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Conserved domains on  [gi|503472039|ref|WP_013706700|]
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hemolysin family protein [Desulfobacca acetoxidans]

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 ...
 22-416 2.28e-132

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 387.17  E-value: 2.28e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  22 SSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETAN----TVLVSALLIDIYGRTGE------ 91
Cdd:COG1253   22 ASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAgalgEAALAALLAPLLGSLGLpaalah 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  92 ----AAAMLTLPPIILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLAPFVTR 167
Cdd:COG1253  102 tlalVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPAVTE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 168 EELKMVVKASGAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNII 247
Cdd:COG1253  182 EELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGDLDDIV 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 248 GILHSFDLLGA--ENPAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADE 325
Cdd:COG1253  262 GVVHVKDLLRAllEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGEIRDE 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 326 FDQEISPFQKLRDGAYLINARMEIEAVNENLGLNLP-LGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIK 404
Cdd:COG1253  342 YDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPeEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVLDMDGRRID 421

                        410
                 ....*....|..
gi 503472039 405 EVEVHVEASKTA 416
Cdd:COG1253  422 KVLVTRLPEEEE 433
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 22-416 2.28e-132

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 387.17  E-value: 2.28e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  22 SSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETAN----TVLVSALLIDIYGRTGE------ 91
Cdd:COG1253   22 ASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAgalgEAALAALLAPLLGSLGLpaalah 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  92 ----AAAMLTLPPIILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLAPFVTR 167
Cdd:COG1253  102 tlalVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPAVTE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 168 EELKMVVKASGAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNII 247
Cdd:COG1253  182 EELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGDLDDIV 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 248 GILHSFDLLGA--ENPAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADE 325
Cdd:COG1253  262 GVVHVKDLLRAllEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGEIRDE 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 326 FDQEISPFQKLRDGAYLINARMEIEAVNENLGLNLP-LGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIK 404
Cdd:COG1253  342 YDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPeEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVLDMDGRRID 421

                        410
                 ....*....|..
gi 503472039 405 EVEVHVEASKTA 416
Cdd:COG1253  422 KVLVTRLPEEEE 433
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 23-411 1.07e-66

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: 217.98  E-value: 1.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039   23 SEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYG-RTGEAAAMLTLPPI 101
Cdd:TIGR03520  13 SEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGsFNTELLRFLIEVVI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  102 ----ILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLapfvTREELKMVVKAS 177
Cdd:TIGR03520  93 vtflILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQKSNI----SVDQLSQALELT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  178 gAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDLLG 257
Cdd:TIGR03520 169 -DEEDTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNITGVLYIKDLLP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  258 AEN-PAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADEFDQEISPFQKL 336
Cdd:TIGR03520 248 HLNkKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFDDEDLIYSKI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  337 RDGAYLINARMEIEAVNENLGLNLPL-----GNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEVHVE 411
Cdd:TIGR03520 328 DDNNYVFEGKTSLKDFYKILKLEEDMfdevkGEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDKKRIKQVKVTIN 407
PRK11573 PRK11573
hypothetical protein; Provisional
 21-408 1.44e-45

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 162.23  E-value: 1.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  21 TSSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYGRTGEAAAMLTLPP 100
Cdd:PRK11573   9 SGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDAGVAIATGVLTF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 101 IILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARS-TSLAPFVTREELKMVVKASGA 179
Cdd:PRK11573  89 VVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTdIVVSGALSKEELRTIVHESRS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 180 EVDLDTEERTIihRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDL--LG 257
Cdd:PRK11573 169 QISRRNQDMLL--SVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLRVREAyrLM 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 258 AENPAFGIKKLIRPAR---FVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGD----IADEFDQEI 330
Cdd:PRK11573 247 TEKKEFTKENMLRAADeiyFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDfttsMSPTLAEEV 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503472039 331 SPfqkLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEV 408
Cdd:PRK11573 327 TP---QNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQVKV 401
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 201-316 1.18e-41

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 143.02  E-value: 1.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 201 TVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDLLGA---ENPAFGIKKLIRPARFVPV 277
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAAlleGREKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503472039 278 TKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLE 316
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 22-187 1.91e-32

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: 120.78  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039   22 SSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYGRTGEAAAMLTLP-- 99
Cdd:pfam01595  15 AAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPLGALGVAIATVlv 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  100 -PIILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLAPFVTREELKMVVKASG 178
Cdd:pfam01595  95 tLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAVTEEELRSLVEESA 174


