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Conserved domains on  [gi|942070976|ref|WP_055285343|]
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MULTISPECIES: hemolysin family protein [Collinsella]

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 ...
 1-434 2.97e-175

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 498.11  E-value: 2.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   1 MDITISLITTLVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAVAST 80
Cdd:COG1253    1 MSLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  81 SLSDPLATWLMSFGIAPlsAIARGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTG 160
Cdd:COG1253   81 ALAALLAPLLGSLGLPA--ALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 161 ACSDGLARILRIKSADDRQNVSEEEIKYMVS---EQDDLLDEEKRMIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADV 237
Cdd:COG1253  159 GSTNLLLRLLGIEPAEEEPAVTEEELRALVEeseESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 238 LSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLIQPALDGKgDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDE 317
Cdd:COG1253  239 LELILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGE-PFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 318 YGGTAGIITIEDIVEEIVGEIEDEFDPDNKYLTRLSRREWLVDGRFSCDDAIE-LGWPLEESDDYETIAGWILELCDSVP 396
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNElLGLDLPEEEDYETLGGLVLEQLGRIP 397

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 942070976 397 DIGEVFEVAGYKFKVQSMRGQRISLIRVIAPAETDKKD 434
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 1-434 2.97e-175

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 498.11  E-value: 2.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   1 MDITISLITTLVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAVAST 80
Cdd:COG1253    1 MSLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  81 SLSDPLATWLMSFGIAPlsAIARGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTG 160
Cdd:COG1253   81 ALAALLAPLLGSLGLPA--ALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 161 ACSDGLARILRIKSADDRQNVSEEEIKYMVS---EQDDLLDEEKRMIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADV 237
Cdd:COG1253  159 GSTNLLLRLLGIEPAEEEPAVTEEELRALVEeseESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 238 LSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLIQPALDGKgDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDE 317
Cdd:COG1253  239 LELILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGE-PFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 318 YGGTAGIITIEDIVEEIVGEIEDEFDPDNKYLTRLSRREWLVDGRFSCDDAIE-LGWPLEESDDYETIAGWILELCDSVP 396
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNElLGLDLPEEEDYETLGGLVLEQLGRIP 397

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 942070976 397 DIGEVFEVAGYKFKVQSMRGQRISLIRVIAPAETDKKD 434
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 11-424 2.27e-61

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: 205.27  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   11 LVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGfassaVASTSLSDPLAtWL 90
Cdd:TIGR03520   1 FILLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFIN-----IAIVLLFTSLS-DN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   91 MSFGIAPLsaiarGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTGACSDGLARil 170
Cdd:TIGR03520  75 LFGSFNTE-----LLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHK-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  171 riKSADDRQNVSEEEIKYMV--SEQDDLLDEEKRMIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSR 248
Cdd:TIGR03520 148 --KFGKQKSNISVDQLSQALelTDEEDTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSR 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  249 IPVYHEDPDNVAGIAHIKDLIqPALDGKgDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIE 328
Cdd:TIGR03520 226 IPVYKETIDNITGVLYIKDLL-PHLNKK-NFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  329 DIVEEIVGEIEDEFDPDNKYLTRLSRREWLVDGRFSCDD---AIELGWP-LEESD-DYETIAGWILELCDSVPDIGEVFE 403
Cdd:TIGR03520 304 DIIEEIVGDISDEFDDEDLIYSKIDDNNYVFEGKTSLKDfykILKLEEDmFDEVKgEAETLAGFLLEISGGFPKKGEKIT 383

                         410       420
                  ....*....|....*....|.
gi 942070976  404 VAGYKFKVQSMRGQRISLIRV 424
Cdd:TIGR03520 384 FENFEFTIEAMDKKRIKQVKV 404
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 8-200 9.52e-46

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: 9.52e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976    8 ITTLVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAVASTSLSDPLA 87
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   88 TWlmsfgiaplsaiaRGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTGACSDGLA 167
Cdd:pfam01595  81 PL-------------GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLIL 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 942070976  168 RILRIKSADDRQNVSEEEIKYMV--SEQDDLLDEE 200
Cdd:pfam01595 148 RLFGVKGGESEPAVTEEELRSLVeeSAEEGVIEEE 182
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 214-332 1.44e-45

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 154.19  E-value: 1.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 214 VAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLIQPALDGKGDQPIAGFLRDATFVPD 293
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 942070976 294 TKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVE 332
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
191-432 2.39e-37

