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Conserved domains on  [gi|1590321109|ref|WP_131644462|]
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HlyC/CorC family transporter [Rhizobium leguminosarum]

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 ...
 14-428 0e+00

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: 621.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  14 WPEILSITALVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFL 93
Cdd:COG4536     7 SLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  94 GLFGSSGVALATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETS 173
Cdd:COG4536    87 RLFGDAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPDADAS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 174 MLTAHEELRGAVDLLHREGSVVKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGT 253
Cdd:COG4536   167 DLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 254 IDNIIGVVHAKDLLRALAEPnmEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:COG4536   247 IDNIVGVLHVRDLLRALRKG--DLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 334 EIVGDISDEHDIEIQGVRQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVM 413
Cdd:COG4536   325 EIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEIL 404

                         410
                  ....*....|....*
gi 1590321109 414 KREKNRITKLRIRPA 428
Cdd:COG4536   405 QVQDNRIKTVRIRPL 419
 
Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 14-428 0e+00

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: 621.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  14 WPEILSITALVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFL 93
Cdd:COG4536     7 SLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  94 GLFGSSGVALATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETS 173
Cdd:COG4536    87 RLFGDAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPDADAS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 174 MLTAHEELRGAVDLLHREGSVVKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGT 253
Cdd:COG4536   167 DLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 254 IDNIIGVVHAKDLLRALAEPnmEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:COG4536   247 IDNIVGVLHVRDLLRALRKG--DLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 334 EIVGDISDEHDIEIQGVRQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVM 413
Cdd:COG4536   325 EIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEIL 404

                         410
                  ....*....|....*
gi 1590321109 414 KREKNRITKLRIRPA 428
Cdd:COG4536   405 QVQDNRIKTVRIRPL 419
PRK11573 PRK11573
hypothetical protein; Provisional
 23-427 2.97e-86

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 269.31  E-value: 2.97e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  23 LVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFLGLFGSSGVA 102
Cdd:PRK11573    1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDAGVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 103 LATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETSMLTAHEELR 182
Cdd:PRK11573   81 IATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTDIVVSGALSKEELR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 183 GAVDLLHREGSvvKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNIIGVVH 262
Cdd:PRK11573  161 TIVHESRSQIS--RRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 263 AKDLLRALAEPNmEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGDISDE 342
Cdd:PRK11573  239 VREAYRLMTEKK-EFTKENMLRAADEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 343 HDIEI-QGVRQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVMKREKNRIT 421
Cdd:PRK11573  318 MSPTLaEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIK 397


                  ....*.
gi 1590321109 422 KLRIRP 427
Cdd:PRK11573  398 QVKVTP 403
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 23-426 1.37e-71

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: 231.08  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  23 LVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFLGLFGSSGVA 102
Cdd:TIGR03520   3 LLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGSFNTE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 103 LA-----TLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGinlsRETSMLTA 177
Cdd:TIGR03520  83 LLrflieVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFG----KQKSNISV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 178 hEELRGAVDLLHREGSVvKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNI 257
Cdd:TIGR03520 159 -DQLSQALELTDEEDTT-KEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 258 IGVVHAKDLLralaePNMEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVG 337
Cdd:TIGR03520 237 TGVLYIKDLL-----PHLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 338 DISDEHDIEIQGVRQEADGSVVVDGGVPIRDLNRALDWNLP-----DEEATTIAGLVIHESMTIPEERQAFTFYGKRFVV 412
Cdd:TIGR03520 312 DISDEFDDEDLIYSKIDDNNYVFEGKTSLKDFYKILKLEEDmfdevKGEAETLAGFLLEISGGFPKKGEKITFENFEFTI 391

                         410
                  ....*....|....
gi 1590321109 413 MKREKNRITKLRIR 426
Cdd:TIGR03520 392 EAMDKKRIKQVKVT 405
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 214-333 1.86e-47

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: 158.81  E-value: 1.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 214 SDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNIIGVVHAKDLLRALAEPNmepQNLDIVKIAQKPWFVP 293
Cdd:cd04590     3 REVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGR---EKLDLRALLRPPLFVP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1590321109 294 DSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:cd04590    80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 18-192 1.24e-44

