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Conserved domains on  [gi|499239570|ref|WP_010937110|]
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MULTISPECIES: HlyC/CorC family transporter [Dehalococcoides]

Protein Classification

HlyC/CorC family transporter( domain architecture ID 11468253)

HlyC/CorC family transporter similar to magnesium and cobalt efflux protein CorC and hemolysin C; the precise transport mechanism is unknown

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 3-418 9.35e-161

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: 459.16  E-value: 9.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   3 TDTWYLILFFLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVL 82
Cdd:COG4536    5 SLSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  83 AVSIWGnERGVLIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGG--PA 160
Cdd:COG4536   85 AIRLFG-DAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVkpDA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 161 LKSSLVAEDDIRAMITVGHKEGTVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVY 240
Cdd:COG4536  164 DASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVY 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 241 EDNMDNVLGILSIKDVLMALAKGTHNQQDLVDdLMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRL 320
Cdd:COG4536  244 RGDIDNIVGVLHVRDLLRALRKGDLSKEDLRK-IAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDI 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 321 MEEIVGPVGDELAEAEKDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVV 400
Cdd:COG4536  323 LEEIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFE 402

                        410
                 ....*....|....*...
gi 499239570 401 ITRMKGMKIDEVLITKEK 418
Cdd:COG4536  403 ILQVQDNRIKTVRIRPLP 420
 
Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 3-418 9.35e-161

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: 459.16  E-value: 9.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   3 TDTWYLILFFLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVL 82
Cdd:COG4536    5 SLSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  83 AVSIWGnERGVLIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGG--PA 160
Cdd:COG4536   85 AIRLFG-DAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVkpDA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 161 LKSSLVAEDDIRAMITVGHKEGTVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVY 240
Cdd:COG4536  164 DASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVY 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 241 EDNMDNVLGILSIKDVLMALAKGTHNQQDLVDdLMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRL 320
Cdd:COG4536  244 RGDIDNIVGVLHVRDLLRALRKGDLSKEDLRK-IAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDI 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 321 MEEIVGPVGDELAEAEKDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVV 400
Cdd:COG4536  323 LEEIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFE 402

                        410
                 ....*....|....*...
gi 499239570 401 ITRMKGMKIDEVLITKEK 418
Cdd:COG4536  403 ILQVQDNRIKTVRIRPLP 420
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 12-417 2.01e-76

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: 243.41  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   12 FLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVLAVSIWG--N 89
Cdd:TIGR03520   1 FILLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGsfN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   90 ERGV--LIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGGpalKSSLVA 167
Cdd:TIGR03520  81 TELLrfLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGK---QKSNIS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  168 EDDIRAMITVGHKEGTVEEDKaELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNV 247
Cdd:TIGR03520 158 VDQLSQALELTDEEDTTKEEQ-KILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  248 LGILSIKDVLMALAKGTHNQQDLvddlMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEIVGP 327
Cdd:TIGR03520 237 TGVLYIKDLLPHLNKKNFDWQSL----LREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  328 VGDELAEAEKDYESINEYTFQVDGSM------RIEEANAEMeLDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVI 401
Cdd:TIGR03520 313 ISDEFDDEDLIYSKIDDNNYVFEGKTslkdfyKILKLEEDM-FDEVKGEAETLAGFLLEISGGFPKKGEKITFENFEFTI 391

                         410
                  ....*....|....*.
gi 499239570  402 TRMKGMKIDEVLITKE 417
Cdd:TIGR03520 392 EAMDKKRIKQVKVTIN 407
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 9-187 5.35e-61

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: 195.90  E-value: 5.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570    9 ILFFLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVLAVSIWG 88
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   89 --NERGVLIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGGPALKS-SL 165
Cdd:pfam01595  81 plGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESePA 160

                         170       180
                  ....*....|....*....|..
gi 499239570  166 VAEDDIRAMITVGHKEGTVEED 187
Cdd:pfam01595 161 VTEEELRSLVEESAEEGVIEEE 182
PRK11573 PRK11573
hypothetical protein; Provisional
 15-415 8.04e-59

