NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1797913229|ref|WP_159345102|]
View 

hemolysin family protein [Cytobacillus firmus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 1-434 0e+00

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 518.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229   1 MDILNLVFIAILIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLGITITALGLGWLGEPT 80
Cdd:COG1253     2 SLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  81 IEHLLRPVINSFGLPSSISHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSA 160
Cdd:COG1253    82 LAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 161 RLLTSMFGLKPASEHElAHSEEELRIILSESYESGEINQSEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQ 240
Cdd:COG1253   162 NLLLRLLGIEPAEEEP-AVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 241 IVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTDLIMNRDLsssTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDE 320
Cdd:COG1253   241 LILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPF---DLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 321 YGGTSGLVTVEDIIEEIVGEIRDEFDmDEVPMVRKTQEGQYIIDSKVLVGEVNDLLGTDI-NDEDVDTIGGWILTENYE- 398
Cdd:COG1253   318 YGGTAGLVTLEDILEEIVGEIRDEYD-EEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRi 396

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1797913229 399 AKQGDIIEHEKYLFKILDMEEHHIKYIEVTAVPETE 434
Cdd:COG1253   397 PEVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEE 432
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 1-434 0e+00

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 518.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229   1 MDILNLVFIAILIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLGITITALGLGWLGEPT 80
Cdd:COG1253     2 SLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  81 IEHLLRPVINSFGLPSSISHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSA 160
Cdd:COG1253    82 LAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 161 RLLTSMFGLKPASEHElAHSEEELRIILSESYESGEINQSEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQ 240
Cdd:COG1253   162 NLLLRLLGIEPAEEEP-AVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 241 IVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTDLIMNRDLsssTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDE 320
Cdd:COG1253   241 LILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPF---DLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 321 YGGTSGLVTVEDIIEEIVGEIRDEFDmDEVPMVRKTQEGQYIIDSKVLVGEVNDLLGTDI-NDEDVDTIGGWILTENYE- 398
Cdd:COG1253   318 YGGTAGLVTLEDILEEIVGEIRDEYD-EEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRi 396

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1797913229 399 AKQGDIIEHEKYLFKILDMEEHHIKYIEVTAVPETE 434
Cdd:COG1253   397 PEVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEE 432
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 9-201 8.22e-56

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: 183.19  E-value: 8.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229   9 IAILIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLGITITALGLGWLGEPTIEHLLRPV 88
Cdd:pfam01595   3 ALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  89 insfglpssisHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSARLLTSMFG 168
Cdd:pfam01595  83 -----------GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFG 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1797913229 169 LKPaSEHELAHSEEELRIILSESYESGEINQSE 201
Cdd:pfam01595 152 VKG-GESEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 216-335 7.30e-46

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: 154.96  E-value: 7.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTDLImnRDLSSSTLESYIRPIIRVI 295
Cdd:cd04590     2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALL--EGREKLDLRALLRPPLFVP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1797913229 296 DSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIE 335
Cdd:cd04590    80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
212-441 1.54e-42

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 151.88  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 212 DNRIaKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTdlIMNRDLSSSTLESYIRPI 291
Cdd:PRK15094   66 DQRV-RDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLP--FMRSDAEAFSMDKVLRQA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 292 IRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEIVGEIRDEFDMDEVPMVRKTQEGQYIIDSKVLVGE 371
Cdd:PRK15094  143 VVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIED 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797913229 372 VNDLLGTDINDEDVDTIGGWILTE-NYEAKQGDIIEHEKYLFKILDMEEHHIKYIEVTaVPEtEVPAPAKE 441
Cdd:PRK15094  223 FNEAFGTHFSDEEVDTIGGLVMQAfGHLPARGETIDIDGYQFKVAMADSRRIIQVHVK-IPD-DSPQPKLD 291
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 99-428 2.92e-40