                  ....*....
gi 503472039  179 AEVDLDTEE 187
Cdd:pfam01595 175 EEGVIEEEE 183
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 334-409 1.67e-18

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


Pssm-ID: 215020 [Multi-domain]  Cd Length: 78  Bit Score: 79.41  E-value: 1.67e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503472039   334 QKLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEVH 409
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 22-416 2.28e-132

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 387.17  E-value: 2.28e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  22 SSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETAN----TVLVSALLIDIYGRTGE------ 91
Cdd:COG1253   22 ASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAgalgEAALAALLAPLLGSLGLpaalah 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  92 ----AAAMLTLPPIILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLAPFVTR 167
Cdd:COG1253  102 tlalVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPAVTE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 168 EELKMVVKASGAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNII 247
Cdd:COG1253  182 EELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGDLDDIV 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 248 GILHSFDLLGA--ENPAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADE 325
Cdd:COG1253  262 GVVHVKDLLRAllEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGEIRDE 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 326 FDQEISPFQKLRDGAYLINARMEIEAVNENLGLNLP-LGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIK 404
Cdd:COG1253  342 YDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPeEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVLDMDGRRID 421

                        410
                 ....*....|..
gi 503472039 405 EVEVHVEASKTA 416
Cdd:COG1253  422 KVLVTRLPEEEE 433
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 22-410 1.67e-106

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: 320.87  E-value: 1.67e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  22 SSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYGRTGEAAAMLTLPPI 101
Cdd:COG4536   25 GSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAIRLFGDAGVAIATLVLTLL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 102 ILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLAP-FVTREELKMVVKASGAE 180
Cdd:COG4536  105 ILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPDADASdLLSEEELRTVVDLGEAG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 181 VDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDLLGA-- 258
Cdd:COG4536  185 GVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLLRAlr 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 259 --ENPAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADEFDQEISPFQKL 336
Cdd:COG4536  265 kgDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDAEEIRPQ 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503472039 337 RDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEVHV 410
Cdd:COG4536  345 EDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQVQDNRIKTVRIRP 418
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 23-411 1.07e-66

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: 217.98  E-value: 1.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039   23 SEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYG-RTGEAAAMLTLPPI 101
Cdd:TIGR03520  13 SEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGsFNTELLRFLIEVVI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  102 ----ILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLapfvTREELKMVVKAS 177
Cdd:TIGR03520  93 vtflILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQKSNI----SVDQLSQALELT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  178 gAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDLLG 257
Cdd:TIGR03520 169 -DEEDTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNITGVLYIKDLLP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  258 AEN-PAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADEFDQEISPFQKL 336
Cdd:TIGR03520 248 HLNkKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFDDEDLIYSKI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  337 RDGAYLINARMEIEAVNENLGLNLPL-----GNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEVHVE 411
Cdd:TIGR03520 328 DDNNYVFEGKTSLKDFYKILKLEEDMfdevkGEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDKKRIKQVKVTIN 407
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 146-410 1.99e-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: 197.64  E-value: 1.99e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 146 FSRLVLLLTGARSTslapfvtREELKMVVKASGAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPetylISQAL 225
Cdd:COG4535   16 LERLSQLFSGEPED-------REELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVID----IDQPL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 226 EEF-----RRGRfSRLPVYRHRIDNIIGILHSFDLL---GAENPAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVI 297
Cdd:COG4535   85 EEIlpvviESAH-SRFPVIGEDRDEVIGILLAKDLLrylAQDAEEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 298 VVDEYGGAVGIVALEDLLEEVVGDIADEFDQE--ISPFQKLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQ 375
Cdd:COG4535  164 VVDEYGGVAGLVTIEDVLEQIVGEIEDEHDEDedEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQE 243

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 503472039 376 VGDIPRTGERIRYRNLLFIIRLADLRAIKEVEVHV 410
Cdd:COG4535  244 FGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTR 278
PRK11573 PRK11573
hypothetical protein; Provisional
 21-408 1.44e-45

