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Conserved domains on  [gi|1265182459|gb|PGR07495|]
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HlyC/CorC family transporter [Priestia megaterium]

Protein Classification

hemolysin family protein( domain architecture ID 11441338)

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

Gene Ontology:  GO:0016020|GO:0005886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 16-428 2.04e-159

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 456.89  E-value: 2.04e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  16 TAFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLGITITALGLGWLGEPTLDRLLHPLFTTFHTN 95
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  96 EPLAGILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIFGITmISEN 175
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIE-PAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 176 EAAHSEEELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRYPIVeD 255
Cdd:COG1253   176 EPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVY-E 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 256 GDKDKVIGLVNIKEIYNDIVfneKDGTNTLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDII 335
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRALL---EGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDIL 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 336 EEIVGEIRDEFDTDEiPYVQKIKDDHYILDGKMLISQVNDLLGTDI-SDEEVDTIAGWVLTEKFDV-TKNDIIQHEQFYF 413
Cdd:COG1253   332 EEIVGEIRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIpEVGETVEVDGLRF 410

                         410
                  ....*....|....*
gi 1265182459 414 KVLIIEDFHIKYIEV 428
Cdd:COG1253   411 EVLDMDGRRIDKVLV 425
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 16-428 2.04e-159

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 456.89  E-value: 2.04e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  16 TAFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLGITITALGLGWLGEPTLDRLLHPLFTTFHTN 95
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  96 EPLAGILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIFGITmISEN 175
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIE-PAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 176 EAAHSEEELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRYPIVeD 255
Cdd:COG1253   176 EPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVY-E 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 256 GDKDKVIGLVNIKEIYNDIVfneKDGTNTLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDII 335
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRALL---EGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDIL 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 336 EEIVGEIRDEFDTDEiPYVQKIKDDHYILDGKMLISQVNDLLGTDI-SDEEVDTIAGWVLTEKFDV-TKNDIIQHEQFYF 413
Cdd:COG1253   332 EEIVGEIRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIpEVGETVEVDGLRF 410

                         410
                  ....*....|....*
gi 1265182459 414 KVLIIEDFHIKYIEV 428
Cdd:COG1253   411 EVLDMDGRRIDKVLV 425
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 17-201 3.63e-52

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 173.56  E-value: 3.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  17 AFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLGITITALGLGWLGEPTLDRLLHPLfttfhtne 96
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  97 plaGILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIFGITmISENE 176
Cdd:pfam01595  83 ---GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVK-GGESE 158

                         170       180
                  ....*....|....*....|....*
gi 1265182459 177 AAHSEEELRILLSESFEGGEINQSE 201
Cdd:pfam01595 159 PAVTEEELRSLVEESAEEGVIEEEE 183
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 88-428 1.71e-39

gliding motility-associated protein GldE; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. GldE was discovered because of its adjacency to GldD in F. johnsonii. Overexpression of GldE partially supresses the effects of a GldB point mutant suggesting that GldB and GldE interact. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility and in fact some do not appear to express the gliding phenotype.


Pssm-ID: 274626 [Multi-domain]  Cd Length: 407  Bit Score: 146.34  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  88 LFTTFHTNeplagILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIF 167
Cdd:TIGR03520  75 LFGSFNTE-----LLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 168 GI--TMISENEAAHSEEelriLLSESFEGGEinqsEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVE 245
Cdd:TIGR03520 150 GKqkSNISVDQLSQALE----LTDEEDTTKE----EQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIEN 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 246 KYTRYPIVEDgDKDKVIGLVNIKEIyndIVFNEKDGTNtLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGT 325
Cdd:TIGR03520 222 GYSRIPVYKE-TIDNITGVLYIKDL---LPHLNKKNFD-WQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGT 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 326 AGLVTVEDIIEEIVGEIRDEFDTDEIPYvQKIKDDHYILDGKmliSQVNDLLG-TDISDE-------EVDTIAGWVL--T 395
Cdd:TIGR03520 297 SGLVTLEDIIEEIVGDISDEFDDEDLIY-SKIDDNNYVFEGK---TSLKDFYKiLKLEEDmfdevkgEAETLAGFLLeiS 372