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 197.67  E-value: 8.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  15 IVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVLAVSIWGNErGVL 94
Cdd:PRK11573   2 VVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDA-GVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  95 IATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFG--GPALKSSLVAEDDIR 172
Cdd:PRK11573  81 IATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGikTDIVVSGALSKEELR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 173 AMITVGHKEgtVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNVLGILS 252
Cdd:PRK11573 161 TIVHESRSQ--ISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 253 IKDV--LMalakgTHNQQDLVDDLMRPA---YFAPETKPIG-KLFNEMREKNfRMCVVVDEYGGTAGIVSLSRLMEEIVG 326
Cdd:PRK11573 239 VREAyrLM-----TEKKEFTKENMLRAAdeiYFVPEGTPLStQLVKFQRNKK-KVGLVVDEYGDIQGLVTVEDILEEIVG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 327 ----PVGDELAEaekDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVIT 402
Cdd:PRK11573 313 dfttSMSPTLAE---EVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDIL 389

                        410
                 ....*....|...
gi 499239570 403 RMKGMKIDEVLIT 415
Cdd:PRK11573 390 DVQDNMIKQVKVT 402
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 202-322 4.09e-39

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: 136.47  E-value: 4.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 202 PVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNVLGILSIKDVLMALAKGthNQQDLVDDLMRPAYFA 281
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEG--REKLDLRALLRPPLFV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499239570 282 PETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLME 322
Cdd:cd04590   79 PETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 342-416 1.30e-21

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: 87.88  E-value: 1.30e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499239570   342 INEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVITRMKGMKIDEVLITK 416
Cdd:smart01091   3 LDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
 
Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 3-418 9.35e-161

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: 459.16  E-value: 9.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   3 TDTWYLILFFLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVL 82
Cdd:COG4536    5 SLSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  83 AVSIWGnERGVLIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGG--PA 160
Cdd:COG4536   85 AIRLFG-DAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVkpDA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 161 LKSSLVAEDDIRAMITVGHKEGTVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVY 240
Cdd:COG4536  164 DASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVY 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 241 EDNMDNVLGILSIKDVLMALAKGTHNQQDLVDdLMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRL 320
Cdd:COG4536  244 RGDIDNIVGVLHVRDLLRALRKGDLSKEDLRK-IAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDI 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 321 MEEIVGPVGDELAEAEKDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVV 400
Cdd:COG4536  323 LEEIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFE 402

                        410
                 ....*....|....*...
gi 499239570 401 ITRMKGMKIDEVLITKEK 418
Cdd:COG4536  403 ILQVQDNRIKTVRIRPLP 420
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 2-421 1.37e-156

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 449.18  E-value: 1.37e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   2 STDTWYLILFFLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTV 81
Cdd:COG1253    1 MSLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  82 LAVSI-------------WGNERGVLIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWI 148
Cdd:COG1253   81 ALAALlapllgslglpaaLAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 149 SSGFTKLFGG-PALKSSLVAEDDIRAMITVGHKEGTVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLD 227
Cdd:COG1253  161 TNLLLRLLGIePAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 228 LYAESPMSRFPVYEDNMDNVLGILSIKDVLMALAKGthnQQDLVDDLMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDE 307
Cdd:COG1253  241 LILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEG---EPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 308 YGGTAGIVSLSRLMEEIVGPVGDELAEAEKDYESINEYTFQVDGSMRIEEANAEMELDLPE-GDYETIAGLILDRLGYIP 386
Cdd:COG1253  318 YGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEeEDYETLGGLVLEQLGRIP 397

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 499239570 387 KQGQQIKLQNLKVVITRMKGMKIDEVLITKEKRAA 421
Cdd:COG1253  398 EVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEE 432
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 12-417 2.01e-76