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: 148.65  E-value: 2.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  99 SHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSARLLTSMFGLK--PASEHE 176
Cdd:TIGR03520  81 TELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQksNISVDQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 177 LAHSEEelriILSESYESGEinqsEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGD 256
Cdd:TIGR03520 161 LSQALE----LTDEEDTTKE----EQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKET 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 257 KDHIIGMVNIKEVMTDLimNRDlsSSTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEE 336
Cdd:TIGR03520 233 IDNITGVLYIKDLLPHL--NKK--NFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEE 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 337 IVGEIRDEFDMDEVpMVRKTQEGQYIIDSKVLVGEVNDLLGTDIND-EDV----DTIGGWILTENYE-AKQGDIIEHEKY 410
Cdd:TIGR03520 309 IVGDISDEFDDEDL-IYSKIDDNNYVFEGKTSLKDFYKILKLEEDMfDEVkgeaETLAGFLLEISGGfPKKGEKITFENF 387

                         330
                  ....*....|....*...
gi 1797913229 411 LFKILDMEEHHIKYIEVT 428
Cdd:TIGR03520 388 EFTIEAMDKKRIKQVKVT 405
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 354-428 3.36e-17

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: 75.94  E-value: 3.36e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797913229  354 RKTQEGQYIIDSKVLVGEVNDLLGTDINDEDVDTIGGWILTEN-YEAKQGDIIEHEKYLFKILDMEEHHIKYIEVT 428
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELgRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 1-434 0e+00

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 518.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229   1 MDILNLVFIAILIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLGITITALGLGWLGEPT 80
Cdd:COG1253     2 SLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  81 IEHLLRPVINSFGLPSSISHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSA 160
Cdd:COG1253    82 LAALLAPLLGSLGLPAALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 161 RLLTSMFGLKPASEHElAHSEEELRIILSESYESGEINQSEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQ 240
Cdd:COG1253   162 NLLLRLLGIEPAEEEP-AVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 241 IVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTDLIMNRDLsssTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDE 320
Cdd:COG1253   241 LILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGEPF---DLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 321 YGGTSGLVTVEDIIEEIVGEIRDEFDmDEVPMVRKTQEGQYIIDSKVLVGEVNDLLGTDI-NDEDVDTIGGWILTENYE- 398
Cdd:COG1253   318 YGGTAGLVTLEDILEEIVGEIRDEYD-EEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRi 396

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1797913229 399 AKQGDIIEHEKYLFKILDMEEHHIKYIEVTAVPETE 434
Cdd:COG1253   397 PEVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEE 432
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 2-431 6.52e-100

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: 305.08  E-value: 6.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229   2 DILNLVFIAILIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLGITI---------TALG 72
Cdd:COG4536     6 LSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLvnilasslaTVIA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  73 LGWLGEPTIehllrpvinsfglpssishvisfSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPI 152
Cdd:COG4536    86 IRLFGDAGV-----------------------AIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 153 IWALNGSARLLTSMFGLKPASEHELAHSEEELRIILSESYESGEINQSEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKD 232
Cdd:COG4536   143 VWLVNLIVRGLLRLFGVKPDADASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLD 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 233 DTLEDFLQIVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTdLIMNRDLSSSTLESYIRPIIRVIDSIPIHELLLKMQKERI 312
Cdd:COG4536   223 DPWEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLLR-ALRKGDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKR 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 313 HMAILMDEYGGTSGLVTVEDIIEEIVGEIRDEFDMDEvPMVRKTQEGQYIIDSKVLVGEVNDLLGTDINDEDVDTIGGWI 392
Cdd:COG4536   302 RFALVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDA-EEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLI 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1797913229 393 LtENYEA--KQGDIIEHEKYLFKILDMEEHHIKYIEVTAVP 431
Cdd:COG4536   381 I-EELEDipEAGQSFTIHGYRFEILQVQDNRIKTVRIRPLP 420
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 180-439 2.87e-58

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: 193.02  E-value: 2.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 180 SEEELRIILSESYESGEINQSEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKDH 259
Cdd:COG4535    29 DREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 260 IIGMVNIKevmtDLI--MNRDLSSSTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEI 337
Cdd:COG4535   109 VIGILLAK----DLLryLAQDAEEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 338 VGEIRDEFDMDEVP-MVRKTQEGQYIIDSKVLVGEVNDLLGTDINDEDVDTIGGWILTE-NYEAKQGDIIEHEKYLFKIL 415
Cdd:COG4535   185 VGEIEDEHDEDEDEdNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEfGHLPKRGESIEIDGLRFKVL 264

