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Conserved domains on  [gi|2750757569|ref|WP_353047654|]
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MULTISPECIES: hemolysin family protein [Exiguobacterium]

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 ...
 5-409 1.39e-151

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 436.47  E-value: 1.39e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569   5 SIILYVVLVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSI 84
Cdd:COG1253     6 ELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  85 F-------------SGGTGLLVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTL 151
Cdd:COG1253    86 LapllgslglpaalAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 152 RMIGMK--DKEPSVTEEELKVLVDMGEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSG 229
Cdd:COG1253   166 RLLGIEpaEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILES 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 230 GHSRLPVYKDSIDNVIGVLSERDFLRSMMKDEVTDVRSLIRPLTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLI 309
Cdd:COG1253   246 GHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 310 TLEDMLEELVGDIWDEHDESVVYLRRLREGVYECMADMNVDEFAEEMGIAEPDV-DSNTMGGWFVELLGDIPEKGAQVTY 388
Cdd:COG1253   326 TLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEeDYETLGGLVLEQLGRIPEVGETVEV 405

                         410       420
                  ....*....|....*....|.
gi 2750757569 389 QDMTFTVLHVEKRRVRKLLVE 409
Cdd:COG1253   406 DGLRFEVLDMDGRRIDKVLVT 426
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 5-409 1.39e-151

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 436.47  E-value: 1.39e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569   5 SIILYVVLVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSI 84
Cdd:COG1253     6 ELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  85 F-------------SGGTGLLVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTL 151
Cdd:COG1253    86 LapllgslglpaalAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 152 RMIGMK--DKEPSVTEEELKVLVDMGEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSG 229
Cdd:COG1253   166 RLLGIEpaEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILES 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 230 GHSRLPVYKDSIDNVIGVLSERDFLRSMMKDEVTDVRSLIRPLTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLI 309
Cdd:COG1253   246 GHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 310 TLEDMLEELVGDIWDEHDESVVYLRRLREGVYECMADMNVDEFAEEMGIAEPDV-DSNTMGGWFVELLGDIPEKGAQVTY 388
Cdd:COG1253   326 TLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEeDYETLGGLVLEQLGRIPEVGETVEV 405

                         410       420
                  ....*....|....*....|.
gi 2750757569 389 QDMTFTVLHVEKRRVRKLLVE 409
Cdd:COG1253   406 DGLRFEVLDMDGRRIDKVLVT 426
PRK11573 PRK11573
hypothetical protein; Provisional
 12-420 2.13e-56

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 191.12  E-value: 2.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  12 LVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSIFsGGTGL 91
Cdd:PRK11573    1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLY-GDAGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  92 LVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTLRMIGMKD---KEPSVTEEEL 168
Cdd:PRK11573   80 AIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTdivVSGALSKEEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 169 KVLVDmgEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSIDNVIGVL 248
Cdd:PRK11573  160 RTIVH--ESRSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISML 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 249 SERDFLRSMMKDEVTDVRSLIRP---LTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEELVGD---- 321
Cdd:PRK11573  238 RVREAYRLMTEKKEFTKENMLRAadeIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDftts 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 322 --------IWDEHDESVvylrrLREGvyecmaDMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTF 393
Cdd:PRK11573  318 msptlaeeVTPQNDGSV-----IIDG------TANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDI 386

                         410       420
                  ....*....|....*....|....*..
gi 2750757569 394 TVLHVEKRRVRKLLVETGQSQQEDMQE 420
Cdd:PRK11573  387 DILDVQDNMIKQVKVTPVKPLRESVAE 413
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 7-185 4.53e-55

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: 180.49  E-value: 4.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569   7 ILYVVLVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSIFS 86
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  87 --GGTGLLVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTLRMIGMK--DKEPS 162
Cdd:pfam01595  81 plGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKggESEPA 160

                         170       180
                  ....*....|....*....|...
gi 2750757569 163 VTEEELKVLVDMGEEEGVLGETE 185
Cdd:pfam01595 161 VTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 199-316 1.88e-41