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1265182459 396 EKFDvTKNDIIQHEQFYFKVLIIEDFHIKYIEV 428
Cdd:TIGR03520 373 GGFP-KKGEKITFENFEFTIEAMDKKRIKQVKV 404
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 216-336 4.55e-36

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: 128.77  E-value: 4.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 216 AKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRYPIVeDGDKDKVIGLVNIKEIYNDIVfnEKDGTNTLESYVKPIFKV 295
Cdd:cd04590     2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVY-EGDLDNIIGVLHVKDLLAALL--EGREKLDLRALLRPPLFV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1265182459 296 IETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDIIE 336
Cdd:cd04590    79 PETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
175-394 1.46e-28

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 113.75  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 175 NEAAHSE----EELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRY 250
Cdd:PRK15094   24 SQLFHGEpknrDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 251 PIVEDgDKDKVIGLVNIKEIyndIVFNEKDGTN-TLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLV 329
Cdd:PRK15094  104 PVISE-DKDHIEGILMAKDL---LPFMRSDAEAfSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLV 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182459 330 TVEDIIEEIVGEIRDEFDTDEIPYVQKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVL 394
Cdd:PRK15094  180 TIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVM 244
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 355-428 3.57e-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: 3.57e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182459  355 QKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVLTEKFDV-TKNDIIQHEQFYFKVLIIEDFHIKYIEV 428
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIpEVGDSVEIGGLRFEVLEVDGRRIDKVRV 75
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 16-428 2.04e-159

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 456.89  E-value: 2.04e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  16 TAFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLGITITALGLGWLGEPTLDRLLHPLFTTFHTN 95
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  96 EPLAGILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIFGITmISEN 175
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIE-PAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 176 EAAHSEEELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRYPIVeD 255
Cdd:COG1253   176 EPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVY-E 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 256 GDKDKVIGLVNIKEIYNDIVfneKDGTNTLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDII 335
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRALL---EGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDIL 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 336 EEIVGEIRDEFDTDEiPYVQKIKDDHYILDGKMLISQVNDLLGTDI-SDEEVDTIAGWVLTEKFDV-TKNDIIQHEQFYF 413
Cdd:COG1253   332 EEIVGEIRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIpEVGETVEVDGLRF 410

                         410
                  ....*....|....*
gi 1265182459 414 KVLIIEDFHIKYIEV 428
Cdd:COG1253   411 EVLDMDGRRIDKVLV 425
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 17-428 5.81e-84

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: 263.86  E-value: 5.81e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  17 AFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLGITI---------TALGLGWLGEptldrllhp 87
Cdd:COG4536    21 AFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLvnilasslaTVIAIRLFGD--------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  88 lfttfhtneplAGIlsfVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIF 167
Cdd:COG4536    92 -----------AGV---AIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 168 GITMISENEAAHSEEELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKY 247
Cdd:COG4536   158 GVKPDADASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPH 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 248 TRYPiVEDGDKDKVIGLVNIKEIYNDIVFNEKDGTNtLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAG 327
Cdd:COG4536   238 TRLP-VYRGDIDNIVGVLHVRDLLRALRKGDLSKED-LRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 328 LVTVEDIIEEIVGEIRDEFDtDEIPYVQKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVLtEKFDV--TKNDI 405
Cdd:COG4536   316 LVTLEDILEEIVGEITDEHD-PDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLII-EELEDipEAGQS 393

                         410       420
                  ....*....|....*....|...
gi 1265182459 406 IQHEQFYFKVLIIEDFHIKYIEV 428
Cdd:COG4536   394 FTIHGYRFEILQVQDNRIKTVRI 416
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 17-201 3.63e-52

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 173.56  E-value: 3.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  17 AFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLGITITALGLGWLGEPTLDRLLHPLfttfhtne 96
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  97 plaGILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIFGITmISENE 176
Cdd:pfam01595  83 ---GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVK-GGESE 158

                         170       180
                  ....*....|....*....|....*
gi 1265182459 177 AAHSEEELRILLSESFEGGEINQSE 201
Cdd:pfam01595 159 PAVTEEELRSLVEESAEEGVIEEEE 183
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 180-416 7.55e-44