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: 243.41  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   12 FLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVLAVSIWG--N 89
Cdd:TIGR03520   1 FILLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGsfN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   90 ERGV--LIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGGpalKSSLVA 167
Cdd:TIGR03520  81 TELLrfLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGK---QKSNIS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  168 EDDIRAMITVGHKEGTVEEDKaELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNV 247
Cdd:TIGR03520 158 VDQLSQALELTDEEDTTKEEQ-KILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  248 LGILSIKDVLMALAKGTHNQQDLvddlMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEIVGP 327
Cdd:TIGR03520 237 TGVLYIKDLLPHLNKKNFDWQSL----LREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  328 VGDELAEAEKDYESINEYTFQVDGSM------RIEEANAEMeLDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVI 401
Cdd:TIGR03520 313 ISDEFDDEDLIYSKIDDNNYVFEGKTslkdfyKILKLEEDM-FDEVKGEAETLAGFLLEISGGFPKKGEKITFENFEFTI 391

                         410
                  ....*....|....*.
gi 499239570  402 TRMKGMKIDEVLITKE 417
Cdd:TIGR03520 392 EAMDKKRIKQVKVTIN 407
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 9-187 5.35e-61

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: 195.90  E-value: 5.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570    9 ILFFLCIVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVLAVSIWG 88
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570   89 --NERGVLIATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFGGPALKS-SL 165
Cdd:pfam01595  81 plGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESePA 160

                         170       180
                  ....*....|....*....|..
gi 499239570  166 VAEDDIRAMITVGHKEGTVEED 187
Cdd:pfam01595 161 VTEEELRSLVEESAEEGVIEEE 182
PRK11573 PRK11573
hypothetical protein; Provisional
 15-415 8.04e-59

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 197.67  E-value: 8.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  15 IVFSAFFASSETAFISIQRFRLQNMVQSKVKGADKVSQLMERPEKFLSTVLLGNNFVNTAASALGTVLAVSIWGNErGVL 94
Cdd:PRK11573   2 VVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDA-GVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  95 IATAGVTIILLVFGETTPKTLATQHSEKIAFAVAPAVEVISKIFAPIVALLGWISSGFTKLFG--GPALKSSLVAEDDIR 172
Cdd:PRK11573  81 IATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGikTDIVVSGALSKEELR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 173 AMITVGHKEgtVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNVLGILS 252
Cdd:PRK11573 161 TIVHESRSQ--ISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 253 IKDV--LMalakgTHNQQDLVDDLMRPA---YFAPETKPIG-KLFNEMREKNfRMCVVVDEYGGTAGIVSLSRLMEEIVG 326
Cdd:PRK11573 239 VREAyrLM-----TEKKEFTKENMLRAAdeiYFVPEGTPLStQLVKFQRNKK-KVGLVVDEYGDIQGLVTVEDILEEIVG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 327 ----PVGDELAEaekDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVIT 402
Cdd:PRK11573 313 dfttSMSPTLAE---EVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDIL 389

                        410
                 ....*....|...
gi 499239570 403 RMKGMKIDEVLIT 415
Cdd:PRK11573 390 DVQDNMIKQVKVT 402
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 168-416 1.11e-56

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: 188.40  E-value: 1.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 168 EDDIRAMItvghkEGtveedkaellhkVFEFSDRPVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNV 247
Cdd:COG4535   47 DADTLSMI-----EG------------VLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 248 LGILSIKDVLMALAKGTHNQQdlVDDLMRPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEIVGP 327
Cdd:COG4535  110 IGILLAKDLLRYLAQDAEEFD--LRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGE 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 328 VGDE--LAEAEKDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVITRMK 405
Cdd:COG4535  188 IEDEhdEDEDEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRAD 267

                        250
                 ....*....|.
gi 499239570 406 GMKIDEVLITK 416
Cdd:COG4535  268 SRRIHLLRVTR 278
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 202-322 4.09e-39

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: 136.47  E-value: 4.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 202 PVREVIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMDNVLGILSIKDVLMALAKGthNQQDLVDDLMRPAYFA 281
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEG--REKLDLRALLRPPLFV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499239570 282 PETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLME 322
Cdd:cd04590   79 PETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
146-396 2.43e-38

