NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495667922|ref|WP_008392501|]
View 

HlyC/CorC family transporter [Anaerostipes hadrus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 15-415 1.14e-156

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: 448.37  E-value: 1.14e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIATA 94
Cdd:COG4536   20 SAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAIRLFGDAGVAIATL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  95 VITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLSTAILIILRID-SKQSKRIMTERELRTIVD 173
Cdd:COG4536  100 VLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKpDADASDLLSEEELRTVVD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 174 VSHEEGVIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFKDV 253
Cdd:COG4536  180 LGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 254 YFYRSQHRGEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEYDDSEE 333
Cdd:COG4536  260 LRALRKGDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDAE 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 334 EtFKKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMETIHIIP 413
Cdd:COG4536  340 E-IRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQVQDNRIKTVRIRP 418


                 ..
gi 495667922 414 KE 415
Cdd:COG4536  419 LP 420
 
Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 15-415 1.14e-156

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: 448.37  E-value: 1.14e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIATA 94
Cdd:COG4536   20 SAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAIRLFGDAGVAIATL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  95 VITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLSTAILIILRID-SKQSKRIMTERELRTIVD 173
Cdd:COG4536  100 VLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKpDADASDLLSEEELRTVVD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 174 VSHEEGVIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFKDV 253
Cdd:COG4536  180 LGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 254 YFYRSQHRGEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEYDDSEE 333
Cdd:COG4536  260 LRALRKGDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDAE 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 334 EtFKKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMETIHIIP 413
Cdd:COG4536  340 E-IRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQVQDNRIKTVRIRP 418


                 ..
gi 495667922 414 KE 415
Cdd:COG4536  419 LP 420
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 15-409 1.17e-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: 230.70  E-value: 1.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIA-- 92
Cdd:TIGR03520   7 SALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGSFNTELLrf 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   93 ---TAVITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLStaILIILRIDSKQSKriMTERELR 169
Cdd:TIGR03520  87 lieVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAIT--NFIHKKFGKQKSN--ISVDQLS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  170 TIVDVSHEEGVIEEsEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVY 249
Cdd:TIGR03520 163 QALELTDEEDTTKE-EQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNITGVLY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  250 FKDVYFYRSQhrgEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEYD 329
Cdd:TIGR03520 242 IKDLLPHLNK---KNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  330 DsEEETFKKLSDGSYMVSASLKL-----DDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKN 404
Cdd:TIGR03520 319 D-EDLIYSKIDDNNYVFEGKTSLkdfykILKLEEDMFDEVKGEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDKK 397


                  ....*
gi 495667922  405 RMETI 409
Cdd:TIGR03520 398 RIKQV 402
PRK11573 PRK11573
hypothetical protein; Provisional
 15-416 1.12e-57

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 194.58  E-value: 1.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIATA 94
Cdd:PRK11573   5 SAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDAGVAIATG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  95 VITVLVLIFGEITPKTFATINNTKLAlsYASSIYL--ITKLLTPVVYIINKLSTAILIILRIDSK-QSKRIMTERELRTI 171
Cdd:PRK11573  85 VLTFVVLVFAEVLPKTIAALYPEKVA--YPSSFLLapLQILMMPLVWLLNTITRLLMRLMGIKTDiVVSGALSKEELRTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 172 VDVSHEEgvIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFK 251
Cdd:PRK11573 163 VHESRSQ--ISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLRVR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 252 DVyfYRSQHRGEIFHLKDVLR---KPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEY 328
Cdd:PRK11573 241 EA--YRLMTEKKEFTKENMLRaadEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTSM 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 329 DDSEEETFKKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMET 408
Cdd:PRK11573 319 SPTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQ 398


                 ....*...
gi 495667922 409 IHIIPKEQ 416
Cdd:PRK11573 399 VKVTPVKP 406
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 15-185 9.32e-56

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: 182.03  E-value: 9.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIF---GSMGAGI 91
Cdd:pfam01595  10 SAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLaplGALGVAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   92 ATAVITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLSTAILIILRIDSKQSKRIMTERELRTI 171
Cdd:pfam01595  90 ATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAVTEEELRSL 169