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: 142.63  E-value: 1.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 199 TVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSIDNVIGVLSERDFLRSMMKDEV-TDVRSLIRPLTYVSP 277
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREkLDLRALLRPPLFVPE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2750757569 278 QTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLE 316
Cdd:cd04590    81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 334-409 3.30e-16

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: 72.86  E-value: 3.30e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750757569  334 RRLREGVYECMADMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTFTVLHVEKRRVRKLLVE 409
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 5-409 1.39e-151

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 436.47  E-value: 1.39e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569   5 SIILYVVLVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSI 84
Cdd:COG1253     6 ELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  85 F-------------SGGTGLLVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTL 151
Cdd:COG1253    86 LapllgslglpaalAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 152 RMIGMK--DKEPSVTEEELKVLVDMGEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSG 229
Cdd:COG1253   166 RLLGIEpaEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILES 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 230 GHSRLPVYKDSIDNVIGVLSERDFLRSMMKDEVTDVRSLIRPLTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLI 309
Cdd:COG1253   246 GHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 310 TLEDMLEELVGDIWDEHDESVVYLRRLREGVYECMADMNVDEFAEEMGIAEPDV-DSNTMGGWFVELLGDIPEKGAQVTY 388
Cdd:COG1253   326 TLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEeDYETLGGLVLEQLGRIPEVGETVEV 405

                         410       420
                  ....*....|....*....|.
gi 2750757569 389 QDMTFTVLHVEKRRVRKLLVE 409
Cdd:COG1253   406 DGLRFEVLDMDGRRIDKVLVT 426
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 3-408 7.27e-150

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: 431.42  E-value: 7.27e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569   3 SSSIILYVVLVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIAT 82
Cdd:COG4536     7 SLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  83 SIFsGGTGLLVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTLRMIGMK---DK 159
Cdd:COG4536    87 RLF-GDAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKpdaDA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 160 EPSVTEEELKVLVDMGEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKD 239
Cdd:COG4536   166 SDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 240 SIDNVIGVLSERDFLRSMMKDEVT--DVRSLIRPLTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEE 317
Cdd:COG4536   246 DIDNIVGVLHVRDLLRALRKGDLSkeDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEE 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 318 LVGDIWDEHDESVVYLRRLREGVYECMADMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTFTVLH 397
Cdd:COG4536   326 IVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQ 405

                         410
                  ....*....|.
gi 2750757569 398 VEKRRVRKLLV 408
Cdd:COG4536   406 VQDNRIKTVRI 416
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 160-420 5.39e-63

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: 204.57  E-value: 5.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 160 EPSVTEEELKVLVDMgEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKD 239
Cdd:COG4535    26 EPEDREELLELLRDA-EERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 240 SIDNVIGVLSERDFLRSMMKD-EVTDVRSLIRPLTYVsPQTK-LIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEE 317
Cdd:COG4535   105 DRDEVIGILLAKDLLRYLAQDaEEFDLRDLLRPAVFV-PESKrLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 318 LVGDIWDEHD--ESVVYLRRLREGVYECMADMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTFTV 395
Cdd:COG4535   184 IVGEIEDEHDedEDEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEFGHLPKRGESIEIDGLRFKV 263

                         250       260
                  ....*....|....*....|....*
gi 2750757569 396 LHVEKRRVRKLLVETGQSQQEDMQE 420
Cdd:COG4535   264 LRADSRRIHLLRVTRLPPAAEPDAE 288
PRK11573 PRK11573
hypothetical protein; Provisional
 12-420 2.13e-56

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 191.12  E-value: 2.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  12 LVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSIFsGGTGL 91
Cdd:PRK11573    1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLY-GDAGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  92 LVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTLRMIGMKD---KEPSVTEEEL 168
Cdd:PRK11573   80 AIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTdivVSGALSKEEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 169 KVLVDmgEEEGVLGETEAELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSIDNVIGVL 248
Cdd:PRK11573  160 RTIVH--ESRSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISML 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 249 SERDFLRSMMKDEVTDVRSLIRP---LTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEELVGD---- 321
Cdd:PRK11573  238 RVREAYRLMTEKKEFTKENMLRAadeIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDftts 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 322 --------IWDEHDESVvylrrLREGvyecmaDMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTF 393
Cdd:PRK11573  318 msptlaeeVTPQNDGSV-----IIDG------TANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDI 386