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 139.94  E-value: 2.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 146 GWISSGFTKLFGGPALKsslvaEDDIRAMITVGHKEGTVEEDKAELLHKVFEFSDRPVREVIVPRPEVESVEKGSTLKDF 225
Cdd:PRK15094  17 GFFSLLLSQLFHGEPKN-----RDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDEC 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 226 LDLYAESPMSRFPVYEDNMDNVLGILSIKDVLMALAkgTHNQQDLVDDLMRPAYFAPETKPIGKLFNEMREKNFRMCVVV 305
Cdd:PRK15094  92 LDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMR--SDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 306 DEYGGTAGIVSLSRLMEEIVGPVGDELAEAE-KDYESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGY 384
Cdd:PRK15094 170 DEFGGVSGLVTIEDILELIVGEIEDEYDEEDdIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGH 249

                        250
                 ....*....|..
gi 499239570 385 IPKQGQQIKLQN 396
Cdd:PRK15094 250 LPARGETIDIDG 261
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 340-418 1.10e-21

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: 88.37  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570  340 ESINEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQ--IKLQNLKVVITRMKGMKIDEVLITKE 417
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKveVELGGLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 499239570  418 K 418
Cdd:pfam03471  81 E 81
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 342-416 1.30e-21

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: 87.88  E-value: 1.30e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499239570   342 INEYTFQVDGSMRIEEANAEMELDLPEGDYETIAGLILDRLGYIPKQGQQIKLQNLKVVITRMKGMKIDEVLITK 416
Cdd:smart01091   3 LDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 212-321 2.89e-13

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: 65.73  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 212 EVESVEKGSTLKDFLDLYAESPMSRFPVYEDNmDNVLGILSIKDVLMALAKGTHNQQDLVDDLM-RPAYFAPETKPIGKL 290
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPVAEVMtPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499239570 291 FNEMREKNFRMCVVVDEYGGTAGIVSLSRLM 321
Cdd:cd02205   82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
202-324 2.92e-12

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 65.29  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 202 PVREVIVPRPEVesVEKGSTLKDFLDLYAESPMSRFPVYEDnmDNVLGILSIKDVLMALAKGTHNQQDLVDDLM-RPAYF 280
Cdd:COG2524   87 KVKDIMTKDVIT--VSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDAPVSDIMtRDVVT 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499239570 281 APETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEI 324
Cdd:COG2524  163 VSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
203-327 2.70e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 60.65  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 203 VREVIvpRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNmDNVLGILSIKDVLMAL-AKGTHNQQDLVDDLM-RPAYF 280
Cdd:COG0517    3 VKDIM--TTDVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRRALaAEGKDLLDTPVSEVMtRPPVT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499239570 281 APETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEIVGP 327
Cdd:COG0517   80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEP 126
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
202-322 5.94e-10

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 56.84  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 202 PVREvIVPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNMdNVLGILSIKDVLMALAkgthnqQDLVDDLM-RPAYF 280
Cdd:COG4109   17 LVED-IMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDD------DTPIEDVMtKNPIT 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499239570 281 APETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLME 322
Cdd:COG4109   89 VTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
203-321 6.58e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 56.80  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 203 VREVIVPrpEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNmDNVLGILSIKDVLMALAKGTHNQ------QDLVDDLM- 275
Cdd:COG3448    4 VRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLPDRLDEleerllDLPVEDVMt 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499239570 276 RPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLM 321
Cdd:COG3448   81 RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLL 126
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 203-321 5.71e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 54.06  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 203 VREVIvpRPEVESVEKGSTLKDFLDLYAESPMSRFPVyEDNMDNVLGILSIKDVLMA-LAKGTHNQQDLVDDLM-RPAYF 280
Cdd:COG2905    1 VKDIM--SRDVVTVSPDATVREAARLMTEKGVGSLVV-VDDDGRLVGIITDRDLRRRvLAEGLDPLDTPVSEVMtRPPIT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499239570 281 APETKPIGKLFNEMREKNFRMCVVVDEyGGTAGIVSLSRLM 321
Cdd:COG2905   78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 271-326 6.93e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.36  E-value: 6.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499239570  271 VDDLM-RPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEIVG 326
Cdd:pfam00571   1 VKDIMtKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 210-324 1.42e-05