                         250       260
                  ....*....|....*....|....
gi 1797913229 416 DMEEHHIKYIEVTAVPETEVPAPA 439
Cdd:COG4535   265 RADSRRIHLLRVTRLPPAAEPDAE 288
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 9-201 8.22e-56

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: 183.19  E-value: 8.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229   9 IAILIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLGITITALGLGWLGEPTIEHLLRPV 88
Cdd:pfam01595   3 ALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  89 insfglpssisHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSARLLTSMFG 168
Cdd:pfam01595  83 -----------GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFG 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1797913229 169 LKPaSEHELAHSEEELRIILSESYESGEINQSE 201
Cdd:pfam01595 152 VKG-GESEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 216-335 7.30e-46

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: 154.96  E-value: 7.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTDLImnRDLSSSTLESYIRPIIRVI 295
Cdd:cd04590     2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALL--EGREKLDLRALLRPPLFVP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1797913229 296 DSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIE 335
Cdd:cd04590    80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
212-441 1.54e-42

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 151.88  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 212 DNRIaKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKDHIIGMVNIKEVMTdlIMNRDLSSSTLESYIRPI 291
Cdd:PRK15094   66 DQRV-RDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLP--FMRSDAEAFSMDKVLRQA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 292 IRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEIVGEIRDEFDMDEVPMVRKTQEGQYIIDSKVLVGE 371
Cdd:PRK15094  143 VVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIED 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797913229 372 VNDLLGTDINDEDVDTIGGWILTE-NYEAKQGDIIEHEKYLFKILDMEEHHIKYIEVTaVPEtEVPAPAKE 441
Cdd:PRK15094  223 FNEAFGTHFSDEEVDTIGGLVMQAfGHLPARGETIDIDGYQFKVAMADSRRIIQVHVK-IPD-DSPQPKLD 291
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 99-428 2.92e-40

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: 148.65  E-value: 2.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  99 SHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSARLLTSMFGLK--PASEHE 176
Cdd:TIGR03520  81 TELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQksNISVDQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 177 LAHSEEelriILSESYESGEinqsEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGD 256
Cdd:TIGR03520 161 LSQALE----LTDEEDTTKE----EQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKET 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 257 KDHIIGMVNIKEVMTDLimNRDlsSSTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEE 336
Cdd:TIGR03520 233 IDNITGVLYIKDLLPHL--NKK--NFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEE 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 337 IVGEIRDEFDMDEVpMVRKTQEGQYIIDSKVLVGEVNDLLGTDIND-EDV----DTIGGWILTENYE-AKQGDIIEHEKY 410
Cdd:TIGR03520 309 IVGDISDEFDDEDL-IYSKIDDNNYVFEGKTSLKDFYKILKLEEDMfDEVkgeaETLAGFLLEISGGfPKKGEKITFENF 387

                         330
                  ....*....|....*...
gi 1797913229 411 LFKILDMEEHHIKYIEVT 428
Cdd:TIGR03520 388 EFTIEAMDKKRIKQVKVT 405
PRK11573 PRK11573
hypothetical protein; Provisional
 12-430 7.25e-36

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 136.80  E-value: 7.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  12 LIALTAFFVTSEFAIVKIRSSRIDQLIEEGNKNAIAAKKVISNLDEYLSACQLG---ITITALGLGwlgepTIehllrpv 88
Cdd:PRK11573    1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGnnlVNILASALG-----TI------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229  89 insfgLPSSISHVISFSIAFAFITFLHVVVGELAPKTLAIQKAEAVTLLTTRPLIWFYRVMYPIIWALNGSARLLTSMFG 168
Cdd:PRK11573   69 -----VGMRLYGDAGVAIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 169 LKPASEHELAHSEEELRIILSESyeSGEINQSEFKYVNKIFEFDNRIAKEIMVPRTEIVSLSKDDTLEDFLQIVQEEKFT 248
Cdd:PRK11573  144 IKTDIVVSGALSKEELRTIVHES--RSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 249 RYPIIDGDKDHIIGMVNIKEVMTDLIMNRDLSSSTLESYIRPIIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLV 328
Cdd:PRK11573  222 RIVLYRDSLDDAISMLRVREAYRLMTEKKEFTKENMLRAADEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLV 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 329 TVEDIIEEIVGEIRDEFDMDEVPMVRKTQEGQYIIDSKVLVGEVNDLLGTDINDEDVDTIGGWILTENYEAKQGDI-IEH 407
Cdd:PRK11573  302 TVEDILEEIVGDFTTSMSPTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTrVRI 381