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: 153.53  E-value: 1.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  18 LSITALVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFLGLF- 96
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  97 --GSSGVALATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETSM 174
Cdd:pfam01595  81 plGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPA 160

                         170
                  ....*....|....*...
gi 1590321109 175 LTAhEELRGAVDLLHREG 192
Cdd:pfam01595 161 VTE-EELRSLVEESAEEG 177
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 351-427 1.27e-20

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: 85.57  E-value: 1.27e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590321109  351 RQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVMKREKNRITKLRIRP 427
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
 
Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 14-428 0e+00

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: 621.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  14 WPEILSITALVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFL 93
Cdd:COG4536     7 SLLIGILVLLLLLSAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  94 GLFGSSGVALATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETS 173
Cdd:COG4536    87 RLFGDAGVAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPDADAS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 174 MLTAHEELRGAVDLLHREGSVVKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGT 253
Cdd:COG4536   167 DLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 254 IDNIIGVVHAKDLLRALAEPnmEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:COG4536   247 IDNIVGVLHVRDLLRALRKG--DLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 334 EIVGDISDEHDIEIQGVRQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVM 413
Cdd:COG4536   325 EIVGEITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEIL 404

                         410
                  ....*....|....*
gi 1590321109 414 KREKNRITKLRIRPA 428
Cdd:COG4536   405 QVQDNRIKTVRIRPL 419
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 11-431 6.60e-143

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 414.90  E-value: 6.60e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  11 STYWPEILSITALVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATS 90
Cdd:COG1253     1 MSLLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  91 LFLGLFG--------------SSGVALATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAI 156
Cdd:COG1253    81 ALAALLApllgslglpaalahTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 157 VRQILSLFGINLSRETSMLTAhEELRGAVDLLHREGSVVKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVV 236
Cdd:COG1253   161 TNLLLRLLGIEPAEEEPAVTE-EELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEAL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 237 RVILESPYTRMPLWRGTIDNIIGVVHAKDLLRALAEPnmepQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVV 316
Cdd:COG1253   240 ELILESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEG----EPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVV 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 317 DEYGEVQGIVTLEDILEEIVGDISDEHDIEIQGVRQEADGSVVVDGGVPIRDLNRALDWNLPD-EEATTIAGLVIHESMT 395
Cdd:COG1253   316 DEYGGTAGLVTLEDILEEIVGEIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEeEDYETLGGLVLEQLGR 395

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1590321109 396 IPEERQAFTFYGKRFVVMKREKNRITKLRIRPAGED 431
Cdd:COG1253   396 IPEVGETVEVDGLRFEVLDMDGRRIDKVLVTRLPEE 431
PRK11573 PRK11573
hypothetical protein; Provisional
 23-427 2.97e-86

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 269.31  E-value: 2.97e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  23 LVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFLGLFGSSGVA 102
Cdd:PRK11573    1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDAGVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 103 LATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETSMLTAHEELR 182
Cdd:PRK11573   81 IATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTDIVVSGALSKEELR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 183 GAVDLLHREGSvvKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNIIGVVH 262
Cdd:PRK11573  161 TIVHESRSQIS--RRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 263 AKDLLRALAEPNmEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGDISDE 342
Cdd:PRK11573  239 VREAYRLMTEKK-EFTKENMLRAADEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 343 HDIEI-QGVRQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVMKREKNRIT 421
Cdd:PRK11573  318 MSPTLaEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIK 397


                  ....*.
gi 1590321109 422 KLRIRP 427
Cdd:PRK11573  398 QVKVTP 403
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 23-426 1.37e-71

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: 231.08  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  23 LVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFLGLFGSSGVA 102
Cdd:TIGR03520   3 LLILSALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGSFNTE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 103 LA-----TLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGinlsRETSMLTA 177
Cdd:TIGR03520  83 LLrflieVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFG----KQKSNISV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 178 hEELRGAVDLLHREGSVvKADRDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNI 257
Cdd:TIGR03520 159 -DQLSQALELTDEEDTT-KEEQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 258 IGVVHAKDLLralaePNMEPQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVG 337
Cdd:TIGR03520 237 TGVLYIKDLL-----PHLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 338 DISDEHDIEIQGVRQEADGSVVVDGGVPIRDLNRALDWNLP-----DEEATTIAGLVIHESMTIPEERQAFTFYGKRFVV 412
Cdd:TIGR03520 312 DISDEFDDEDLIYSKIDDNNYVFEGKTSLKDFYKILKLEEDmfdevKGEAETLAGFLLEISGGFPKKGEKITFENFEFTI 391