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 138.02  E-value: 2.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 191 SEQDDLLDEEKR-MIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLI 269
Cdd:PRK15094  44 SEQNDLIDEDTRdMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 270 QPALDGKGDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEIVGEIEDEFD-PDNKY 348
Cdd:PRK15094 124 PFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDeEDDID 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 349 LTRLSRREWLVDGRFSCDDAIELGWPLEESDDYETIAGWILELCDSVPDIGEVFEVAGYKFKVQSMRGQRISLIRVIAPA 428
Cdd:PRK15094 204 FRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPD 283


                 ....
gi 942070976 429 ETDK 432
Cdd:PRK15094 284 DSPQ 287
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 350-424 1.28e-15

Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.


Pssm-ID: 215020 [Multi-domain]  Cd Length: 78  Bit Score: 71.32  E-value: 1.28e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942070976   350 TRLSRREWLVDGRFSCDDAIE-LGWPLEEsDDYETIAGWILELCDSVPDIGEVFEVAGYKFKVQSMRGQRISLIRV 424
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNElLGLDLPE-EEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRV 75
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 1-434 2.97e-175

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 498.11  E-value: 2.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   1 MDITISLITTLVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAVAST 80
Cdd:COG1253    1 MSLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  81 SLSDPLATWLMSFGIAPlsAIARGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTG 160
Cdd:COG1253   81 ALAALLAPLLGSLGLPA--ALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 161 ACSDGLARILRIKSADDRQNVSEEEIKYMVS---EQDDLLDEEKRMIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADV 237
Cdd:COG1253  159 GSTNLLLRLLGIEPAEEEPAVTEEELRALVEeseESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 238 LSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLIQPALDGKgDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDE 317
Cdd:COG1253  239 LELILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEGE-PFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 318 YGGTAGIITIEDIVEEIVGEIEDEFDPDNKYLTRLSRREWLVDGRFSCDDAIE-LGWPLEESDDYETIAGWILELCDSVP 396
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNElLGLDLPEEEDYETLGGLVLEQLGRIP 397

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 942070976 397 DIGEVFEVAGYKFKVQSMRGQRISLIRVIAPAETDKKD 434
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 1-424 1.87e-113

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: 340.13  E-value: 1.87e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   1 MD---ITISLITTLVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAV 77
Cdd:COG4536    1 MDdisLSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  78 AsTSLSDPLatwlmsFGiaplsaiARGLApvIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVW 157
Cdd:COG4536   81 A-TVIAIRL------FG-------DAGVA--IATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVW 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 158 LTGACSDGLARILRIK-SADDRQNVSEEEIKYMVSEQDD---LLDEEKRMIHEIFDLGDTVAREVMVPRVDTTMCEDDET 233
Cdd:COG4536  145 LVNLIVRGLLRLFGVKpDADASDLLSEEELRTVVDLGEAggvIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDP 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 234 VADVLSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLIQPALDGKGDQ-PIAGFLRDATFVPDTKDILPLLSEMQTSHDQIV 312
Cdd:COG4536  225 WEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLLRALRKGDLSKeDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFA 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 313 VVVDEYGGTAGIITIEDIVEEIVGEIEDEFDPDNKYLTRLSRREWLVDGRFSCDDaI--ELGWPLEEsDDYETIAGWILE 390
Cdd:COG4536  305 LVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRD-LnrALDWNLPD-DGAKTLNGLIIE 382

                        410       420       430
                 ....*....|....*....|....*....|....
gi 942070976 391 LCDSVPDIGEVFEVAGYKFKVQSMRGQRISLIRV 424
Cdd:COG4536  383 ELEDIPEAGQSFTIHGYRFEILQVQDNRIKTVRI 416
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 11-424 2.27e-61

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: 205.27  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   11 LVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGfassaVASTSLSDPLAtWL 90
Cdd:TIGR03520   1 FILLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFIN-----IAIVLLFTSLS-DN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   91 MSFGIAPLsaiarGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTGACSDGLARil 170
Cdd:TIGR03520  75 LFGSFNTE-----LLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHK-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  171 riKSADDRQNVSEEEIKYMV--SEQDDLLDEEKRMIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSR 248
Cdd:TIGR03520 148 --KFGKQKSNISVDQLSQALelTDEEDTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSR 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  249 IPVYHEDPDNVAGIAHIKDLIqPALDGKgDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIE 328
Cdd:TIGR03520 226 IPVYKETIDNITGVLYIKDLL-PHLNKK-NFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  329 DIVEEIVGEIEDEFDPDNKYLTRLSRREWLVDGRFSCDD---AIELGWP-LEESD-DYETIAGWILELCDSVPDIGEVFE 403
Cdd:TIGR03520 304 DIIEEIVGDISDEFDDEDLIYSKIDDNNYVFEGKTSLKDfykILKLEEDmFDEVKgEAETLAGFLLEISGGFPKKGEKIT 383