                         410       420
                  ....*....|....*....|...
gi 1797913229 408 EKYLFKILDMEEHHIKYIEVTAV 430
Cdd:PRK11573  382 GEYDIDILDVQDNMIKQVKVTPV 404
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 354-428 3.36e-17

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: 75.94  E-value: 3.36e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797913229  354 RKTQEGQYIIDSKVLVGEVNDLLGTDINDEDVDTIGGWILTEN-YEAKQGDIIEHEKYLFKILDMEEHHIKYIEVT 428
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELgRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 354-431 6.21e-14

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: 66.80  E-value: 6.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 354 RKTQEGQYIIDSKVLVGEVNDLLGTDINDEDVDTIGGWILTE-NYEAKQGDIIEHEK--YLFKILDMEEHHIKYIEVTAV 430
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERlGRIPKVGDKVEVELggLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 1797913229 431 P 431
Cdd:pfam03471  81 E 81
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
216-337 4.70e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 62.21  E-value: 4.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMVPRteIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdhIIGMVNIKEVMTDLIMNRDLSSSTLESYI-RPIIRV 294
Cdd:COG2524    88 VKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDAPVSDIMtRDVVTV 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1797913229 295 IDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEI 337
Cdd:COG2524   164 SEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 223-334 2.24e-10

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: 57.64  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 223 RTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDgDKDHIIGMVNIKEVMTDLIMNRDLSSSTLESY-IRPIIRVIDSIPIH 301
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVD-DDGKLVGIVTERDILRALVEGGLALDTPVAEVmTPDVITVSPDTDLE 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1797913229 302 ELLLKMQKERIHMAILMDEYGGTSGLVTVEDII 334
Cdd:cd02205    80 EALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
217-335 1.22e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 53.38  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 217 KEIMVpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdHIIGMVNIKEVMT-------DLIMNRDLssstlesyir 289
Cdd:COG4109    19 EDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGkdddtpiEDVMTKNP---------- 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1797913229 290 piIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIE 335
Cdd:COG4109    87 --ITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
216-344 2.55e-08

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 52.56  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMVprTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDgDKDHIIGMVNIKEVMTDLI------MNRDLSSSTLESYIR 289
Cdd:COG3448     4 VRDIMT--RDVVTVSPDTTLREALELMREHGIRGLPVVD-EDGRLVGIVTERDLLRALLpdrldeLEERLLDLPVEDVMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1797913229 290 PIIRVID-SIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEIVGEIRDE 344
Cdd:COG3448    81 RPVVTVTpDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS COG0517
CBS domain [Signal transduction mechanisms];
216-342 1.53e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 49.86  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDgDKDHIIGMVNIKEVMTDLI-MNRDLSSSTLESYI-RPIIR 293
Cdd:COG0517     3 VKDIM--TTDVVTVSPDATVREALELMSEKRIGGLPVVD-EDGKLVGIVTDRDLRRALAaEGKDLLDTPVSEVMtRPPVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1797913229 294 VIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEIVGEIR 342
Cdd:COG0517    80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 225-270 2.64e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 43.23  E-value: 2.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1797913229 225 EIVSLSKDDTLEDFLQIVQEEKFTRYPIIDgDKDHIIGMVNIKEVM 270
Cdd:cd04596     3 ETGYLRETDTVRDYKQLSEETGHSRFPVVD-EENRVVGIVTAKDVI 47
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 216-334 2.80e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 43.28  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDkDHIIGMVNIKEVMTDLIM-NRDLSSSTLESY-IRPIIR 293
Cdd:COG2905     1 VKDIM--SRDVVTVSPDATVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLRRRVLAeGLDPLDTPVSEVmTRPPIT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1797913229 294 VIDSIPIHELLLKMQKERIHMAILMDEyGGTSGLVTVEDII 334
Cdd:COG2905    78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 216-270 4.37e-05