                         410
                  ....*....|....
gi 1590321109 413 MKREKNRITKLRIR 426
Cdd:TIGR03520 392 EAMDKKRIKQVKVT 405
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 179-435 1.69e-61

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: 201.11  E-value: 1.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 179 EELrgaVDLLH--REGSVVKAD-RDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTID 255
Cdd:COG4535    31 EEL---LELLRdaEERELIDADtLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 256 NIIGVVHAKDLLRALAEPNmepQNLDIVKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEI 335
Cdd:COG4535   108 EVIGILLAKDLLRYLAQDA---EEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 336 VGDISDEHDIE--IQGVRQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVM 413
Cdd:COG4535   185 VGEIEDEHDEDedEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEFGHLPKRGESIEIDGLRFKVL 264

                         250       260
                  ....*....|....*....|..
gi 1590321109 414 KREKNRITKLRIRPAGEDGAKP 435
Cdd:COG4535   265 RADSRRIHLLRVTRLPPAAEPD 286
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 214-333 1.86e-47

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: 158.81  E-value: 1.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 214 SDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNIIGVVHAKDLLRALAEPNmepQNLDIVKIAQKPWFVP 293
Cdd:cd04590     3 REVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGR---EKLDLRALLRPPLFVP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1590321109 294 DSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:cd04590    80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 18-192 1.24e-44

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: 153.53  E-value: 1.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  18 LSITALVLMSAFFSGSETALTAVSRSRVHTLEVNGDERAGLVRQLIERRDRLIGALLIGNNLANILSSSIATSLFLGLF- 96
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109  97 --GSSGVALATLAMTVILVIFAEVLPKSWAISAPERFALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETSM 174
Cdd:pfam01595  81 plGALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPA 160

                         170
                  ....*....|....*...
gi 1590321109 175 LTAhEELRGAVDLLHREG 192
Cdd:pfam01595 161 VTE-EELRSLVEESAEEG 177
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
199-426 2.41e-37

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 137.63  E-value: 2.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 199 RDRLGGVLDLSELELSDIMVHRTAMRAINADDAPEAVVRVILESPYTRMPLWRGTIDNIIGVVHAKDLLRALAEpNMEPQ 278
Cdd:PRK15094   55 RDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRS-DAEAF 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 279 NLDivKIAQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGDISDEHD-IEIQGVRQEADGS 357
Cdd:PRK15094  134 SMD--KVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDeEDDIDFRQLSRHT 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590321109 358 VVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVMKREKNRITKLRIR 426
Cdd:PRK15094  212 WTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVK 280
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 351-427 1.27e-20

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: 85.57  E-value: 1.27e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590321109  351 RQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFTFYGKRFVVMKREKNRITKLRIRP 427
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 351-427 6.46e-18

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: 77.97  E-value: 6.46e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590321109 351 RQEADGSVVVDGGVPIRDLNRALDWNLPDEEATTIAGLVIHESMTIPEERQAFT--FYGKRFVVMKREKNRITKLRIRP 427
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKVEveLGGLRFTVLEMDGRRIKKVRITK 79
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
214-342 1.96e-08

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 52.56  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 214 SDIMVHRTAmrAINADDAPEAVVRVILESPYTRMPLwrgtIDN---IIGVVHAKDLLRALAEPNMEPQNLDI--VKIAQ- 287
Cdd:COG3448     5 RDIMTRDVV--TVSPDTTLREALELMREHGIRGLPV----VDEdgrLVGIVTERDLLRALLPDRLDELEERLldLPVEDv 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1590321109 288 ---KPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGDISDE 342
Cdd:COG3448    79 mtrPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
131-335 3.45e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 53.73  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 131 FALAIALPAKLFVAVVGPVSSFVNAIVRQILSLFGINLSRETSMLTAHEELRGAVDLLHREGSVVKADRDRLGGVLDLSE 210
Cdd:COG2524     6 LLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 211 LELSDIMVHRtaMRAINADDAPEAVVRVILESPYTRMPLwrgtIDN--IIGVVHAKDLLRALAEpNMEPQNLDIVKIAQK 288
Cdd:COG2524    86 MKVKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPV----VDDgkLVGIITERDLLKALAE-GRDLLDAPVSDIMTR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1590321109 289 -PWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEI 335
Cdd:COG2524   159 dVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 226-332 1.79e-07