                         170
                  ....*....|....
gi 495667922  172 VDVSHEEGVIEESE 185
Cdd:pfam01595 170 VEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 200-318 5.78e-43

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 146.49  E-value: 5.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 200 AKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFKDVYFYRSQHRGEIFhLKDVLRKPFFTYE 279
Cdd:cd04590    2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLD-LRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495667922 280 TQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVE 318
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 337-414 5.89e-12

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: 60.92  E-value: 5.89e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495667922   337 KKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMETIHIIPK 414
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTRP 78
 
Name Accession Description Interval E-value
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 15-415 1.14e-156

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: 448.37  E-value: 1.14e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIATA 94
Cdd:COG4536   20 SAFFSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASSLATVIAIRLFGDAGVAIATL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  95 VITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLSTAILIILRID-SKQSKRIMTERELRTIVD 173
Cdd:COG4536  100 VLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKpDADASDLLSEEELRTVVD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 174 VSHEEGVIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFKDV 253
Cdd:COG4536  180 LGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 254 YFYRSQHRGEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEYDDSEE 333
Cdd:COG4536  260 LRALRKGDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEITDEHDPDAE 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 334 EtFKKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMETIHIIP 413
Cdd:COG4536  340 E-IRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQVQDNRIKTVRIRP 418


                 ..
gi 495667922 414 KE 415
Cdd:COG4536  419 LP 420
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 15-416 3.47e-146

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 422.61  E-value: 3.47e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFG--------- 85
Cdd:COG1253   17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLApllgslglp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  86 -----SMGAGIATAVITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLSTAILIILRIDSKQSK 160
Cdd:COG1253   97 aalahTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 161 RIMTERELRTIVDVSHEEGVIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGS 240
Cdd:COG1253  177 PAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGD 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 241 KDHVVGIVYFKDVyfYRSQHRGEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEI 320
Cdd:COG1253  257 LDDIVGVVHVKDL--LRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEI 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 321 FGELRDEYDDsEEETFKKLSDGSYMVSASLKLDD-LDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVV 399
Cdd:COG1253  335 VGEIRDEYDE-EEPEIVKLDDGSYLVDGRLPIDElNELLGLDLPEEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVL 413

                        410
                 ....*....|....*..
gi 495667922 400 SVDKNRMETIHIIPKEQ 416
Cdd:COG1253  414 DMDGRRIDKVLVTRLPE 430
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 15-409 1.17e-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: 230.70  E-value: 1.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIA-- 92
Cdd:TIGR03520   7 SALVSGSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILIANNFINIAIVLLFTSLSDNLFGSFNTELLrf 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   93 ---TAVITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLStaILIILRIDSKQSKriMTERELR 169
Cdd:TIGR03520  87 lieVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAIT--NFIHKKFGKQKSN--ISVDQLS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  170 TIVDVSHEEGVIEEsEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVY 249
Cdd:TIGR03520 163 QALELTDEEDTTKE-EQKILQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKIIENGYSRIPVYKETIDNITGVLY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  250 FKDVYFYRSQhrgEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEYD 329
Cdd:TIGR03520 242 IKDLLPHLNK---KNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTLEDIIEEIVGDISDEFD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  330 DsEEETFKKLSDGSYMVSASLKL-----DDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKN 404
Cdd:TIGR03520 319 D-EDLIYSKIDDNNYVFEGKTSLkdfykILKLEEDMFDEVKGEAETLAGFLLEISGGFPKKGEKITFENFEFTIEAMDKK 397


                  ....*
gi 495667922  405 RMETI 409
Cdd:TIGR03520 398 RIKQV 402
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 167-416 1.63e-58