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 162.23  E-value: 1.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  21 TSSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYGRTGEAAAMLTLPP 100
Cdd:PRK11573   9 SGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDAGVAIATGVLTF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 101 IILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARS-TSLAPFVTREELKMVVKASGA 179
Cdd:PRK11573  89 VVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTdIVVSGALSKEELRTIVHESRS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 180 EVDLDTEERTIihRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDL--LG 257
Cdd:PRK11573 169 QISRRNQDMLL--SVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLRVREAyrLM 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 258 AENPAFGIKKLIRPAR---FVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGD----IADEFDQEI 330
Cdd:PRK11573 247 TEKKEFTKENMLRAADeiyFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDfttsMSPTLAEEV 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503472039 331 SPfqkLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEV 408
Cdd:PRK11573 327 TP---QNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQVKV 401
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 201-316 1.18e-41

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 143.02  E-value: 1.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 201 TVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNIIGILHSFDLLGA---ENPAFGIKKLIRPARFVPV 277
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAAlleGREKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503472039 278 TKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLE 316
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
167-410 4.11e-39

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 141.87  E-value: 4.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 167 REELKMVVKASGAEVDLDTEERTIIHRILYFSQTTVKEVMIPLIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDNI 246
Cdd:PRK15094  34 RDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 247 IGILHSFDLLG---AENPAFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIA 323
Cdd:PRK15094 114 EGILMAKDLLPfmrSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIE 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 324 DEFD-QEISPFQKLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRA 402
Cdd:PRK15094 194 DEYDeEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRR 273


                 ....*...
gi 503472039 403 IKEVEVHV 410
Cdd:PRK15094 274 IIQVHVKI 281
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 22-187 1.91e-32

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: 120.78  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039   22 SSEIALVSANHRQLQHLAENGQRQAILAQKLLRAPERLFATTLLGSNLAETANTVLVSALLIDIYGRTGEAAAMLTLP-- 99
Cdd:pfam01595  15 AAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPLGALGVAIATVlv 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  100 -PIILLFAEILPKSIARLRPTRMAQKVSFFVWLASILLAPITWFFASFSRLVLLLTGARSTSLAPFVTREELKMVVKASG 178
Cdd:pfam01595  95 tLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAVTEEELRSLVEESA 174


                  ....*....
gi 503472039  179 AEVDLDTEE 187
Cdd:pfam01595 175 EEGVIEEEE 183
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 334-409 1.67e-18

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


Pssm-ID: 215020 [Multi-domain]  Cd Length: 78  Bit Score: 79.41  E-value: 1.67e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503472039   334 QKLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGERIRYRNLLFIIRLADLRAIKEVEVH 409
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVT 76
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 334-410 3.05e-17

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: 76.05  E-value: 3.05e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503472039  334 QKLRDGAYLINARMEIEAVNENLGLNLPLGNYHTLGGFLIKQVGDIPRTGE--RIRYRNLLFIIRLADLRAIKEVEVHV 410
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDkvEVELGGLRFTVLEMDGRRIKKVRITK 79
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
201-325 9.76e-08

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 50.63  E-value: 9.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 201 TVKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVyrhrIDN---IIGILHSFDLLGAENPAFGIKKLIRPARFV-- 275
Cdd:COG3448    3 TVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPV----VDEdgrLVGIVTERDLLRALLPDRLDELEERLLDLPve 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 276 ------PVTKRADRLLVE----MQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIADE 325
Cdd:COG3448   77 dvmtrpVVTVTPDTPLEEaaelMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS COG0517
CBS domain [Signal transduction mechanisms];
201-323 5.66e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 48.32  E-value: 5.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 201 TVKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVyrhrIDN---IIGILHSFDLLGAENpAFGIKKLIRPARFV-- 275
Cdd:COG0517    2 KVKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPV----VDEdgkLVGIVTDRDLRRALA-AEGKDLLDTPVSEVmt 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503472039 276 --PVTKRADRLLVE----MQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVGDIA 323
Cdd:COG0517   75 rpPVTVSPDTSLEEaaelMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 211-315 2.00e-06

