Length: 178  Bit Score: 157.63  E-value: 1.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   14 LTLIVLELVLGIDNLVFIAILADKLPPEQRDKARVIGLSLALIMRLGLLASISWmvtltepLFEIFDktfsgrdLIMLFG 93
Cdd:pfam03741   1 FTLVLIEIVLSVDNAFVIALIFRKLPPEQQRKALFWGIGGALVLRILLIFLGVA-------LLELFD-------WLLLIG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   94 GVFLLFKATMELHE-RLEGHVAQRAGNAGYALFWPIVAQIVVLDAVFSLDAVITAVGMVEHLSVMMIAVIFSIGLMMIAS 172
Cdd:pfam03741  67 GLFLLYTAIKLLRDlRKLVREEDKKLPVTSSSLWLAVIQIELADLVFSLDSVPAAVGITDDPFIVITGNVFSILGLRFLS 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 492232616  173 KPLTKFVNSRPTVIMLCLGFLMMIGFSLTAEG 204
Cdd:pfam03741 147 FLLAKLIERFPYLKYLAAAILGFIGVKLLLEG 178
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 302-420 1.39e-32

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: 120.68  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 302 PIRTVMTPRAEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGErGIDEPLGFVHKKELFKELLSGNEP-DLKLMSRKAINLL 380
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEG-DLDNIIGVLHVKDLLAALLEGREKlDLRALLRPPLFVP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492232616 381 ESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILE 420
Cdd:cd04590   80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
263-510 2.38e-21

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 94.10  E-value: 2.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 263 ESGDVDEEITDMLEGESSEpVFDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGE 342
Cdd:PRK15094  30 EPKNRDELLALIRDSEQND-LIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 343 RGiDEPLGFVHKKELFKELLSGNEP-DLKLMSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILES 421
Cdd:PRK15094 109 DK-DHIEGILMAKDLLPFMRSDAEAfSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILEL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 422 IAGQLPDA-SEVEGPDI------------VKQGEDFVVSGALNLSlirertgfqakaTEDYQTLAGLVMSLLDRLPSTGD 488
Cdd:PRK15094 188 IVGEIEDEyDEEDDIDFrqlsrhtwtvraLASIEDFNEAFGTHFS------------DEEVDTIGGLVMQAFGHLPARGE 255

                        250       260
                 ....*....|....*....|..
gi 492232616 489 SLDWQGWNLQVVGVEERRVTRV 510
Cdd:PRK15094 256 TIDIDGYQFKVAMADSRRIIQV 277
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 438-514 3.85e-15

Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.


Pssm-ID: 215020 [Multi-domain]  Cd Length: 78  Bit Score: 70.16  E-value: 3.85e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492232616   438 VKQGE-DFVVSGALNLSLIRERTGFQAKaTEDYQTLAGLVMSLLDRLPSTGDSLDWQGWNLQVVGVEERRVTRVLLQK 514
Cdd:smart01091   1 VKLDDgSYLVDGRTPIDDLNELLGLDLP-EEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 438-516 2.50e-12

Transporter associated domain; This small domain is found in a family of proteins with the pfam01595 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.


Pssm-ID: 460935 [Multi-domain]  Cd Length: 81  Bit Score: 62.56  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616  438 VKQGED-FVVSGALNLSLIRERTGFQAKaTEDYQTLAGLVMSLLDRLPSTGDSL--DWQGWNLQVVGVEERRVTRVLLQK 514
Cdd:pfam03471   1 EKLDDGsYLVDGRAPLDDLNELLGLELP-EEDYDTLGGLVLERLGRIPKVGDKVevELGGLRFTVLEMDGRRIKKVRITK 79


                  ..
gi 492232616  515 QP 516
Cdd:pfam03471  80 LE 81
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 248-522 7.03e-72