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: 41.04  E-value: 4.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1797913229 216 AKEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDkDHIIGMVNIKEVM 270
Cdd:pfam00571   1 VKDIM--TKDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLL 52
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 227-334 1.08e-04

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: 41.75  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 227 VSLSKDDTLEDFLQIVQEEKFTRYPIIDGDkDHIIGMVNIKEVMTDLIMNRDLSSSTLESYI-RPIIRVIDSIPIHELLL 305
Cdd:cd04608    13 VTVLPDDTLGEAIEIMREYGVDQLPVVDED-GRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMyKQFKQVDLDTPLGALSR 91

                          90       100
                  ....*....|....*....|....*....
gi 1797913229 306 KMqkERIHMAILMDEYGGTSGLVTVEDII 334
Cdd:cd04608    92 IL--ERDHFALVVDGQGKVLGIVTRIDLL 118
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 184-270 2.58e-04

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: 40.50  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 184 LRIILSESYESGEINQsefkyvnkifefdnriAKEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdhIIGM 263
Cdd:cd04629    48 LKALLEASYHCEPGGT----------------VADYM--STEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGK--LVGQ 107


                  ....*..
gi 1797913229 264 VNIKEVM 270
Cdd:cd04629   108 ISRRDVL 114
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 216-334 4.91e-04

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. 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.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 40.01  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 216 AKEIMVprTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdhIIGMVNIK---------EVMTDLIM-NRDLSSSTLE 285
Cdd:cd17778     2 VKEFMT--TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK--LVGIVTAMdivkyfgshEAKKRLTTgDIDEAYSTPV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1797913229 286 SYI--RPIIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDII 334
Cdd:cd17778    78 EEImsKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 210-276 7.02e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.43  E-value: 7.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1797913229 210 EFDNRIAKEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdhIIGMVNIKEVMTDLIMN 276
Cdd:COG2905    61 DPLDTPVSEVM--TRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGK--LVGIVSITDLLRALSEE 123
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 217-309 8.70e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. 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: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 39.33  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 217 KEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdhIIGMVnikevmTDLIMNRDLSSSTLESYIRPIIRVID 296
Cdd:cd04584     3 KDIM--TKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGK--LVGIV------TDRDLLRASPSKATSLSIYELNYLLS 72

                          90
                  ....*....|...
gi 1797913229 297 SIPIHELllkMQK 309
Cdd:cd04584    73 KIPVKDI---MTK 82
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 220-335 1.30e-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: 38.71  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 220 MVPRTEIVSlsKDDTLEDF--LQIVQEEKFTRYPIIDGDkDHIIGMVNIKEVMTdlIMNRDLSSSTLESYIRP---IIRV 294
Cdd:cd04639     3 MVTEFPIVD--ADLTLREFadDYLIGKKSWREFLVTDEA-GRLVGLITVDDLRA--IPTSQWPDTPVRELMKPleeIPTV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1797913229 295 IDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIE 335
Cdd:cd04639    78 AADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIE 118
CBS COG0517
CBS domain [Signal transduction mechanisms];
210-270 1.35e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 38.69  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797913229 210 EFDNRIAKEIMvpRTEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdHIIGMVNIKEVM 270
Cdd:COG0517    63 DLLDTPVSEVM--TRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDG-RLVGIITIKDLL 120
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 289-339 2.15e-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: 36.04  E-value: 2.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1797913229 289 RPIIRVIDSIPIHELLLKMQKERIHMAILMDEYGGTSGLVTVEDIIEEIVG 339
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 218-334 3.58e-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: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 37.16  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797913229 218 EIMVPrtEIVSLSKDDTLEDFLQIVQEEKFTRYPIIDGDKdhIIGMVNIKEVmtdlimnRDLSSSTLESYI------RPI 291
Cdd:cd04801     1 DIMTP--EVVTVTPEMTVSELLDRMFEEKHLGYPVVENGR--LVGIVTLEDI-------RKVPEVEREATRvrdvmtKDV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1797913229 292 IRVIDSIPIHELLLKMQKERIHMAILMDEyGGTSGLVTVEDII 334
Cdd:cd04801    70 ITVSPDADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH