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Conserved domains on  [gi|647576056|ref|WP_025853929|]
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MULTISPECIES: hemolysin family protein [Bacillus]

Protein Classification

hemolysin family protein( domain architecture ID 11441338)

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

Gene Ontology:  GO:0016020|GO:0005886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 16-428 1.36e-171

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 487.70  E-value: 1.36e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  16 TAIFVAAEFAIVKIRGSKIAELVETGDSRALAAHRVISNLDEYLSACQLGITITALGLGWLGEPTIQRLLHPVFSLIGMP 95
Cdd:COG1253   17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  96 SSITHVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFHSVKEH 175
Cdd:COG1253   97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 176 EVVVSEEeLRLILSESYKKGQINQSEFRYVNKIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKE 255
Cdd:COG1253  177 PAVTEEE-LRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 256 DKDHILGIINNKDLFKAYFLGRSIELKEMMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIV 335
Cdd:COG1253  256 DLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIV 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 336 GEIRDEYDQDEmPHIVKKGEHHYVMDGKALIEEVNDLLDIAI-ENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLE 413
Cdd:COG1253  336 GEIRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIpEVGETVEVDGLRFEVLD 414

                        410
                 ....*....|....*
gi 647576056 414 AEDHHIRFVEIKKTD 428
Cdd:COG1253  415 MDGRRIDKVLVTRLP 429
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 16-428 1.36e-171

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 487.70  E-value: 1.36e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  16 TAIFVAAEFAIVKIRGSKIAELVETGDSRALAAHRVISNLDEYLSACQLGITITALGLGWLGEPTIQRLLHPVFSLIGMP 95
Cdd:COG1253   17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  96 SSITHVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFHSVKEH 175
Cdd:COG1253   97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 176 EVVVSEEeLRLILSESYKKGQINQSEFRYVNKIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKE 255
Cdd:COG1253  177 PAVTEEE-LRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 256 DKDHILGIINNKDLFKAYFLGRSIELKEMMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIV 335
Cdd:COG1253  256 DLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIV 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 336 GEIRDEYDQDEmPHIVKKGEHHYVMDGKALIEEVNDLLDIAI-ENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLE 413
Cdd:COG1253  336 GEIRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIpEVGETVEVDGLRFEVLD 414

                        410
                 ....*....|....*
gi 647576056 414 AEDHHIRFVEIKKTD 428
Cdd:COG1253  415 MDGRRIDKVLVTRLP 429
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 215-332 2.57e-48

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: 160.74  E-value: 2.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 215 VAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDHILGIINNKDLFKAYFLGR-SIELKEMMRPVIRVIE 293
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGReKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 647576056 294 SIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILE 332
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
212-428 1.06e-45

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 159.97  E-value: 1.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 212 DNRVaREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDHILGIINNKDLFKayFLGRSIE---LKEMMRPV 288
Cdd:PRK15094  66 DQRV-RDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLP--FMRSDAEafsMDKVLRQA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 289 IRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDEYDQDEMPHIVKKGEHHYVMDGKALIEE 368
Cdd:PRK15094 143 VVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIED 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647576056 369 VNDLLDIAIENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLEAEDHHIRFVEIKKTD 428
Cdd:PRK15094 223 FNEAFGTHFSDEEVDTIGGLVMQAFGHLpARGETIDIDGYQFKVAMADSRRIIQVHVKIPD 283
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 17-201 1.12e-42

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: 148.13  E-value: 1.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056   17 AIFVAAEFAIVKIRGSKIAELVETGDSRALAAHRVISNLDEYLSACQLGITITALGLGWLGEPTIQRLLHPVfsligmps 96
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056   97 sitHVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFhSVKEHE 176
Cdd:pfam01595  83 ---GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGV-KGGESE 158

                         170       180
                  ....*....|....*....|....*
gi 647576056  177 VVVSEEELRLILSESYKKGQINQSE 201
Cdd:pfam01595 159 PAVTEEELRSLVEESAEEGVIEEEE 183
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 99-426 2.84e-42

