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Conserved domains on  [gi|1087496578|emb|SDC07391|]
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Hemolysin, contains CBS domains [Paenibacillus sp. cl123]

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 ...
 35-452 5.82e-169

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 482.31  E-value: 5.82e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  35 GFFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASLGLGWVGEPAISHLIvEPLFGLMGLG 114
Cdd:COG1253    18 GFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALL-APLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 115 HAwYADALSIAIGFAVITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIHPATE 194
Cdd:COG1253    97 AA-LAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 195 HEAAHTEEeIRILMDESARSGHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVAT 274
Cdd:COG1253   176 EPAVTEEE-LRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 275 HDKDEIIGFVHITDMLTA--KGAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEI 352
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRAllEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEI 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 353 VGEIHDEFDvTERPEIEKVGEG-YSVDGRVLLEDLDDMLGLGI-EDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEIT 430
Cdd:COG1253   335 VGEIRDEYD-EEEPEIVKLDDGsYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVL 413

                         410       420
                  ....*....|....*....|..
gi 1087496578 431 EVDRLRVMRLTIHQLPAAPEPE 452
Cdd:COG1253   414 DMDGRRIDKVLVTRLPEEEEEE 435
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 35-452 5.82e-169

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 482.31  E-value: 5.82e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  35 GFFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASLGLGWVGEPAISHLIvEPLFGLMGLG 114
Cdd:COG1253    18 GFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALL-APLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 115 HAwYADALSIAIGFAVITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIHPATE 194
Cdd:COG1253    97 AA-LAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 195 HEAAHTEEeIRILMDESARSGHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVAT 274
Cdd:COG1253   176 EPAVTEEE-LRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 275 HDKDEIIGFVHITDMLTA--KGAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEI 352
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRAllEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEI 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 353 VGEIHDEFDvTERPEIEKVGEG-YSVDGRVLLEDLDDMLGLGI-EDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEIT 430
Cdd:COG1253   335 VGEIRDEYD-EEEPEIVKLDDGsYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVL 413

                         410       420
                  ....*....|....*....|..
gi 1087496578 431 EVDRLRVMRLTIHQLPAAPEPE 452
Cdd:COG1253   414 DMDGRRIDKVLVTRLPEEEEEE 435
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 35-221 1.12e-45

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: 156.99  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  35 GFFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASLGLGWVGEPAISHLIVEPlfglmglg 114
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 115 hawyaDALSIAIGFAVITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIhPATE 194
Cdd:pfam01595  83 -----GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGV-KGGE 156

                         170       180
                  ....*....|....*....|....*..
gi 1087496578 195 HEAAHTEEEIRILMDESARSGHIDQDE 221
Cdd:pfam01595 157 SEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 235-350 1.79e-42

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: 146.10  E-value: 1.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 235 VAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHITDMLTAKGAQQ---DLKRFVRPVLMVPE 311
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGReklDLRALLRPPLFVPE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1087496578 312 SMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILE 350
Cdd:cd04590    81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
207-452 6.48e-41

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 147.65  E-value: 6.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 207 LMDESARSGHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHI 286
Cdd:PRK15094   40 LIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 287 TDML---TAKGAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVT 363
Cdd:PRK15094  120 KDLLpfmRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 364 ERPEIEKVG-EGYSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEITEVDRLRVMRLTI 442
Cdd:PRK15094  200 DDIDFRQLSrHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHV 279

                         250
                  ....*....|
gi 1087496578 443 HQLPAAPEPE 452
Cdd:PRK15094  280 KIPDDSPQPK 289
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 130-443 1.93e-37

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: 141.33  E-value: 1.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 130 VITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGI--HPATEHEAAHTEEeiriL 207
Cdd:TIGR03520  92 IVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKqkSNISVDQLSQALE----L 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 208 MDESARSghidQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHIT 287
Cdd:TIGR03520 168 TDEEDTT----KEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNITGVLYIK 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 288 DMLTAKGAQQ-DLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVTERP 366
Cdd:TIGR03520 244 DLLPHLNKKNfDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFDDEDLI 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 367 EIEKVGEGYSVDGRVLLEDLDDMLGLgiEDE-------EVDSIGGWLFKQLEGSVDKGQQLVHERFVLEITEVD--RLRV 437
Cdd:TIGR03520 324 YSKIDDNNYVFEGKTSLKDFYKILKL--EEDmfdevkgEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDkkRIKQ 401


                  ....*.
gi 1087496578 438 MRLTIH 443
Cdd:TIGR03520 402 VKVTIN 407
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 369-443 4.04e-14

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: 67.08  E-value: 4.04e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087496578  369 EKVGEG-YSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEITEVDRLRVMRLTIH 443
Cdd:smart01091   1 VKLDDGsYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 35-452 5.82e-169