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 235.40  E-value: 7.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 248 RAAHAVMRLLGGRKLESGDV--DEEITDMLEGESSEPVFDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKI 325
Cdd:COG1253  159 GSTNLLLRLLGIEPAEEEPAvtEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEA 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 326 RLKLMHSSYSRLPLIGErGIDEPLGFVHKKELFKELLSGNEPDLKLMSRKAINLLESFTILNALEQMRKESTHIAFVVNE 405
Cdd:COG1253  239 LELILESGHSRIPVYEG-DLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 406 FGDFIGVLSMTDILESIAGQLPDASEVEGPDIVKQGED-FVVSGALNLSLIRERTGFQAKATEDYQTLAGLVMSLLDRLP 484
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGsYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIP 397

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 492232616 485 STGDSLDWQGWNLQVVGVEERRVTRVLLQKQPEVDAGK 522
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
TerC COG0861
Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism];
1-240 2.16e-69

Tellurite resistance membrane protein TerC [Inorganic ion transport and metabolism];


Pssm-ID: 440622  Cd Length: 225  Bit Score: 221.85  E-value: 2.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   1 MEWIAD-PTAWLGLLTLIVLELVLGIDNLVFIAILADKLPPEQRDKARVIGLSLALIMRLGLLASISWMVTLteplfeif 79
Cdd:COG0861    1 MDLLLFgPEAWLALLTLYLLEIVLSIDNAFVIALIFRKLPPEQQKKALFWGILGALVLRIILIFLGAWLLSF-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616  80 dktfsgrDLIMLFGGVFLLFKATMELHERLEGHVAQRAGNAGYALFWPIVAQIVVLDAVFSLDAVITAVGMVEHLSVMMI 159
Cdd:COG0861   73 -------PWILYLGGLFLLWTAIKLLHEKEEEDEENENGKRAATPLWLAVVQIELADLVFSLDSVPAAFGITQDPFLVFT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 160 AVIFSIGLMMIASKPLTKFVNSRPTVIMLCLGFLMMIGFSLTAEGLGFHIPKGYLYAAIGFSILIevFNQIARKRSKKSA 239
Cdd:COG0861  146 GNIFAILGLRFLAFLLAGLLDRFPYLKYLAAAILGFIGVKLILEDLHFHIPKGYISLAVIFSVLA--LGILASLLKRRKA 223


                 .
gi 492232616 240 H 240
Cdd:COG0861  224 K 224
TerC pfam03741
Integral membrane protein TerC family; This family contains a number of integral membrane ...
 14-204 1.35e-45

Integral membrane protein TerC family; This family contains a number of integral membrane proteins that also contains the TerC protein. TerC has been implicated in resistance to tellurium. This protein may be involved in efflux of tellurium ions. The tellurite-resistant Escherichia coli strain KL53 was found during testing of the group of clinical isolates for antibiotics and heavy metal ion resistance. Determinant of the tellurite resistance of the strain was located on a large conjugative plasmid. Analyses showed, the genes terB, terC, terD and terE are essential for conservation of the resistance. The members of the family contain a number of conserved aspartates that could be involved in binding to metal ions.


Pssm-ID: 461035  Cd Length: 178  Bit Score: 157.63  E-value: 1.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   14 LTLIVLELVLGIDNLVFIAILADKLPPEQRDKARVIGLSLALIMRLGLLASISWmvtltepLFEIFDktfsgrdLIMLFG 93
Cdd:pfam03741   1 FTLVLIEIVLSVDNAFVIALIFRKLPPEQQRKALFWGIGGALVLRILLIFLGVA-------LLELFD-------WLLLIG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   94 GVFLLFKATMELHE-RLEGHVAQRAGNAGYALFWPIVAQIVVLDAVFSLDAVITAVGMVEHLSVMMIAVIFSIGLMMIAS 172
Cdd:pfam03741  67 GLFLLYTAIKLLRDlRKLVREEDKKLPVTSSSLWLAVIQIELADLVFSLDSVPAAVGITDDPFIVITGNVFSILGLRFLS 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 492232616  173 KPLTKFVNSRPTVIMLCLGFLMMIGFSLTAEG 204
Cdd:pfam03741 147 FLLAKLIERFPYLKYLAAAILGFIGVKLLLEG 178
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 250-516 5.73e-42

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: 155.23  E-value: 5.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 250 AHAVMRLLGGRKLESGDV---DEEITDMLEGESSEPVFDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKIR 326
Cdd:COG4536  150 VRGLLRLFGVKPDADASDllsEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEIL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 327 LKLMHSSYSRLPLIgERGIDEPLGFVHKKELFKELLSGNEPDLKLMS--RKAINLLESFTILNALEQMRKESTHIAFVVN 404
Cdd:COG4536  230 KQLLTSPHTRLPVY-RGDIDNIVGVLHVRDLLRALRKGDLSKEDLRKiaREPYFIPETTPLSTQLQNFQKRKRRFALVVD 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 405 EFGDFIGVLSMTDILESIAGQLPDASEVEGPDIVKQGED-FVVSGALNLSLIRERTGFQAKaTEDYQTLAGLVMSLLDRL 483
Cdd:COG4536  309 EYGDVQGLVTLEDILEEIVGEITDEHDPDAEEIRPQEDGsYLVDGSATIRDLNRALDWNLP-DDGAKTLNGLIIEELEDI 387

                        250       260       270
                 ....*....|....*....|....*....|...
gi 492232616 484 PSTGDSLDWQGWNLQVVGVEERRVTRVLLQKQP 516
Cdd:COG4536  388 PEAGQSFTIHGYRFEILQVQDNRIKTVRIRPLP 420
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 302-420 1.39e-32

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: 120.68  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 302 PIRTVMTPRAEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGErGIDEPLGFVHKKELFKELLSGNEP-DLKLMSRKAINLL 380
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEG-DLDNIIGVLHVKDLLAALLEGREKlDLRALLRPPLFVP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492232616 381 ESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILE 420
Cdd:cd04590   80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
263-510 2.38e-21

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 94.10  E-value: 2.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 263 ESGDVDEEITDMLEGESSEpVFDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGE 342
Cdd:PRK15094  30 EPKNRDELLALIRDSEQND-LIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 343 RGiDEPLGFVHKKELFKELLSGNEP-DLKLMSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILES 421
Cdd:PRK15094 109 DK-DHIEGILMAKDLLPFMRSDAEAfSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILEL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 422 IAGQLPDA-SEVEGPDI------------VKQGEDFVVSGALNLSlirertgfqakaTEDYQTLAGLVMSLLDRLPSTGD 488
Cdd:PRK15094 188 IVGEIEDEyDEEDDIDFrqlsrhtwtvraLASIEDFNEAFGTHFS------------DEEVDTIGGLVMQAFGHLPARGE 255

                        250       260
                 ....*....|....*....|..
gi 492232616 489 SLDWQGWNLQVVGVEERRVTRV 510
Cdd:PRK15094 256 TIDIDGYQFKVAMADSRRIIQV 277
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 438-514 3.85e-15

Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.


Pssm-ID: 215020 [Multi-domain]  Cd Length: 78  Bit Score: 70.16  E-value: 3.85e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492232616   438 VKQGE-DFVVSGALNLSLIRERTGFQAKaTEDYQTLAGLVMSLLDRLPSTGDSLDWQGWNLQVVGVEERRVTRVLLQK 514
Cdd:smart01091   1 VKLDDgSYLVDGRTPIDDLNELLGLDLP-EEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 438-516 2.50e-12

Transporter associated domain; This small domain is found in a family of proteins with the pfam01595 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.


Pssm-ID: 460935 [Multi-domain]  Cd Length: 81  Bit Score: 62.56  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616  438 VKQGED-FVVSGALNLSLIRERTGFQAKaTEDYQTLAGLVMSLLDRLPSTGDSL--DWQGWNLQVVGVEERRVTRVLLQK 514
Cdd:pfam03471   1 EKLDDGsYLVDGRAPLDDLNELLGLELP-EEDYDTLGGLVLERLGRIPKVGDKVevELGGLRFTVLEMDGRRIKKVRITK 79


                  ..
gi 492232616  515 QP 516
Cdd:pfam03471  80 LE 81
PRK11573 PRK11573
hypothetical protein; Provisional
 251-510 1.64e-11

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 65.93  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 251 HAVMRLLGGRK--LESGDVDEEITDMLEGESSEPVfDRRERVMISGVLQLAERPIRTVMTPRAEIDYIDLKDDAEKIRLK 328
Cdd:PRK11573 136 RLLMRLMGIKTdiVVSGALSKEELRTIVHESRSQI-SRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQ 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 329 LMHSSYSRLPLIGErGIDEPLGFVHKKELFKELLSGNEPDLKLMSRKA--INLLESFTILNA-LEQMRKESTHIAFVVNE 405
Cdd:PRK11573 215 LTHSPHGRIVLYRD-SLDDAISMLRVREAYRLMTEKKEFTKENMLRAAdeIYFVPEGTPLSTqLVKFQRNKKKVGLVVDE 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 406 FGDFIGVLSMTDILESIAGQLPDA-SEVEGPDIVKQGEDFV-VSGALNLSLIRERTGFQAKAtEDYQTLAGLVMSLLDRL 483
Cdd:PRK11573 294 YGDIQGLVTVEDILEEIVGDFTTSmSPTLAEEVTPQNDGSViIDGTANVREINKAFNWHLPE-DDARTVNGVILEALEEI 372

                        250       260
                 ....*....|....*....|....*..
gi 492232616 484 PSTGDSLDWQGWNLQVVGVEERRVTRV 510
Cdd:PRK11573 373 PVAGTRVRIGEYDIDILDVQDNMIKQV 399
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
303-429 8.01e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 54.10  E-value: 8.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 303 IRTVMTPraEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGERGidEPLGFVHKKELFKELLSGNEPDLK----------LM 372
Cdd:COG3448    4 VRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDG--RLVGIVTERDLLRALLPDRLDELEerlldlpvedVM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492232616 373 SRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESIAGQLPDA 429
Cdd:COG3448   80 TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
302-421 8.81e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 48.37  E-value: 8.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 302 PIRTVMTpRAEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGERGidEPLGFVHKKELFkellsGNEPDL---KLMSRKAIN 378
Cdd:COG4109   17 LVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG--RLVGIVTSKDIL-----GKDDDTpieDVMTKNPIT 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492232616 379 LLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILES 421
Cdd:COG4109   89 VTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKA 131
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 327-419 1.08e-06

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: 47.24  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 327 LKLMHSS-YSRLPLIGERGidEPLGFVHKKELFKELLSGNEPDLK----LMSRKAINLLESFTILNALEQMRKESTHIAF 401
Cdd:cd02205   17 LELMAENgIGALPVVDDDG--KLVGIVTERDILRALVEGGLALDTpvaeVMTPDVITVSPDTDLEEALELMLEHGIRRLP 94

                         90
                 ....*....|....*...
gi 492232616 402 VVNEFGDFIGVLSMTDIL 419
Cdd:cd02205   95 VVDDDGKLVGIVTRRDIL 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 371-424 1.97e-06