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: 192.63  E-value: 1.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 167 ELRTIVDVSHEEGVIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVG 246
Cdd:COG4535   32 ELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 247 IVYFKDVYFYRSQHRgEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRD 326
Cdd:COG4535  112 ILLAKDLLRYLAQDA-EEFDLRDLLRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIED 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 327 EYDDSEEETF-KKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNR 405
Cdd:COG4535  191 EHDEDEDEDNiRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRR 270

                        250
                 ....*....|.
gi 495667922 406 METIHIIPKEQ 416
Cdd:COG4535  271 IHLLRVTRLPP 281
PRK11573 PRK11573
hypothetical protein; Provisional
 15-416 1.12e-57

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 194.58  E-value: 1.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIATA 94
Cdd:PRK11573   5 SAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNILASALGTIVGMRLYGDAGVAIATG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  95 VITVLVLIFGEITPKTFATINNTKLAlsYASSIYL--ITKLLTPVVYIINKLSTAILIILRIDSK-QSKRIMTERELRTI 171
Cdd:PRK11573  85 VLTFVVLVFAEVLPKTIAALYPEKVA--YPSSFLLapLQILMMPLVWLLNTITRLLMRLMGIKTDiVVSGALSKEELRTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 172 VDVSHEEgvIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFK 251
Cdd:PRK11573 163 VHESRSQ--ISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLRVR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 252 DVyfYRSQHRGEIFHLKDVLR---KPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEY 328
Cdd:PRK11573 241 EA--YRLMTEKKEFTKENMLRaadEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTSM 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 329 DDSEEETFKKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMET 408
Cdd:PRK11573 319 SPTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQ 398


                 ....*...
gi 495667922 409 IHIIPKEQ 416
Cdd:PRK11573 399 VKVTPVKP 406
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 15-185 9.32e-56

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: 182.03  E-value: 9.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   15 SAYFSSAETALTTVNPHSMRAMAEDGNKKAAIVLKLIENPSQMLSSVLVGNNLVNISLTSLTTTIAIRIF---GSMGAGI 91
Cdd:pfam01595  10 SAFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLaplGALGVAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922   92 ATAVITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTPVVYIINKLSTAILIILRIDSKQSKRIMTERELRTI 171
Cdd:pfam01595  90 ATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAVTEEELRSL 169

                         170
                  ....*....|....
gi 495667922  172 VDVSHEEGVIEESE 185
Cdd:pfam01595 170 VEESAEEGVIEEEE 183
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
167-413 4.94e-46

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 160.36  E-value: 4.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 167 ELRTIVDVSHEEGVIEESEKDMLNNVFDFKESLAKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVG 246
Cdd:PRK15094  36 ELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 247 IVYFKDVY-FYRSQhrGEIFHLKDVLRKPFFTYETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELR 325
Cdd:PRK15094 116 ILMAKDLLpFMRSD--AEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIE 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 326 DEYDDSEEETFKKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNR 405
Cdd:PRK15094 194 DEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRR 273


                 ....*....
gi 495667922 406 METIHI-IP 413
Cdd:PRK15094 274 IIQVHVkIP 282
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 200-318 5.78e-43

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 146.49  E-value: 5.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 200 AKDIMIPRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFKDVYFYRSQHRGEIFhLKDVLRKPFFTYE 279
Cdd:cd04590    2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLD-LRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495667922 280 TQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVE 318
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
199-327 1.90e-12

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 64.12  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 199 LAKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVYEgSKDHVVGIVYFKDV-------YFYRSQHRGEIFHLKDVL 271
Cdd:COG3448    3 TVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVD-EDGRLVGIVTERDLlrallpdRLDELEERLLDLPVEDVM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495667922 272 RKPFFT-YETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDE 327
Cdd:COG3448   80 TRPVVTvTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 337-414 5.89e-12

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: 60.92  E-value: 5.89e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495667922   337 KKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGETAEDEHFLFKVVSVDKNRMETIHIIPK 414
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTRP 78
CBS COG0517
CBS domain [Signal transduction mechanisms];
199-325 1.10e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 61.81  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 199 LAKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVyEGSKDHVVGIVYFKDVYFYRSQHRGEIFHLK--DVLRKPFF 276
Cdd:COG0517    2 KVKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPV-VDEDGKLVGIVTDRDLRRALAAEGKDLLDTPvsEVMTRPPV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495667922 277 T-YETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELR 325
Cdd:COG0517   79 TvSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
194-318 1.25e-10