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 482.31  E-value: 5.82e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  35 GFFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASLGLGWVGEPAISHLIvEPLFGLMGLG 114
Cdd:COG1253    18 GFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALL-APLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 115 HAwYADALSIAIGFAVITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIHPATE 194
Cdd:COG1253    97 AA-LAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 195 HEAAHTEEeIRILMDESARSGHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVAT 274
Cdd:COG1253   176 EPAVTEEE-LRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 275 HDKDEIIGFVHITDMLTA--KGAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEI 352
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRAllEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEI 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 353 VGEIHDEFDvTERPEIEKVGEG-YSVDGRVLLEDLDDMLGLGI-EDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEIT 430
Cdd:COG1253   335 VGEIRDEYD-EEEPEIVKLDDGsYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVL 413

                         410       420
                  ....*....|....*....|..
gi 1087496578 431 EVDRLRVMRLTIHQLPAAPEPE 452
Cdd:COG1253   414 DMDGRRIDKVLVTRLPEEEEEE 435
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 35-446 4.18e-91

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: 282.74  E-value: 4.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  35 GFFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASlglgwVGEPAISHLIVEPLFGLMGlg 114
Cdd:COG4536    21 AFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVN-----ILASSLATVIAIRLFGDAG-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 115 hawyadalsIAIGFAVITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIHPATE 194
Cdd:COG4536    94 ---------VAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPDAD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 195 HEAAHTEEEIRILMDESARSGHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVAT 274
Cdd:COG4536   165 ASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 275 HDKDEIIGFVHITDMLTAKGAQQ----DLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILE 350
Cdd:COG4536   245 GDIDNIVGVLHVRDLLRALRKGDlskeDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 351 EIVGEIHDEFDVTErPEIEKVGEG-YSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEI 429
Cdd:COG4536   325 EIVGEITDEHDPDA-EEIRPQEDGsYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEI 403

                         410
                  ....*....|....*..
gi 1087496578 430 TEVDRLRVMRLTIHQLP 446
Cdd:COG4536   404 LQVQDNRIKTVRIRPLP 420
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 217-452 3.01e-60

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: 198.41  E-value: 3.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 217 IDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHITDML---TAK 293
Cdd:COG4535    46 IDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLrylAQD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 294 GAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVTERPE-IEKVG 372
Cdd:COG4535   126 AEEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIEDEHDEDEDEDnIRPLS 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 373 EG-YSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLeGSV-DKGQQLVHERFVLEITEVD--RLRVMRLTIHQLPAA 448
Cdd:COG4535   206 DGsYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEF-GHLpKRGESIEIDGLRFKVLRADsrRIHLLRVTRLPPAAE 284


                  ....
gi 1087496578 449 PEPE 452
Cdd:COG4535   285 PDAE 288
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 35-221 1.12e-45

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: 156.99  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  35 GFFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASLGLGWVGEPAISHLIVEPlfglmglg 114
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 115 hawyaDALSIAIGFAVITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIhPATE 194
Cdd:pfam01595  83 -----GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGV-KGGE 156

                         170       180
                  ....*....|....*....|....*..
gi 1087496578 195 HEAAHTEEEIRILMDESARSGHIDQDE 221
Cdd:pfam01595 157 SEPAVTEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 235-350 1.79e-42

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: 146.10  E-value: 1.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 235 VAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHITDMLTAKGAQQ---DLKRFVRPVLMVPE 311
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGReklDLRALLRPPLFVPE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1087496578 312 SMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILE 350
Cdd:cd04590    81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
207-452 6.48e-41

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 147.65  E-value: 6.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 207 LMDESARSGHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHI 286
Cdd:PRK15094   40 LIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 287 TDML---TAKGAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVT 363
Cdd:PRK15094  120 KDLLpfmRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 364 ERPEIEKVG-EGYSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEITEVDRLRVMRLTI 442
Cdd:PRK15094  200 DDIDFRQLSrHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHV 279

                         250
                  ....*....|
gi 1087496578 443 HQLPAAPEPE 452
Cdd:PRK15094  280 KIPDDSPQPK 289
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 130-443 1.93e-37

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: 141.33  E-value: 1.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 130 VITFLHIVLGELAPKSLAIQKSEMTSLWLSAPLMFFYKLFFPVIWLLNGAANRLLRLVGI--HPATEHEAAHTEEeiriL 207
Cdd:TIGR03520  92 IVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKqkSNISVDQLSQALE----L 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 208 MDESARSghidQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKDEIIGFVHIT 287
Cdd:TIGR03520 168 TDEEDTT----KEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNITGVLYIK 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 288 DMLTAKGAQQ-DLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVTERP 366
Cdd:TIGR03520 244 DLLPHLNKKNfDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFDDEDLI 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 367 EIEKVGEGYSVDGRVLLEDLDDMLGLgiEDE-------EVDSIGGWLFKQLEGSVDKGQQLVHERFVLEITEVD--RLRV 437
Cdd:TIGR03520 324 YSKIDDNNYVFEGKTSLKDFYKILKL--EEDmfdevkgEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDkkRIKQ 401