                         410       420
                  ....*....|....*....|....*..
gi 2750757569 394 TVLHVEKRRVRKLLVETGQSQQEDMQE 420
Cdd:PRK11573  387 DILDVQDNMIKQVKVTPVKPLRESVAE 413
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 7-185 4.53e-55

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: 180.49  E-value: 4.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569   7 ILYVVLVMLSAFFSSAETALSSVNRVRMIRMAEDGDKAAKRVLSLVDRFDDTLSTILVGNNIVNIGSATVSTAIATSIFS 86
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569  87 --GGTGLLVSTFATTVIILIFGEILPKSLAKEFAEKYSLLISGILVFLVKVLKPVTMIFTGLKKLTLRMIGMK--DKEPS 162
Cdd:pfam01595  81 plGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKggESEPA 160

                         170       180
                  ....*....|....*....|...
gi 2750757569 163 VTEEELKVLVDMGEEEGVLGETE 185
Cdd:pfam01595 161 VTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 199-316 1.88e-41

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: 142.63  E-value: 1.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 199 TVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSIDNVIGVLSERDFLRSMMKDEV-TDVRSLIRPLTYVSP 277
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREkLDLRALLRPPLFVPE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2750757569 278 QTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLE 316
Cdd:cd04590    81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
160-408 1.26e-29

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 116.45  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 160 EPSVTEEELKVLVDMGEEEGVLGETEaELVHSAFAFNDITVDDVLTPRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYKD 239
Cdd:PRK15094   30 EPKNRDELLALIRDSEQNDLIDEDTR-DMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 240 SIDNVIGVLSERDFLRSMMKD-EVTDVRSLIRPLTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEEL 318
Cdd:PRK15094  109 DKDHIEGILMAKDLLPFMRSDaEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 319 VGDIWDEHD-ESVVYLRRLREGVYECMADMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTFTVLH 397
Cdd:PRK15094  189 VGEIEDEYDeEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAM 268

                         250
                  ....*....|.
gi 2750757569 398 VEKRRVRKLLV 408
Cdd:PRK15094  269 ADSRRIIQVHV 279
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 334-409 3.30e-16

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: 72.86  E-value: 3.30e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750757569  334 RRLREGVYECMADMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQDMTFTVLHVEKRRVRKLLVE 409
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 334-409 3.17e-15

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: 70.27  E-value: 3.17e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2750757569 334 RRLREGVYECMADMNVDEFAEEMGIAEPDVDSNTMGGWFVELLGDIPEKGAQVTYQ--DMTFTVLHVEKRRVRKLLVE 409
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKVEVElgGLRFTVLEMDGRRIKKVRIT 78
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
198-319 8.81e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 59.49  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 198 ITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSiDNVIGVLSERDFLRSMMKDEVTDVRSLIRPLT---- 273
Cdd:COG3448     2 MTVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLPDRLDELEERLLDLPvedv 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2750757569 274 ------YVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEELV 319
Cdd:COG3448    79 mtrpvvTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS COG0517
CBS domain [Signal transduction mechanisms];
198-319 6.20e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 56.80  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 198 ITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSiDNVIGVLSERDFLRSMMKDEVTDVRSLI-----RPL 272
Cdd:COG0517     1 MKVKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRRALAAEGKDLLDTPVsevmtRPP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2750757569 273 TYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEELV 319
Cdd:COG0517    78 VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
197-318 1.42e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 57.59  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 197 DITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDsiDNVIGVLSERDFLRSMMKDEVTD---VRSLI-RPL 272
Cdd:COG2524    85 KMKVKDIMTK--DVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLdapVSDIMtRDV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2750757569 273 TYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEEL 318
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 209-315 2.17e-09