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: 153.66  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056   99 THVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFH-SVKEHEV 177
Cdd:TIGR03520  81 TELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQkSNISVDQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  178 VVSEEELRLILSESYKKGQINQSefryvnkIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDK 257
Cdd:TIGR03520 161 LSQALELTDEEDTTKEEQKILQG-------IVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  258 DHILGIINNKDLFkAYFLGRSIELKEMMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGE 337
Cdd:TIGR03520 234 DNITGVLYIKDLL-PHLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGD 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  338 IRDEYDQDEMPHiVKKGEHHYVMDGKALIEEVNDLLDiaIENEDID-------TIAGWLLTQKMEL-KNGDVFHAEGCEF 409
Cdd:TIGR03520 313 ISDEFDDEDLIY-SKIDDNNYVFEGKTSLKDFYKILK--LEEDMFDevkgeaeTLAGFLLEISGGFpKKGEKITFENFEF 389

                         330
                  ....*....|....*..
gi 647576056  410 KVLEAEDHHIRFVEIKK 426
Cdd:TIGR03520 390 TIEAMDKKRIKQVKVTI 406
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 351-426 8.86e-18

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: 77.48  E-value: 8.86e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647576056   351 VKKGEHHYVMDGKALIEEVNDLLDIAIENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLEAEDHHIRFVEIKK 426
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIpEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 16-428 1.36e-171

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 487.70  E-value: 1.36e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  16 TAIFVAAEFAIVKIRGSKIAELVETGDSRALAAHRVISNLDEYLSACQLGITITALGLGWLGEPTIQRLLHPVFSLIGMP 95
Cdd:COG1253   17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  96 SSITHVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFHSVKEH 175
Cdd:COG1253   97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 176 EVVVSEEeLRLILSESYKKGQINQSEFRYVNKIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKE 255
Cdd:COG1253  177 PAVTEEE-LRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 256 DKDHILGIINNKDLFKAYFLGRSIELKEMMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIV 335
Cdd:COG1253  256 DLDDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIV 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 336 GEIRDEYDQDEmPHIVKKGEHHYVMDGKALIEEVNDLLDIAI-ENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLE 413
Cdd:COG1253  336 GEIRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIpEVGETVEVDGLRFEVLD 414

                        410
                 ....*....|....*
gi 647576056 414 AEDHHIRFVEIKKTD 428
Cdd:COG1253  415 MDGRRIDKVLVTRLP 429
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 17-426 1.66e-83

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: 261.93  E-value: 1.66e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  17 AIFVAAEFAIVKIRGSKIAELVETGDSRALAAHRVISNLDEYLSACQLGITI---------TALGLGWLGEPTIqrllhp 87
Cdd:COG4536   21 AFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLvnilasslaTVIAIRLFGDAGV------ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  88 vfsligmpssithvvtfIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLF 167
Cdd:COG4536   95 -----------------AIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 168 GFHSVKEHEVVVSEEELRLILSESYKKGQINQSEFRYVNKIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERY 247
Cdd:COG4536  158 GVKPDADASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 248 TRYPVIKEDKDHILGIINNKDLFKAYFLGR--SIELKEMMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLV 325
Cdd:COG4536  238 TRLPVYRGDIDNIVGVLHVRDLLRALRKGDlsKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLV 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 326 TVEDILEEIVGEIRDEYDQDEmPHIVKKGEHHYVMDGKALIEEVNDLLDIAIENEDIDTIAGWLLtqkMEL----KNGDV 401
Cdd:COG4536  318 TLEDILEEIVGEITDEHDPDA-EEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLII---EELedipEAGQS 393

                        410       420
                 ....*....|....*....|....*
gi 647576056 402 FHAEGCEFKVLEAEDHHIRFVEIKK 426
Cdd:COG4536  394 FTIHGYRFEILQVQDNRIKTVRIRP 418
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 216-428 1.85e-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: 206.12  E-value: 1.85e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 216 AREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDHILGIINNKDLFKAYFLGR-SIELKEMMRPVIRVIES 294
Cdd:COG4535   65 VRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAeEFDLRDLLRPAVFVPES 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 295 IPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDEYDQDEMP-HIVKKGEHHYVMDGKALIEEVNDLL 373
Cdd:COG4535  145 KRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIEDEHDEDEDEdNIRPLSDGSYRVKALTPIEDFNEYF 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 647576056 374 DIAIENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLEAEDHHIRFVEIKKTD 428
Cdd:COG4535  225 GTDFSDEEFDTIGGLVAQEFGHLpKRGESIEIDGLRFKVLRADSRRIHLLRVTRLP 280
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 215-332 2.57e-48

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: 160.74  E-value: 2.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 215 VAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDHILGIINNKDLFKAYFLGR-SIELKEMMRPVIRVIE 293
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGReKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 647576056 294 SIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILE 332
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
212-428 1.06e-45