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 44.05  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 210 RPEVESVEKGSTLKDFLDLYAESPMSRFPVyEDNMDNVLGILSIKDVLMALAKGTHNQQDLVDDLMRPAYFAPETKPIGK 289
Cdd:cd09836    2 SKPVVTVPPETTIREAAKLMAENNIGSVVV-VDDDGKPVGIVTERDIVRAVAEGIDLDTPVEEIMTKNLVTVSPDESIYE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499239570 290 LFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEI 324
Cdd:cd09836   81 AAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 208-262 1.96e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.82  E-value: 1.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499239570  208 VPRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNmDNVLGILSIKDVLMALAK 262
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALLG 57
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 219-322 2.48e-05

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 43.23  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 219 GSTLKDFLDLYAESPMSRFPVYEDNMdNVLGILSIKDVLmalakgTHNQQDLVDDLM-RPAYFAPETKPIGKLFNEMREK 297
Cdd:cd04596   10 TDTVRDYKQLSEETGHSRFPVVDEEN-RVVGIVTAKDVI------GKEDDTPIEKVMtKNPITVKPKTSVASAAHMMIWE 82

                         90       100
                 ....*....|....*....|....*
gi 499239570 298 NFRMCVVVDEYGGTAGIVSLSRLME 322
Cdd:cd04596   83 GIELLPVVDENRKLLGVISRQDVLK 107
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 215-323 1.57e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 40.98  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 215 SVEKGSTLKDFLDLYAESPMSRFPVYEDnmDNVLGILSIKDVLMALAKGTHNQQdlVDDLMRP-AYFAPETKPIGKLFNE 293
Cdd:cd04588    6 TLKPDATIKDAAKLLSENNIHGAPVVDD--GKLVGIVTLTDIAKALAEGKENAK--VKDIMTKdVITIDKDEKIYDAIRL 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 499239570 294 MREKNFRMCVVVDEYGGTAGIVSLSRLMEE 323
Cdd:cd04588   82 MNKHNIGRLIVVDDNGKPVGIITRTDILKV 111
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 248-324 1.88e-04

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: 40.60  E-value: 1.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499239570 248 LGILSIKD-VLMALAKGTHNQQDLVDDLM-RPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEI 324
Cdd:cd17775   39 VGIVTDRDiVVEVVAKGLDPKDVTVGDIMsADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
197-267 2.94e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.62  E-value: 2.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499239570 197 EFSDRPVREVIvpRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNmDNVLGILSIKDVLMALAKGTHNQ 267
Cdd:COG3448   69 RLLDLPVEDVM--TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLRALARLLEEE 136
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
270-338 1.47e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 38.69  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 270 LVDDLM-RPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIVSLSRLMEEIVGPVGDELAEAEKD 338
Cdd:COG3448    3 TVRDIMtRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLD 72
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 221-315 3.11e-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: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 221 TLKDFLDLY--AESPMSRFPVYEDNmDNVLGILSIKDVLMALAKGTHNQQdlVDDLMRPAYFAP---ETKPIGKLFNEMR 295
Cdd:cd04639   15 TLREFADDYliGKKSWREFLVTDEA-GRLVGLITVDDLRAIPTSQWPDTP--VRELMKPLEEIPtvaADQSLLEVVKLLE 91

                         90       100
                 ....*....|....*....|
gi 499239570 296 EKNFRMCVVVDEYGGTAGIV 315
Cdd:cd04639   92 EQQLPALAVVSENGTLVGLI 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
190-262 6.35e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 36.77  E-value: 6.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499239570 190 ELLHKVFEFSDRPVREVIvpRPEVESVEKGSTLKDFLDLYAESPMSRFPVYEDNmDNVLGILSIKDVLMALAK 262
Cdd:COG0517   56 ALAAEGKDLLDTPVSEVM--TRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDD-GRLVGIITIKDLLKALLE 125
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 238-317 8.15e-03

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: 35.86  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499239570 238 PVYEDnmDNVLGILSIKD-VLMALAKGTHNQQDLVDDLM-RPAYFAPETKPIGKLFNEMREKNFRMCVVVDEYGGTAGIV 315
Cdd:cd04622   30 PVCEG--DRLVGMVTDRDiVVRAVAEGKDPNTTTVREVMtGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIV 107


                 ..
gi 499239570 316 SL 317
Cdd:cd04622  108 SL 109
 
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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