                         410       420
                  ....*....|....*....|.
gi 942070976  404 VAGYKFKVQSMRGQRISLIRV 424
Cdd:TIGR03520 384 FENFEFTIEAMDKKRIKQVKV 404
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 191-436 2.48e-57

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: 190.71  E-value: 2.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 191 SEQDDLLDEE-KRMIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLI 269
Cdd:COG4535   40 AEERELIDADtLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 270 QPALDGKGDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEIVGEIEDEFD--PDNK 347
Cdd:COG4535  120 RYLAQDAEEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIEDEHDedEDED 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 348 YLTRLSRREWLVDG---------RFSCDdaielgwpLEEsDDYETIAGWILELCDSVPDIGEVFEVAGYKFKVQSMRGQR 418
Cdd:COG4535  200 NIRPLSDGSYRVKAltpiedfneYFGTD--------FSD-EEFDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRR 270

                        250
                 ....*....|....*...
gi 942070976 419 ISLIRVIAPAETDKKDSE 436
Cdd:COG4535  271 IHLLRVTRLPPAAEPDAE 288
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 8-200 9.52e-46

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: 9.52e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976    8 ITTLVLTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAVASTSLSDPLA 87
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976   88 TWlmsfgiaplsaiaRGLAPVIITVAVAFVSIVIGELVPKRIGLANAEGVSKQVVGPLSFFQKIARPLVWLTGACSDGLA 167
Cdd:pfam01595  81 PL-------------GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLIL 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 942070976  168 RILRIKSADDRQNVSEEEIKYMV--SEQDDLLDEE 200
Cdd:pfam01595 148 RLFGVKGGESEPAVTEEELRSLVeeSAEEGVIEEE 182
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 214-332 1.44e-45

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 154.19  E-value: 1.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 214 VAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLIQPALDGKGDQPIAGFLRDATFVPD 293
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 942070976 294 TKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVE 332
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
191-432 2.39e-37

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 138.02  E-value: 2.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 191 SEQDDLLDEEKR-MIHEIFDLGDTVAREVMVPRVDTTMCEDDETVADVLSTMRQTGFSRIPVYHEDPDNVAGIAHIKDLI 269
Cdd:PRK15094  44 SEQNDLIDEDTRdMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 270 QPALDGKGDQPIAGFLRDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEIVGEIEDEFD-PDNKY 348
Cdd:PRK15094 124 PFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDeEDDID 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 349 LTRLSRREWLVDGRFSCDDAIELGWPLEESDDYETIAGWILELCDSVPDIGEVFEVAGYKFKVQSMRGQRISLIRVIAPA 428
Cdd:PRK15094 204 FRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPD 283


                 ....
gi 942070976 429 ETDK 432
Cdd:PRK15094 284 DSPQ 287
PRK11573 PRK11573
hypothetical protein; Provisional
 13-425 5.60e-32

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 126.40  E-value: 5.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  13 LTLINGYFSMSEMALTTAKRAVLEHEAEEGDKRAERAIKLAADSDQLLATIQVAITLVGFASSAVASTslsdplaTWLMS 92
Cdd:PRK11573   1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTI-------VGMRL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976  93 FGIAPLsAIARGLapviitvaVAFVSIVIGELVPKRIGLANAEGV---SKQVVGPLsffQKIARPLVWLTGACSDGLARI 169
Cdd:PRK11573  74 YGDAGV-AIATGV--------LTFVVLVFAEVLPKTIAALYPEKVaypSSFLLAPL---QILMMPLVWLLNTITRLLMRL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 170 LRIKSADDRQN-VSEEEIKYMVSEQDDLLDEEKR-MIHEIFDLGDTVAREVMVPRVDTTMCEDDEtvaDVLSTMRQTGFS 247
Cdd:PRK11573 142 MGIKTDIVVSGaLSKEELRTIVHESRSQISRRNQdMLLSVLDLEKVTVDDIMVPRNEIVGIDIND---DWKSILRQLTHS 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 248 ---RIPVYHEDPDNVAGIAHIKDLIQpALDGKGDQPIAGFLRDAT---FVPDTKDILPLLSEMQTSHDQIVVVVDEYGGT 321
Cdd:PRK11573 219 phgRIVLYRDSLDDAISMLRVREAYR-LMTEKKEFTKENMLRAADeiyFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDI 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 322 AGIITIEDIVEEIVGEIEDEFDPD-NKYLTRLSRREWLVDGRFSCDDAIE-LGWPLEEsDDYETIAGWILELCDSVPDIG 399
Cdd:PRK11573 298 QGLVTVEDILEEIVGDFTTSMSPTlAEEVTPQNDGSVIIDGTANVREINKaFNWHLPE-DDARTVNGVILEALEEIPVAG 376