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 159.97  E-value: 1.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 212 DNRVaREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDHILGIINNKDLFKayFLGRSIE---LKEMMRPV 288
Cdd:PRK15094  66 DQRV-RDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLP--FMRSDAEafsMDKVLRQA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 289 IRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDEYDQDEMPHIVKKGEHHYVMDGKALIEE 368
Cdd:PRK15094 143 VVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIED 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647576056 369 VNDLLDIAIENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLEAEDHHIRFVEIKKTD 428
Cdd:PRK15094 223 FNEAFGTHFSDEEVDTIGGLVMQAFGHLpARGETIDIDGYQFKVAMADSRRIIQVHVKIPD 283
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 17-201 1.12e-42

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: 148.13  E-value: 1.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056   17 AIFVAAEFAIVKIRGSKIAELVETGDSRALAAHRVISNLDEYLSACQLGITITALGLGWLGEPTIQRLLHPVfsligmps 96
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056   97 sitHVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFhSVKEHE 176
Cdd:pfam01595  83 ---GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGV-KGGESE 158

                         170       180
                  ....*....|....*....|....*
gi 647576056  177 VVVSEEELRLILSESYKKGQINQSE 201
Cdd:pfam01595 159 PAVTEEELRSLVEESAEEGVIEEEE 183
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 99-426 2.84e-42

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: 153.66  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056   99 THVVTFIAAFIAVTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFH-SVKEHEV 177
Cdd:TIGR03520  81 TELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQkSNISVDQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  178 VVSEEELRLILSESYKKGQINQSefryvnkIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDK 257
Cdd:TIGR03520 161 LSQALELTDEEDTTKEEQKILQG-------IVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  258 DHILGIINNKDLFkAYFLGRSIELKEMMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGE 337
Cdd:TIGR03520 234 DNITGVLYIKDLL-PHLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGD 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  338 IRDEYDQDEMPHiVKKGEHHYVMDGKALIEEVNDLLDiaIENEDID-------TIAGWLLTQKMEL-KNGDVFHAEGCEF 409
Cdd:TIGR03520 313 ISDEFDDEDLIY-SKIDDNNYVFEGKTSLKDFYKILK--LEEDMFDevkgeaeTLAGFLLEISGGFpKKGEKITFENFEF 389

                         330
                  ....*....|....*..
gi 647576056  410 KVLEAEDHHIRFVEIKK 426
Cdd:TIGR03520 390 TIEAMDKKRIKQVKVTI 406
PRK11573 PRK11573
hypothetical protein; Provisional
 111-425 1.58e-23

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 101.75  E-value: 1.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 111 VTYLHVVIGELAPKTISIQKAEAVSLWTAKPLILFYKVMYPFIKLLNGSAGFLVKLFGFHSVKEHEVVVSEEELRLILSE 190
Cdd:PRK11573  86 LTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTDIVVSGALSKEELRTIVHE 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 191 SykKGQINQSEFRYVNKIFEFDNRVAREIMVPRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDHILGIINNKDLF 270
Cdd:PRK11573 166 S--RSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLRVREAY 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 271 KAYFLGRSIELKEMMRP---VIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDEYDQDEM 347
Cdd:PRK11573 244 RLMTEKKEFTKENMLRAadeIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTSMSPTLA 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647576056 348 PHIVKKGEHHYVMDGKALIEEVNDLLDIAIENEDIDTIAGWLLTQKMELKNGDV-FHAEGCEFKVLEAEDHHIRFVEIK 425
Cdd:PRK11573 324 EEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTrVRIGEYDIDILDVQDNMIKQVKVT 402
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 351-426 8.86e-18

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: 77.48  E-value: 8.86e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647576056   351 VKKGEHHYVMDGKALIEEVNDLLDIAIENEDIDTIAGWLLTQKMEL-KNGDVFHAEGCEFKVLEAEDHHIRFVEIKK 426
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIpEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 351-428 2.56e-16

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: 73.35  E-value: 2.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  351 VKKGEHHYVMDGKALIEEVNDLLDIAIENEDIDTIAGWLLTQKMEL-KNGDVF--HAEGCEFKVLEAEDHHIRFVEIKKT 427
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIpKVGDKVevELGGLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 647576056  428 D 428
Cdd:pfam03471  81 E 81
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
216-334 2.57e-13