                  ....*.
gi 1087496578 438 MRLTIH 443
Cdd:TIGR03520 402 VKVTIN 407
PRK11573 PRK11573
hypothetical protein; Provisional
 36-432 1.60e-23

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 102.14  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578  36 FFVAAEFSLVKVRQTRLQQLESEGNGKARYALAVTKKLDAYLSSTQLGITLASlglgwvgepaishlIVEPLFGLMgLGH 115
Cdd:PRK11573    7 YFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVN--------------ILASALGTI-VGM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 116 AWYADAlSIAIGFAVITFLHIVLGELAPKSLAI---QKSEMTSLWLSAPLMffyKLFFPVIWLLNGAANRLLRLVGIHPA 192
Cdd:PRK11573   72 RLYGDA-GVAIATGVLTFVVLVFAEVLPKTIAAlypEKVAYPSSFLLAPLQ---ILMMPLVWLLNTITRLLMRLMGIKTD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 193 TEHEAAHTEEEIRILMDESaRSgHIDQDEMALFDNIFEFSERVAREIMLPRTDMDCLFTELSFEDNLNIVYETKHTRYPV 272
Cdd:PRK11573  148 IVVSGALSKEELRTIVHES-RS-QISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 273 ATHDKDEIIGFVHITD---MLTAKGA--QQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAED 347
Cdd:PRK11573  226 YRDSLDDAISMLRVREayrLMTEKKEftKENMLRAADEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVED 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 348 ILEEIVGEIHDEFDVTERPEIEKVGEGYS-VDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHERFV 426
Cdd:PRK11573  306 ILEEIVGDFTTSMSPTLAEEVTPQNDGSViIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYD 385


                  ....*.
gi 1087496578 427 LEITEV 432
Cdd:PRK11573  386 IDILDV 391
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 369-443 4.04e-14

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: 67.08  E-value: 4.04e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1087496578  369 EKVGEG-YSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHERFVLEITEVDRLRVMRLTIH 443
Cdd:smart01091   1 VKLDDGsYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 369-446 4.45e-13

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


Pssm-ID: 460935 [Multi-domain]  Cd Length: 81  Bit Score: 64.49  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 369 EKVGEG-YSVDGRVLLEDLDDMLGLGIEDEEVDSIGGWLFKQLEGSVDKGQQLVHER--FVLEITEVDRLRVMRLTIHQL 445
Cdd:pfam03471   1 EKLDDGsYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKVEVELggLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 1087496578 446 P 446
Cdd:pfam03471  81 E 81
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
230-350 1.14e-09

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 56.46  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 230 EFSERV-AREIMLpRTDMDCLFTELSFEDNLNIVYETKHTRYPVaTHDKDEIIGFVHITDMLTAKGAQQDLKRFVRPVLM 308
Cdd:COG4109    11 TFKEILlVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPV-VDENGRLVGIVTSKDILGKDDDTPIEDVMTKNPIT 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1087496578 309 VPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILE 350
Cdd:COG4109    89 VTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
158-352 4.90e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 53.35  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 158 LSAPLMFFYKLFFPVIWLLNGAANRLLRLVGIHPATEHEAAHTEEEIRILMDESARSGHIDQDEMALFDNIFEFSERVaR 237
Cdd:COG2524    11 LLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKV-K 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 238 EIMlpRTDMDCLFTELSFEDNLNIVYETKHTRYPVAthDKDEIIGFVHITDMLTAKGAQQDLKRF------VRPVLMVPE 311
Cdd:COG2524    90 DIM--TKDVITVSPDTTLEEALELMLEKGISGLPVV--DDGKLVGIITERDLLKALAEGRDLLDApvsdimTRDVVTVSE 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1087496578 312 SMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEI 352
Cdd:COG2524   166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 259-349 5.39e-07

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: 48.01  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 259 LNIVYETKHTRYPVaTHDKDEIIGFVHITDMLTAKGAQQDLKRFV------RPVLMVPESMEISHVLRMMQKKRSQLAIV 332
Cdd:cd02205    17 LELMAENGIGALPV-VDDDGKLVGIVTERDILRALVEGGLALDTPvaevmtPDVITVSPDTDLEEALELMLEHGIRRLPV 95

                          90
                  ....*....|....*..
gi 1087496578 333 IDEYGGTAGLITAEDIL 349
Cdd:cd02205    96 VDDDGKLVGIVTRRDIL 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 304-354 2.72e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.51  E-value: 2.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1087496578 304 RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVG 354
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 298-351 1.02e-05