                        410       420
                 ....*....|....*....|....*.
gi 942070976 400 EVFEVAGYKFKVQSMRGQRISLIRVI 425
Cdd:PRK11573 377 TRVRIGEYDIDILDVQDNMIKQVKVT 402
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 350-424 1.28e-15

Transporter associated domain; This small domain is found in a family of proteins with the DUF21 domain and two CBS domains with this domain found at the C-terminus of the proteins, the domain is also found at the C terminus of some Na+/H+ antiporters. This domain is also found in CorC that is involved in Magnesium and cobalt efflux. The function of this domain is uncertain but might be involved in modulating transport of ion substrates.


Pssm-ID: 215020 [Multi-domain]  Cd Length: 78  Bit Score: 71.32  E-value: 1.28e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942070976   350 TRLSRREWLVDGRFSCDDAIE-LGWPLEEsDDYETIAGWILELCDSVPDIGEVFEVAGYKFKVQSMRGQRISLIRV 424
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNElLGLDLPE-EEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRV 75
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 350-424 7.49e-15

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


Pssm-ID: 460935 [Multi-domain]  Cd Length: 81  Bit Score: 69.50  E-value: 7.49e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942070976  350 TRLSRREWLVDGRFSCDDAIE-LGWPLEEsDDYETIAGWILELCDSVPDIGEVFEV--AGYKFKVQSMRGQRISLIRV 424
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNElLGLELPE-EDYDTLGGLVLERLGRIPKVGDKVEVelGGLRFTVLEMDGRRIKKVRI 77
CBS COG0517
CBS domain [Signal transduction mechanisms];
215-339 1.54e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 52.95  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 215 AREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVYHEDpDNVAGIAHIKDLIQpALDGKG----DQPIAGFL-RDAT 289
Cdd:COG0517    3 VKDIMTTDVVT--VSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRR-ALAAEGkdllDTPVSEVMtRPPV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 942070976 290 FVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEIVGEIE 339
Cdd:COG0517   79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 230-331 2.21e-08

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: 51.86  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 230 DDETVADVLSTMRQTGFSRIPVyHEDPDNVAGIAHIKDLIQ--PALDGKGDQPIAGFL-RDATFVPDTKDILPLLSEMQT 306
Cdd:cd02205    9 PDTTVREALELMAENGIGALPV-VDDDGKLVGIVTERDILRalVEGGLALDTPVAEVMtPDVITVSPDTDLEEALELMLE 87

                         90       100
                 ....*....|....*....|....*
gi 942070976 307 SHDQIVVVVDEYGGTAGIITIEDIV 331
Cdd:cd02205   88 HGIRRLPVVDDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
214-341 5.19e-08

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 51.40  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 214 VAREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVYHEDpDNVAGIAHIKDLIQPALDGKGDQPIAGFL-------- 285
Cdd:COG3448    3 TVRDIMTRDVVT--VSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLPDRLDELEERLLdlpvedvm 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 942070976 286 -RDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEIVGEIEDE 341
Cdd:COG3448   80 tRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
200-334 2.07e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 51.42  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 200 EKRMIHEIFDLGDTVAREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVyhEDPDNVAGIAHIKDLIQPALDGKG-- 277
Cdd:COG2524   73 RVVAEKELGLVLKMKVKDIMTKDVIT--VSPDTTLEEALELMLEKGISGLPV--VDDGKLVGIITERDLLKALAEGRDll 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 942070976 278 DQPIAGFL-RDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEI 334
Cdd:COG2524  149 DAPVSDIMtRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 195-270 4.05e-07