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


Pssm-ID: 443601 [Multi-domain]  Cd Length: 288  Bit Score: 154.88  E-value: 7.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 180 SEEELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRYPIVEDgDKD 259
Cdd:COG4535    29 DREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGE-DRD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 260 KVIGLVNIKeiynD---IVFNEKDGTNtLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDIIE 336
Cdd:COG4535   108 EVIGILLAK----DllrYLAQDAEEFD-LRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLE 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 337 EIVGEIRDEFDTDEIP-YVQKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVLTEkFD--VTKNDIIQHEQFYF 413
Cdd:COG4535   183 QIVGEIEDEHDEDEDEdNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQE-FGhlPKRGESIEIDGLRF 261


                  ...
gi 1265182459 414 KVL 416
Cdd:COG4535   262 KVL 264
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 88-428 1.71e-39

gliding motility-associated protein GldE; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. GldE was discovered because of its adjacency to GldD in F. johnsonii. Overexpression of GldE partially supresses the effects of a GldB point mutant suggesting that GldB and GldE interact. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility and in fact some do not appear to express the gliding phenotype.


Pssm-ID: 274626 [Multi-domain]  Cd Length: 407  Bit Score: 146.34  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  88 LFTTFHTNeplagILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIF 167
Cdd:TIGR03520  75 LFGSFNTE-----LLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 168 GI--TMISENEAAHSEEelriLLSESFEGGEinqsEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVE 245
Cdd:TIGR03520 150 GKqkSNISVDQLSQALE----LTDEEDTTKE----EQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIEN 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 246 KYTRYPIVEDgDKDKVIGLVNIKEIyndIVFNEKDGTNtLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGT 325
Cdd:TIGR03520 222 GYSRIPVYKE-TIDNITGVLYIKDL---LPHLNKKNFD-WQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGT 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 326 AGLVTVEDIIEEIVGEIRDEFDTDEIPYvQKIKDDHYILDGKmliSQVNDLLG-TDISDE-------EVDTIAGWVL--T 395
Cdd:TIGR03520 297 SGLVTLEDIIEEIVGDISDEFDDEDLIY-SKIDDNNYVFEGK---TSLKDFYKiLKLEEDmfdevkgEAETLAGFLLeiS 372

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1265182459 396 EKFDvTKNDIIQHEQFYFKVLIIEDFHIKYIEV 428
Cdd:TIGR03520 373 GGFP-KKGEKITFENFEFTIEAMDKKRIKQVKV 404
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 216-336 4.55e-36

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: 128.77  E-value: 4.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 216 AKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRYPIVeDGDKDKVIGLVNIKEIYNDIVfnEKDGTNTLESYVKPIFKV 295
Cdd:cd04590     2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVY-EGDLDNIIGVLHVKDLLAALL--EGREKLDLRALLRPPLFV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1265182459 296 IETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDIIE 336
Cdd:cd04590    79 PETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
175-394 1.46e-28

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 113.75  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 175 NEAAHSE----EELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASKDDVVEVFLQIANVEKYTRY 250
Cdd:PRK15094   24 SQLFHGEpknrDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 251 PIVEDgDKDKVIGLVNIKEIyndIVFNEKDGTN-TLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLV 329
Cdd:PRK15094  104 PVISE-DKDHIEGILMAKDL---LPFMRSDAEAfSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLV 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182459 330 TVEDIIEEIVGEIRDEFDTDEIPYVQKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVL 394
Cdd:PRK15094  180 TIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVM 244
PRK11573 PRK11573
hypothetical protein; Provisional
 16-428 1.63e-28

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 116.39  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  16 TAFFVATEFAIVKVRSSKINQLLEEGHKKAVSAKHVITHLDEYLSACQLG---ITITALGLGWLgeptldrllhplfttf 92
Cdd:PRK11573    5 SAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGnnlVNILASALGTI---------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459  93 hTNEPLAGILSFVIAFVVITFLHVVLGELAPKTFAIQMAEQITLNFAKPIIVFYKLMYPFIKILNGSARMLTKIFGITMI 172
Cdd:PRK11573   69 -VGMRLYGDAGVAIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 173 SENEAAHSEEELRILLSESfeGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSAS-KDDVVEVFLQIANvEKYTRYP 251
Cdd:PRK11573  148 IVVSGALSKEELRTIVHES--RSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDiNDDWKSILRQLTH-SPHGRIV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 252 IVEDgDKDKVIGLVNIKEIYNDIVFNEKDGTNTLESYVKPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTV 331
Cdd:PRK11573  225 LYRD-SLDDAISMLRVREAYRLMTEKKEFTKENMLRAADEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTV 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 332 EDIIEEIVGEIRDEFDTDEIPYVQKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVLTEKFDV-TKNDIIQHEQ 410
Cdd:PRK11573  304 EDILEEIVGDFTTSMSPTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIpVAGTRVRIGE 383