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: 46.47  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 211 EVLAIPETYLISQALEEFRRGRFSRLPVyRHRIDNIIGILHSFDLLGAENPAFGIKK------LIRPARFVPVTKRADRL 284
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPV-VDDDGKLVGIVTERDILRALVEGGLALDtpvaevMTPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 503472039 285 LVEMQQEGIHLVIVVDEYGGAVGIVALEDLL 315
Cdd:cd02205   82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 187-258 8.92e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 44.82  E-value: 8.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503472039 187 ERTIIHRIL----YFSQTTVKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVyrhrIDN--IIGILHSFDLLGA 258
Cdd:COG2905   48 DRDLRRRVLaeglDPLDTPVSEVMTR--PPITVSPDDSLAEALELMEEHRIRHLPV----VDDgkLVGIVSITDLLRA 119
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
201-318 1.25e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.03  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 201 TVKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVYRHriDNIIGILHSFDLLGAENPAFGIKKLirPARFV----P 276
Cdd:COG2524   87 KVKDIMTK--DVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDA--PVSDImtrdV 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503472039 277 VTKRADRLLVE----MQQEGIHLVIVVDEYGGAVGIVALEDLLEEV 318
Cdd:COG2524  161 VTVSEDDSLEEalrlMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
201-316 1.57e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 44.13  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 201 TVKEVMIpLIEVLAIPETYLISQALEEFRRGRFSRLPVyrhrIDN---IIGILHSFDLLGAEnPAFGIKKLIRPArfvPV 277
Cdd:COG4109   17 LVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPV----VDEngrLVGIVTSKDILGKD-DDTPIEDVMTKN---PI 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503472039 278 TKRADRLLVE----MQQEGIHLVIVVDEYGGAVGIVALEDLLE 316
Cdd:COG4109   88 TVTPDTSLASaahkMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 202-315 3.48e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.89  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 202 VKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVYRHRiDNIIGILHSFDLLGAeNPAFGIKKLIRPARFV----PV 277
Cdd:COG2905    1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLRRR-VLAEGLDPLDTPVSEVmtrpPI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503472039 278 TKRADRLLVE----MQQEGIHLVIVVDEyGGAVGIVALEDLL 315
Cdd:COG2905   77 TVSPDDSLAEalelMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 202-258 1.48e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 39.50  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 503472039  202 VKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVYRHRiDNIIGILHSFDLLGA 258
Cdd:pfam00571   1 VKDIMTK--DVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRA 54
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 183-338 2.79e-04

Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129495 [Multi-domain]  Cd Length: 449  Bit Score: 42.89  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  183 LDTEERTIIHRILYFSQTTVKEVMIplIEVLAIPETYLISQALEEFRRGRFSRLPVYRHRIDN----IIGILHSFDLLGA 258
Cdd:TIGR00400 114 STEEERKAINLLLSYSDDSAGRIMT--IEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTNeskhLKGVLSIRDLILA 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039  259 EnPAFGIKKLIRPARFVPVT----KRADRLLvemQQEGIHLVIVVDEYGGAVGIVALEDLLeEVVGDIADEFDQEISPFQ 334
Cdd:TIGR00400 192 K-PEEILSSIMRSSVFSIVGvndqEEVARLI---QKYDFLAVPVVDNEGRLVGIVTVDDII-DVIQSEATEDFYMIAAVK 266


                  ....
gi 503472039  335 KLRD 338
Cdd:TIGR00400 267 PLDD 270
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 271-317 6.30e-04

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: 39.47  E-value: 6.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 503472039 271 PARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEE 317
Cdd:cd04640    6 PPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGE 52
CBS COG0517
CBS domain [Signal transduction mechanisms];
188-258 1.24e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 38.69  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503472039 188 RTIIHRILYFSQTTVKEVMIPliEVLAIPETYLISQALEEFRRGRFSRLPVyrhrIDN---IIGILHSFDLLGA 258
Cdd:COG0517   55 RALAAEGKDLLDTPVSEVMTR--PPVTVSPDTSLEEAAELMEEHKIRRLPV----VDDdgrLVGIITIKDLLKA 122
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 270-320 1.75e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.42  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503472039  270 RPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLEEVVG 320
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 202-315 2.88e-03

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 37.71  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503472039 202 VKEVMIPL-IEVLAIPETYLISQALEEFRRGRFSRLPVY-----------RHRID--------NIIGILHSFDLLGAENP 261
Cdd:cd17777    1 EKELMIIAsPPVLSISPSAPILSAFEKMNRRGIRRLVVVdenklegilsaRDLVSylgggclfKIVESRHQGDLYSALNR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503472039 262 AFGIKKLIRPARFVPVTKRADRLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLL 315
Cdd:cd17777   81 EVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 276-316 9.32e-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: 35.98  E-value: 9.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 503472039 276 PVTKRAD----RLLVEMQQEGIHLVIVVDEYGGAVGIVALEDLLE 316
Cdd:cd17775   71 LITAREDdglfEALERMREKGVRRLPVVDDDGELVGIVTLDDILE 115
 
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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