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 68.37  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 216 AREIMVPRteIAAISLEQSVDEAIHLIINERYTRYPVIkeDKDHILGIINNKDLFKAYFLGRSIE---LKEMM-RPVIRV 291
Cdd:COG2524   88 VKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPVV--DDGKLVGIITERDLLKALAEGRDLLdapVSDIMtRDVVTV 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 647576056 292 IESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEI 334
Cdd:COG2524  164 SEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
215-341 3.05e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 66.43  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 215 VAREIMVprTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDkDHILGIINNKDLFKAYFLGRSIELKE----------M 284
Cdd:COG3448    3 TVRDIMT--RDVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLPDRLDELEErlldlpvedvM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 647576056 285 MRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDE 341
Cdd:COG3448   80 TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 223-331 2.63e-12

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: 63.03  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 223 RTEIAAISLEQSVDEAIHLIINERYTRYPVIkEDKDHILGIINNKDLFKAYFLGRSIELKE----MMRPVIRVIESIPVQ 298
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVV-DDDGKLVGIVTERDILRALVEGGLALDTPvaevMTPDVITVSPDTDLE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 647576056 299 ELLIRMQKERIHMAILVDEYGGTAGLVTVEDIL 331
Cdd:cd02205   80 EALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
CBS COG0517
CBS domain [Signal transduction mechanisms];
216-339 1.39e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 61.42  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 216 AREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDkDHILGIINNKDL-FKAYFLGRSIE---LKEMM-RPVIR 290
Cdd:COG0517    3 VKDIM--TTDVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLrRALAAEGKDLLdtpVSEVMtRPPVT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 647576056 291 VIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIR 339
Cdd:COG0517   80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
217-332 9.05e-11

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 59.54  E-value: 9.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 217 REIMVpRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKdHILGIINNKDLFKAyflGRSIELKEMM-RPVIRVIESI 295
Cdd:COG4109   19 EDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGK---DDDTPIEDVMtKNPITVTPDT 93

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 647576056 296 PVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILE 332
Cdd:COG4109   94 SLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 216-331 1.03e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 53.29  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 216 AREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDkDHILGIINNKDLFKAYFLG----RSIELKEMM-RPVIR 290
Cdd:COG2905    1 VKDIM--SRDVVTVSPDATVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLRRRVLAEgldpLDTPVSEVMtRPPIT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 647576056 291 VIESIPVQELLIRMQKERIHMAILVDEyGGTAGLVTVEDIL 331
Cdd:COG2905   78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 215-330 1.40e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. 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: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 52.63  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 215 VAREIMVprTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKDhILGIINNKDLFKAYFLGrSIELKEMM-RPVIRVIE 293
Cdd:cd04605    1 LVEDIMS--KDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGK-LIGIVTSWDISKAVALK-KDSLEEIMtRNVITARP 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 647576056 294 SIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDI 330
Cdd:cd04605   77 DEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 229-331 1.35e-06

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 50.46  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056  229 ISLEQSVDEAIHLIINERYTRYPVIkeDKDHILGIINNKDL-FKAYFlgrSIELKEMM--RPVIRVIESIPVQELLIRMQ 305
Cdd:pfam00478  93 LSPDATVADALALMERYGISGVPVV--DDGKLVGIVTNRDLrFETDL---SQPVSEVMtkENLVTAPEGTTLEEAKEILH 167

                          90       100
                  ....*....|....*....|....*.
gi 647576056  306 KERIHMAILVDEYGGTAGLVTVEDIL 331
Cdd:pfam00478 168 KHKIEKLPVVDDNGRLVGLITIKDIE 193
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 228-333 3.31e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 45.60  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 228 AISLEQSVDEAIHLIINERYTRYPVIkeDKDHILGIINNKDLFKAYFLGR-SIELKEMMRP-VIRVIESIPVQELLIRMQ 305
Cdd:cd04588    6 TLKPDATIKDAAKLLSENNIHGAPVV--DDGKLVGIVTLTDIAKALAEGKeNAKVKDIMTKdVITIDKDEKIYDAIRLMN 83

                         90       100
                 ....*....|....*....|....*...
gi 647576056 306 KERIHMAILVDEYGGTAGLVTVEDILEE 333
Cdd:cd04588   84 KHNIGRLIVVDDNGKPVGIITRTDILKV 111
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 284-336 4.34e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.74  E-value: 4.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 647576056  284 MMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVG 336
Cdd:pfam00571   5 MTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 216-331 5.43e-06