                         410
                  ....*....|....*...
gi 1265182459 411 FYFKVLIIEDFHIKYIEV 428
Cdd:PRK11573  384 YDIDILDVQDNMIKQVKV 401
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 355-428 3.57e-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: 3.57e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265182459  355 QKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVLTEKFDV-TKNDIIQHEQFYFKVLIIEDFHIKYIEV 428
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIpEVGDSVEIGGLRFEVLEVDGRRIDKVRV 75
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 355-428 7.98e-13

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: 63.72  E-value: 7.98e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265182459 355 QKIKDDHYILDGKMLISQVNDLLGTDISDEEVDTIAGWVLTEKFDVTKND---IIQHEQFYFKVLIIEDFHIKYIEV 428
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGdkvEVELGGLRFTVLEMDGRRIKKVRI 77
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
155-338 2.83e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 44.87  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 155 ILNGSARMLTKIFGITMISENEAAHSEEELRILLSESFEGGEINQSEYRYMSKIFDFDDRLAKEVMVPRTEIVSASK--D 232
Cdd:COG2524    27 AALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTtlE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 233 DVVEVFLQianvEKYTRYPIVEDGdkdKVIGLVNIKeiynDIVFNEKDGTNTLESYV-----KPIFKVIETVPIHDLLVK 307
Cdd:COG2524   107 EALELMLE----KGISGLPVVDDG---KLVGIITER----DLLKALAEGRDLLDAPVsdimtRDVVTVSEDDSLEEALRL 175

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1265182459 308 MQKERIQMAILFDEYGGTAGLVTVEDIIEEI 338
Cdd:COG2524   176 MLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
215-336 3.36e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 40.67  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 215 LAKEVMVpRTEIVSASKDDVVEVFLQIANVEKYTRYPIVEDgdKDKVIGLVNIKEIyndivfNEKDGTNTLESYV-KPIF 293
Cdd:COG4109    17 LVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDE--NGRLVGIVTSKDI------LGKDDDTPIEDVMtKNPI 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1265182459 294 KVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDIIE 336
Cdd:COG4109    88 TVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 223-335 3.94e-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: 36.84  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 223 RTEIVSASKDDVVEVFLQIANVEKYTRYPIVEDgdKDKVIGLVNIKEIYNDIVFNEKDGTNTLESYV-KPIFKVIETVPI 301
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDD--DGKLVGIVTERDILRALVEGGLALDTPVAEVMtPDVITVSPDTDL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1265182459 302 HDLLVKMQKERIQMAILFDEYGGTAGLVTVEDII 335
Cdd:cd02205    79 EEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 218-336 5.59e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. 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: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 36.78  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 218 EVMVPRTEIVSA--SKDDVVEvfLQIANVEKYTRYPIV-EDGdkdKVIGLVNIKEIYNdiVFNEKDGTNTLESYVKPIfK 294
Cdd:cd04639     1 DAMVTEFPIVDAdlTLREFAD--DYLIGKKSWREFLVTdEAG---RLVGLITVDDLRA--IPTSQWPDTPVRELMKPL-E 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1265182459 295 VIETV----PIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDIIE 336
Cdd:cd04639    73 EIPTVaadqSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIE 118
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 215-270 8.83e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 35.88  E-value: 8.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265182459 215 LAKEVMvpRTEIVSASKD----DVVEVFLQianvEKYTRYPIVEDGdkdKVIGLVNIKEI 270
Cdd:cd04629    63 TVADYM--STEVLTVSPDtsivDLAQLFLK----NKPRRYPVVEDG---KLVGQISRRDV 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 290-340 9.98e-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: 34.50  E-value: 9.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1265182459 290 KPIFKVIETVPIHDLLVKMQKERIQMAILFDEYGGTAGLVTVEDIIEEIVG 340
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 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.
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