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 49.55  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 226 INADDAPEAVVRVILESPYTRMPLWRGTiDNIIGVVHAKDLLRALAEPnmepQNLDIVKIAQ----KPWFVPDSTNLEDQ 301
Cdd:cd02205     7 VDPDTTVREALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEG----GLALDTPVAEvmtpDVITVSPDTDLEEA 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590321109 302 LNAFLRRKQHFAVVVDEYGEVQGIVTLEDIL 332
Cdd:cd02205    82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
CBS COG0517
CBS domain [Signal transduction mechanisms];
257-336 8.46e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 47.94  E-value: 8.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 257 IIGVVHAKDLLRALAEPNMEPQNLDIVKIAQK-PWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEI 335
Cdd:COG0517    44 LVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRpPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123


                  .
gi 1590321109 336 V 336
Cdd:COG0517   124 L 124
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
214-333 2.47e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 46.83  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 214 SDIMVHRTAMRaINADDAPEAVVRVILESPYTRMPLwrgtIDN---IIGVVHAKDLLRALAepnmepqNLDIVKIAQK-P 289
Cdd:COG4109    19 EDIMTLEDVAT-LSEDDTVEDALELLEKTGHSRFPV----VDEngrLVGIVTSKDILGKDD-------DTPIEDVMTKnP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1590321109 290 WFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:COG4109    87 ITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 288-337 1.19e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 42.59  E-value: 1.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1590321109 288 KPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVG 337
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 255-334 4.55e-05

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: 42.52  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 255 DNIIGVVHAKDLLRALAEPNMepqNLDIVKI-AQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:cd04588    34 GKLVGIVTLTDIAKALAEGKE---NAKVKDImTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110


                  .
gi 1590321109 334 E 334
Cdd:cd04588   111 V 111
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
280-333 4.86e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 42.98  E-value: 4.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1590321109 280 LDIVKI-----AQKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILE 333
Cdd:COG4109    13 KEILLVedimtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG 71
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 292-332 3.25e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 38.26  E-value: 3.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1590321109  292 VPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDIL 332
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 255-332 5.62e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.81  E-value: 5.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590321109 255 DNIIGVVHAKDLLRALAEPNMEPQNLDIVKIAQKPWF-VPDSTNLEDQLNAFLRRKQHFAVVVDEyGEVQGIVTLEDIL 332
Cdd:COG2905    40 GRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPItVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
292-351 8.09e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 8.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 292 VPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGDISDEHDIEIQGVR 351
Cdd:COG3448    15 VSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLP 74
CBS COG0517
CBS domain [Signal transduction mechanisms];
288-350 5.85e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 36.77  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590321109 288 KPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGDISDEHDIEIQGV 350
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEV 72
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 291-331 6.37e-03

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


Pssm-ID: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 36.58  E-value: 6.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1590321109 291 FVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDI 331
Cdd:cd04592     7 TVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDI 47
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 212-333 8.89e-03

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


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 35.78  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590321109 212 ELSDIMVHrtamrainADDAPEAVVRVILESPYTRMPLWRGTiDNIIGVVHAKDLLRALAEPNMEpqnldiVKIAQKPWF 291
Cdd:cd04594     1 KIRDIKVS--------AYDTVERALKIMRENNLLSLPVVDND-SNFLGAVYLRDIENKSPGKVGK------YVVRGSPYV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1590321109 292 VPDSTnLEDQLNAFLRRKQHFAVVVDEyGEVQGIVTLEDILE 333
Cdd:cd04594    66 TPTSS-LEEAWEIMMRNKSRWVAVVEK-GKFLGIITLDDLLE 105
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 287-338 9.38e-03

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: 36.07  E-value: 9.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1590321109 287 QKPWFVPDSTNLEDQLNAFLRRKQHFAVVVDEYGEVQGIVTLEDILEEIVGD 338
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG 53
 
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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