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: 45.40  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 216 AREIMVprTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKdhILGIINNKDLFKaYFLGR---------------SIE 280
Cdd:cd17778    2 VKEFMT--TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK--LVGIVTAMDIVK-YFGSHeakkrlttgdideaySTP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 647576056 281 LKEMM-RPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDIL 331
Cdd:cd17778   77 VEEIMsKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 216-272 6.68e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.36  E-value: 6.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 647576056  216 AREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDkDHILGIINNKDLFKA 272
Cdd:pfam00571   1 VKDIM--TKDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRA 54
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
212-273 8.61e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 44.90  E-value: 8.61e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647576056 212 DNRVAREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIkEDKDHILGIINNKDLFKAY 273
Cdd:COG4109   74 DDTPIEDVM--TKNPITVTPDTSLASAAHKMIWEGIELLPVV-DDDGRLLGIISRQDVLKAL 132
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 223-334 1.13e-05

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 44.46  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 223 RTEIAAISLEQSVDEAIHLIInERYTRYPVIKEDKDHILGIINNKDLFKAyFLGRSIELKE------MMRPVIRVIESIP 296
Cdd:cd17775    2 RREVVTASPDTSVLEAARLMR-DHHVGSVVVVEEDGKPVGIVTDRDIVVE-VVAKGLDPKDvtvgdiMSADLITAREDDG 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 647576056 297 VQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEI 334
Cdd:cd17775   80 LFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 252-334 1.59e-05

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 43.67  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 252 VIKEDKDHILGIINNKDLFKAYFLGRSIELKE---MMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVE 328
Cdd:cd09836   30 VVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVeeiMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIR 109


                 ....*.
gi 647576056 329 DILEEI 334
Cdd:cd09836  110 DLAREL 115
CBS COG0517
CBS domain [Signal transduction mechanisms];
210-273 4.38e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 42.93  E-value: 4.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647576056 210 EFDNRVAREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIkEDKDHILGIINNKDLFKAY 273
Cdd:COG0517   63 DLLDTPVSEVM--TRPPVTVSPDTSLEEAAELMEEHKIRRLPVV-DDDGRLVGIITIKDLLKAL 123
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 284-344 5.56e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.51  E-value: 5.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647576056 284 MMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDEYDQ 344
Cdd:COG2905    5 MSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDT 65
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 217-331 6.54e-05

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: 42.41  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 217 REIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIkeDKDHILGIINNKDLFKA-------------YFLGRSIELKE 283
Cdd:cd04584    3 KDIM--TKNVVTVTPDTSLAEARELMKEHKIRHLPVV--DDGKLVGIVTDRDLLRAspskatslsiyelNYLLSKIPVKD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 647576056 284 MM-RPVIRVIESIPVQELLIRMQKERIHMAILVDEyGGTAGLVTVEDIL 331
Cdd:cd04584   79 IMtKDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDIL 126
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 229-331 1.38e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 40.86  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 229 ISLEQSVDEAIHLIINERYTRYPVIkEDKDHILGIINNKDL-FKAyflGRSIELKEMMRPVIRVI---ESIPVQELLIRM 304
Cdd:cd04601    7 LSPDATVADVLELKAEYGISGVPVT-EDGGKLVGIVTSRDIrFET---DLSTPVSEVMTPDERLVtapEGITLEEAKEIL 82

                         90       100
                 ....*....|....*....|....*..
gi 647576056 305 QKERIHMAILVDEYGGTAGLVTVEDIL 331
Cdd:cd04601   83 HKHKIEKLPIVDDNGELVGLITRKDIE 109
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 218-331 2.14e-04

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: 40.63  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 218 EIMVPrtEIAAISLEQSVDEAIHLIINERYTRYPVIkeDKDHILGIINNKDLFKAYFLGRSIELKE--MMRPVIRVIESI 295
Cdd:cd04801    1 DIMTP--EVVTVTPEMTVSELLDRMFEEKHLGYPVV--ENGRLVGIVTLEDIRKVPEVEREATRVRdvMTKDVITVSPDA 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 647576056 296 PVQELLIRMQKERIHMAILVDEyGGTAGLVTVEDIL 331
Cdd:cd04801   77 DAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 203-273 7.16e-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: 7.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647576056 203 RYVNKIFEFDNRVAREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIkeDKDHILGIINNKDLFKAY 273
Cdd:COG2905   54 RVLAEGLDPLDTPVSEVM--TRPPITVSPDDSLAEALELMEEHRIRHLPVV--DDGKLVGIVSITDLLRAL 120
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 223-332 7.94e-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: 38.96  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 223 RTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKdHILGIINNKDLFKA-----YFLGRSIELKEMMRP-VIRVIESIP 296
Cdd:cd04629    2 TRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQG-RLVGFLSEQDCLKAlleasYHCEPGGTVADYMSTeVLTVSPDTS 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 647576056 297 VQELLIRMQKERIHMAILVDEyGGTAGLVTVEDILE 332
Cdd:cd04629   81 IVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLR 115
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 212-271 8.36e-04

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 38.76  E-value: 8.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 212 DNRVAREIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIkEDKDHILGIINNKDLFK 271
Cdd:cd02205   57 LDTPVAEVM--TPDVITVSPDTDLEEALELMLEHGIRRLPVV-DDDGKLVGIVTRRDILR 113
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
284-352 8.65e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 8.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647576056 284 MMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEEIVGEIRDEYDQDEMPHIVK 352
Cdd:COG3448    8 MTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVE 76
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 217-272 1.67e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 38.19  E-value: 1.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 647576056 217 REIMvpRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDKdhILGIINNKDLFKA 272
Cdd:cd04629   65 ADYM--STEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGK--LVGQISRRDVLRA 116
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 220-332 2.09e-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: 37.94  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 220 MVPRTEI--AAISLEQSVDEAIhlIINERYTRYPVIKEDkDHILGIINNKDLFKA-YFLGRSIELKEMMRPV---IRVIE 293
Cdd:cd04639    3 MVTEFPIvdADLTLREFADDYL--IGKKSWREFLVTDEA-GRLVGLITVDDLRAIpTSQWPDTPVRELMKPLeeiPTVAA 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 647576056 294 SIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILE 332
Cdd:cd04639   80 DQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIE 118
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 229-332 4.12e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. 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: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 36.71  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 229 ISLEQSVDEAIHLIINERYTRYPVIKEDKdhILGIINNKDLFKAYFLGRS-IELKEMM-RPVIRVIESIP---VQELLIR 303
Cdd:cd04595    7 VSPDTTIEEARKIMLRYGHTGLPVVEDGK--LVGIISRRDVDKAKHHGLGhAPVKGYMsTNVITIDPDTSleeAQELMVE 84

                         90       100
                 ....*....|....*....|....*....
gi 647576056 304 MQKERihmaILVDEYGGTAGLVTVEDILE 332
Cdd:cd04595   85 HDIGR----LPVVEEGKLVGIVTRSDVLR 109
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 222-303 4.84e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 37.45  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 222 PRTEIAAISLEQSVDEAIHLIINERYTRYPVIKEDkDHILGIINNKDLFKAYFLGRSIELKEMMRPVIRVIESIP-VQEL 300
Cdd:cd17789    1 PKGKLHVVKPNTTVDEALELLVENRITGLPVIDED-WRLVGVVSDYDLLALDSISGRSQTDNNFPPADSTWKTFNeVQKL 79


                 ...
gi 647576056 301 LIR 303
Cdd:cd17789   80 LSK 82
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 284-330 5.31e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 36.96  E-value: 5.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 647576056 284 MMRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDI 330
Cdd:cd04592    1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDI 47
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 285-333 9.15e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in proteobacteria; 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: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 36.39  E-value: 9.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 647576056 285 MRPVIRVIESIPVQELLIRMQKERIHMAILVDEYGGTAGLVTVEDILEE 333
Cdd:cd04640    4 RVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGE 52
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 228-331 9.92e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. 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: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 35.62  E-value: 9.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647576056 228 AISLEQSVDEAihliiNERYTRY-----PVIKEDKDHILGIINNKDLFKAYFLGRS-IELKEMMRPVIRVIES----IPV 297
Cdd:cd17772    6 SVEPDTTIAEA-----AELMTRYninalPVVDGGTGRLVGIITRQVAEKAIYHGLGdLPVSEYMTTEFATVTPdaplSEI 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 647576056 298 QELLIRmQKERIhmaILVDEYGGTAGLVTVEDIL 331
Cdd:cd17772   81 QEIIVE-QRQRL---VPVVEDGRLVGVITRTDLL 110
 
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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