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: 54.94  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 209 DILAVDIDDSLDEIKDTIFSGGHSRLPVyKDSIDNVIGVLSERDFLRSMMKDEVTDVRS----LIRPLTYVSPQTKLIEL 284
Cdd:cd02205     3 DVVTVDPDTTVREALELMAENGIGALPV-VDDDGKLVGIVTERDILRALVEGGLALDTPvaevMTPDVITVSPDTDLEEA 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750757569 285 LPILQQKQSHMAVVLDEFGGTAGLITLEDML 315
Cdd:cd02205    82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
198-318 5.56e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 51.45  E-value: 5.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 198 ITVDDVLTpRIDILAVDIDDSLDEIKDTIFSGGHSRLPVYkDSIDNVIGVLSERDFLRSMMKDEVTDVRSliRPLTYVSP 277
Cdd:COG4109    16 LLVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVV-DENGRLVGIVTSKDILGKDDDTPIEDVMT--KNPITVTP 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750757569 278 QTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEEL 318
Cdd:COG4109    92 DTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 202-318 2.87e-07

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: 49.11  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 202 DVLTPRIDIlaVDIDDSLDEIKDTIFSGGHSRLPVY-KDSIDNVIGVLSeRDFLRSMMKDE--VTDVRSLIRPL---TYV 275
Cdd:cd04639     1 DAMVTEFPI--VDADLTLREFADDYLIGKKSWREFLvTDEAGRLVGLIT-VDDLRAIPTSQwpDTPVRELMKPLeeiPTV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2750757569 276 SPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEEL 318
Cdd:cd04639    78 AADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIELL 120
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 197-315 1.34e-06

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 47.14  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 197 DITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSiDNVIGVLSERDFLRSMMKDEV--TD-VRSLI-RPL 272
Cdd:cd04608     1 DLIVRRLDLG--APVTVLPDDTLGEAIEIMREYGVDQLPVVDED-GRVVGMVTEGNLLSSLLAGRAqpSDpVSKAMyKQF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2750757569 273 TYVSPQTKLIELLPILQQkqSHMAVVLDEFGGTAGLITLEDML 315
Cdd:cd04608    78 KQVDLDTPLGALSRILER--DHFALVVDGQGKVLGIVTRIDLL 118
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 200-318 9.02e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 44.82  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 200 VDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVyKDSIDNVIGVLSERDFLRSMMKDE-------VTDVRSliRPL 272
Cdd:COG2905     1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVV-VDDDGRLVGIITDRDLRRRVLAEGldpldtpVSEVMT--RPP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2750757569 273 TYVSPQTKLIELLPILQQKQSHMAVVLDEfGGTAGLITLEDMLEEL 318
Cdd:COG2905    76 ITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRAL 120
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 200-259 1.34e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 39.50  E-value: 1.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 200 VDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSiDNVIGVLSERDFLRSMMK 259
Cdd:pfam00571   1 VKDIMTK--DVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALLG 57
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
196-260 2.01e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 41.00  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750757569 196 NDITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSiDNVIGVLSERDFLRSMMKD 260
Cdd:COG3448    71 LDLPVEDVMTR--PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLRALARL 132
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 170-260 1.25e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.66  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750757569 170 VLVDMGEEEGVLgeTEAELVHSAFA----FNDITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDsiDNVI 245
Cdd:COG2905    35 VVDDDGRLVGII--TDRDLRRRVLAegldPLDTPVSEVMTR--PPITVSPDDSLAEALELMEEHRIRHLPVVDD--GKLV 108

                          90
                  ....*....|....*
gi 2750757569 246 GVLSERDFLRSMMKD 260
Cdd:COG2905   109 GIVSITDLLRALSEE 123
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
197-259 2.82e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.97  E-value: 2.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2750757569 197 DITVDDVLTPriDILAVDIDDSLDEIKDTIFSGGHSRLPVYKDSiDNVIGVLSERDFLRSMMK 259
Cdd:COG4109    75 DTPIEDVMTK--NPITVTPDTSLASAAHKMIWEGIELLPVVDDD-GRLLGIISRQDVLKALQK 134
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 270-320 4.32e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 35.27  E-value: 4.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2750757569 270 RPLTYVSPQTKLIELLPILQQKQSHMAVVLDEFGGTAGLITLEDMLEELVG 320
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.
  • 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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