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 48.67  E-value: 4.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942070976 195 DLLdeeKRMIHEIFDLGDTVAREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVyhEDPDNVAGIAHIKDLIQ 270
Cdd:COG2905   50 DLR---RRVLAEGLDPLDTPVSEVMTRPPIT--VSPDDSLAEALELMEEHRIRHLPV--VDDGKLVGIVSITDLLR 118
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 215-269 1.56e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 42.20  E-value: 1.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 942070976  215 AREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVYHEDpDNVAGIAHIKDLI 269
Cdd:pfam00571   1 VKDIMTKDVVT--VSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLL 52
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 215-331 1.15e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 41.74  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 215 AREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVYHEDpDNVAGIAHIKDLIQPALDGKGD---QPIAGFL-RDATF 290
Cdd:COG2905    1 VKDIMSRDVVT--VSPDATVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLRRRVLAEGLDpldTPVSEVMtRPPIT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 942070976 291 VPDTKDILPLLSEMQTSHDQIVVVVDEyGGTAGIITIEDIV 331
Cdd:COG2905   78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
201-332 3.21e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 40.67  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 201 KRMIHEIFD--LGDTVAREVMVPRVDTTMCEDDeTVADVLSTMRQTGFSRIPVyhEDPDN-VAGIAHIKDLIqPALDgkg 277
Cdd:COG4109    2 KHIISTSYDtfKEILLVEDIMTLEDVATLSEDD-TVEDALELLEKTGHSRFPV--VDENGrLVGIVTSKDIL-GKDD--- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 942070976 278 DQPIAGFL-RDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVE 332
Cdd:COG4109   75 DTPIEDVMtKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 202-268 3.25e-04

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. 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: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 40.10  E-value: 3.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942070976 202 RMIHEIFDLGDTVAREVMVPRVDTtmCEDDETVADVLSTMRQTGFSRIPVYhEDPDNVAGIAHIKDL 268
Cdd:cd04622   49 RAVAEGKDPNTTTVREVMTGDVVT--CSPDDDVEEAARLMAEHQVRRLPVV-DDDGRLVGIVSLGDL 112
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 224-270 4.62e-04

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 37.88  E-value: 4.62e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 942070976   224 DTTMCEDDETVADVLSTMRQTGFSRIPVYHEDpDNVAGIAHIKDLIQ 270
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIK 46
CBS_pair_chlorobiales cd09837
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 229-332 8.31e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in chlorobiales; 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: 341406 [Multi-domain]  Cd Length: 111  Bit Score: 38.89  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 229 EDDETVADVLSTMRQTGFSRIPVYHEdpDNVAGIAHIKDLIqPALDGKgdqPIAGFLRDATFVPDTKDILP------LLS 302
Cdd:cd09837    8 TDDAPAAEVLAFMQAKELSCAPVLHD--GRYVAMVTLADLL-PARQGT---PTAGLKLGELSLEEVGSIGPhehlfdLFS 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 942070976 303 EMQTSHDQIVVVVDEYGGTAGIITIEDIVE 332
Cdd:cd09837   82 RLALFPCSIIPVSDEDGRYIGVVSKKRVLE 111
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 248-332 2.54e-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: 37.55  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 248 RIPVYHEDpDNVAGIAHIKDLIQPALDGKGDQPIAGFLRDATFVPDTKDILPLL---SEMQTSHDQIVVVVDEYGGTAGI 324
Cdd:cd04639   32 EFLVTDEA-GRLVGLITVDDLRAIPTSQWPDTPVRELMKPLEEIPTVAADQSLLevvKLLEEQQLPALAVVSENGTLVGL 110


                 ....*...
gi 942070976 325 ITIEDIVE 332
Cdd:cd04639  111 IEKEDIIE 118
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 230-332 4.57e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; 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 archaea. 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: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 36.55  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942070976 230 DDETVADVLSTMRQTGFSRIPVYHEDpDNVAGIAHIKDLiqpaLDGKGDQPIAGFLRDATFVPDTKDILPLLSEMQTSHD 309
Cdd:cd04594    9 AYDTVERALKIMRENNLLSLPVVDND-SNFLGAVYLRDI----ENKSPGKVGKYVVRGSPYVTPTSSLEEAWEIMMRNKS 83

                         90       100
                 ....*....|....*....|...
gi 942070976 310 QIVVVVDEyGGTAGIITIEDIVE 332
Cdd:cd04594   84 RWVAVVEK-GKFLGIITLDDLLE 105
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 286-336 8.93e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 34.50  E-value: 8.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 942070976  286 RDATFVPDTKDILPLLSEMQTSHDQIVVVVDEYGGTAGIITIEDIVEEIVG 336
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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