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: 44.90  E-value: 1.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 492232616  371 LMSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESIAG 424
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
275-422 1.15e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.42  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 275 LEGESSEPVFDRRERVMISGVLQLAERPIRTVMTPRAEIdyIDLKDDAEKIRLKLMHSSYSRLPLIGErgiDEPLGFVHK 354
Cdd:COG2524   60 LLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVIT--VSPDTTLEEALELMLEKGISGLPVVDD---GKLVGIITE 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492232616 355 KELFKELLSGNEPD----LKLMSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESI 422
Cdd:COG2524  135 RDLLKALAEGRDLLdapvSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
303-426 5.39e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 42.93  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 303 IRTVMTPraEIDYIDLKDDAEKIRLKLMHSSYSRLPLIGERGidEPLGFVHKKELFKELLSGNEPDLK-----LMSRKAI 377
Cdd:COG0517    3 VKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPVVDEDG--KLVGIVTDRDLRRALAAEGKDLLDtpvseVMTRPPV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 492232616 378 NLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESIAGQL 426
Cdd:COG0517   79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPL 127
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 371-419 1.25e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 38.85  E-value: 1.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492232616 371 LMSRKAINLLESFTILNALEQMRK-----ESTHIAFVVNEFGDFIGVLSMTDIL 419
Cdd:cd04606    6 LMTTEFVAVRPDWTVEEALEYLRRlapdpETIYYIYVVDEDRRLLGVVSLRDLL 59
CitMHS pfam03600
Citrate transporter;
51-201 1.81e-03

Citrate transporter;


Pssm-ID: 460985 [Multi-domain]  Cd Length: 342  Bit Score: 40.76  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616   51 LSLALIMRLGLLASISWMVTLTEPLFEIFDKtfsgrDLIMLFGGVFLLFKATME--LHERLEGHVAQRAGNAGYALFWPI 128
Cdd:pfam03600   9 LPRDVVALLGAVLLVLLGVLTPEEALSGIDS-----PTILLLLGMMIIGAILERtgLFDRLALKLLRLAGGKPRRLLVAL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492232616  129 VAQIVVLDAVFSLDAVItavgmvehlsVMMIAVIFSIGLMMiaskpltkfvNSRPTVIMLCLGFLMMIGFSLT 201
Cdd:pfam03600  84 MLATALLSAFLSNDGTV----------LIMIPIVLALARRL----------GLPPSPLLIALAFAANIGGTAT 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 373-425 1.96e-03

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 37.99  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492232616 373 SRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESIAGQ 425
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG 53
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 344-422 2.12e-03

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 37.91  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 344 GIDEPLGFVHKKELFKELLSGNEP--DLK---LMSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDI 418
Cdd:cd17775   34 EDGKPVGIVTDRDIVVEVVAKGLDpkDVTvgdIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113


                 ....
gi 492232616 419 LESI 422
Cdd:cd17775  114 LELL 117
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 371-432 2.40e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.89  E-value: 2.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492232616 371 LMSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESIAGQLPDASEV 432
Cdd:COG2905    4 IMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDT 65
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 372-433 6.78e-03

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 36.73  E-value: 6.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492232616 372 MSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESIAGQLPDASEVE 433
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVE 62
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 346-426 8.28e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 36.35  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492232616 346 DEPLGFVHKKELFKELLSGNEPDLK-----LMSRKAINLLESFTILNALEQMRKESTHIAFVVNEfGDFIGVLSMTDILE 420
Cdd:COG2905   40 GRLVGIITDRDLRRRVLAEGLDPLDtpvseVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLR 118


                 ....*.
gi 492232616 421 SIAGQL 426
Cdd:COG2905  119 ALSEEL 124
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
371-419 8.32e-03

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 38.51  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492232616 371 LMSRKAINLLESFTILNALEQMRK-----ESTHIAFVVNEFGDFIGVLSMTDIL 419
Cdd:COG2239  134 LMTTEFVAVREDWTVGEALRYLRRqaedpETIYYIYVVDDDGRLVGVVSLRDLL 187
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 372-422 9.15e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. 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: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 36.58  E-value: 9.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492232616 372 MSRKAINLLESFTILNALEQMRKESTHIAFVVNEFGDFIGVLSMTDILESI 422
Cdd:cd04592    1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFL 51
 
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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