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: 44.86  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1087496578 298 DLKRFvrPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEE 351
Cdd:cd04640     1 DFRRV--PPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGE 52
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 254-350 1.08e-05

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: 44.48  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 254 SFEDNLnIVYETKHTRYPVATHDkDEIIGFVHITDM---LTAKGAQQDLKRFVRPVLMVP---ESMEISHVLRMMQKKRS 327
Cdd:cd04639    18 EFADDY-LIGKKSWREFLVTDEA-GRLVGLITVDDLraiPTSQWPDTPVRELMKPLEEIPtvaADQSLLEVVKLLEEQQL 95

                          90       100
                  ....*....|....*....|...
gi 1087496578 328 QLAIVIDEYGGTAGLITAEDILE 350
Cdd:cd04639    96 PALAVVSENGTLVGLIEKEDIIE 118
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 305-355 4.39e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. 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: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 42.57  E-value: 4.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1087496578 305 PVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGE 355
Cdd:cd17781     3 PALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVAS 53
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 236-351 1.78e-04

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: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 40.97  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 236 AREIMlpRTDMDCLFTELSFEDNLNIVYETKHTRYPVATHDKD-EIIGFVHITDMLTAKGAqqDLKRFVRPV-LMVPESM 313
Cdd:cd04591     2 AEDVM--RPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESqTLVGFILRSQLILLLEA--DLRPIMDPSpFTVTEET 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1087496578 314 EISHVLRMMQKKRSQLAIVIDeYGGTAGLITAEDILEE 351
Cdd:cd04591    78 SLEKVHDLFRLLGLRHLLVTN-NGRLVGIVTRKDLLRA 114
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 256-350 1.85e-04

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: 40.53  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 256 EDNLNIVYETKHTRYPVaTHDKDEIIGFVHITDMLTAKGAQQDLKRFVRPVLMVPESMEISHVLRMMQKKRSQLAIVIDE 335
Cdd:cd04596    14 RDYKQLSEETGHSRFPV-VDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDE 92

                          90
                  ....*....|....*
gi 1087496578 336 YGGTAGLITAEDILE 350
Cdd:cd04596    93 NRKLLGVISRQDVLK 107
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 304-355 2.21e-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: 40.69  E-value: 2.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1087496578 304 RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGE 355
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG 53
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 304-363 4.24e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 40.20  E-value: 4.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 304 RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVT 363
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTP 66
CBS COG0517
CBS domain [Signal transduction mechanisms];
236-355 4.45e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.23  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 236 AREIMlpRTDMDCLFTELSFEDNLNIVYETKHTRYPVaTHDKDEIIGFVHITDML--TAKGAQQDLKRFV-----RPVLM 308
Cdd:COG0517     3 VKDIM--TTDVVTVSPDATVREALELMSEKRIGGLPV-VDEDGKLVGIVTDRDLRraLAAEGKDLLDTPVsevmtRPPVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1087496578 309 VPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGE 355
Cdd:COG0517    80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEP 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
235-359 5.46e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 235 VAREIMlpRTDMDCLFTELSFEDNLNIVYETKHTRYPVaTHDKDEIIGFVHITDMLTA-------KGAQQDLKRFV---- 303
Cdd:COG3448     3 TVRDIM--TRDVVTVSPDTTLREALELMREHGIRGLPV-VDEDGRLVGIVTERDLLRAllpdrldELEERLLDLPVedvm 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1087496578 304 -RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDE 359
Cdd:COG3448    80 tRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 238-349 5.72e-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: 39.47  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 238 EIMLPrtDMDCLFTELSFEDNLNIVYETKHTRYPVAthDKDEIIGFVHITDMLTAKGAQQDLKR----FVRPVLMVPESM 313
Cdd:cd04801     1 DIMTP--EVVTVTPEMTVSELLDRMFEEKHLGYPVV--ENGRLVGIVTLEDIRKVPEVEREATRvrdvMTKDVITVSPDA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1087496578 314 EISHVLRMMQKKRSQLAIVIDEyGGTAGLITAEDIL 349
Cdd:cd04801    77 DAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
304-363 2.37e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 37.92  E-value: 2.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 304 RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVT 363
Cdd:COG0517     9 TDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTP 68
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
304-373 2.48e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.92  E-value: 2.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087496578 304 RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEIVGEIHDEFDVTERPeiEKVGE 373
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLD--LPVED 77
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 304-352 6.78e-03

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 36.37  E-value: 6.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1087496578 304 RPVLMVPESMEISHVLRMMQKKRSQLAIVIDEYGGTAGLITAEDILEEI 352
Cdd:cd17775    69 ADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
 
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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