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 58.77  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 194 DFKESL-AKDIMIpRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKdHVVGIVYFKDVYFYRSQHRgeifhLKDVLR 272
Cdd:COG4109   11 TFKEILlVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDDTP-----IEDVMT 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 495667922 273 KPFFT-YETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVE 318
Cdd:COG4109   84 KNPITvTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 337-415 2.40e-10

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: 56.40  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  337 KKLSDGSYMVSASLKLDDLDDLLDVDLDSEDYDSLGGYIIELLDHLPSEGE--TAEDEHFLFKVVSVDKNRMETIHIIPK 414
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDkvEVELGGLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 495667922  415 E 415
Cdd:pfam03471  81 E 81
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
200-320 3.10e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 59.51  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 200 AKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVYEGskDHVVGIVYFKDVYFYRSqHRGEIFHLK--DVLRKPFFT 277
Cdd:COG2524   88 VKDIMTK--DVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALA-EGRDLLDAPvsDIMTRDVVT 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 495667922 278 -YETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEI 320
Cdd:COG2524  163 vSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 209-317 5.88e-10

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: 56.48  E-value: 5.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 209 DVTFVSVDASYDEVLDIFREAGYSRLPVYEgSKDHVVGIVYFKDVYFyRSQHRGEIFHLK--DVLRKPFFT-YETQKVSS 285
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVD-DDGKLVGIVTERDILR-ALVEGGLALDTPvaEVMTPDVITvSPDTDLEE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495667922 286 LLAQMREKSVSFSIVLDEYGVTAGLITLEDIV 317
Cdd:cd02205   81 ALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
57-253 1.04e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 49.11  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922  57 MLSSVLVGNNLVNISLTSLTTTIAIRIFGSMGAGIATAVITVLVLIFGEITPKTFATINNTKLALSYASSIYLITKLLTP 136
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 137 VVYIINKLSTAILIILRIDS--KQSKRIMTERELRTIVDVSHEE--GVIeeSEKDMLNNVFDFKESL---AKDIMIPriD 209
Cdd:COG2524   84 LKMKVKDIMTKDVITVSPDTtlEEALELMLEKGISGLPVVDDGKlvGII--TERDLLKALAEGRDLLdapVSDIMTR--D 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495667922 210 VTFVSVDASYDEVLDIFREAGYSRLPVYEgSKDHVVGIVYFKDV 253
Cdd:COG2524  160 VVTVSEDDSLEEALRLMLEHGIGRLPVVD-DDGKLVGIITRTDI 202
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 161-260 1.21e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 47.13  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 161 RIMTERELRTIV---DVSHEEGVIeeSEKDMLNNVF----DFKESLAKDIMIPriDVTFVSVDASYDEVLDIFREAGYSR 233
Cdd:COG2905   23 RLMTEKGVGSLVvvdDDGRLVGII--TDRDLRRRVLaeglDPLDTPVSEVMTR--PPITVSPDDSLAEALELMEEHRIRH 98

                         90       100
                 ....*....|....*....|....*..
gi 495667922 234 LPVYEGskDHVVGIVYFKDVYFYRSQH 260
Cdd:COG2905   99 LPVVDD--GKLVGIVSITDLLRALSEE 123
CBS COG0517
CBS domain [Signal transduction mechanisms];
161-253 1.70e-06

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 46.78  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 161 RIMTERELRTIVDVSHEE---GVIeeSEKDMLNNVF----DFKESLAKDIMIPriDVTFVSVDASYDEVLDIFREAGYSR 233
Cdd:COG0517   25 ELMSEKRIGGLPVVDEDGklvGIV--TDRDLRRALAaegkDLLDTPVSEVMTR--PPVTVSPDTSLEEAAELMEEHKIRR 100

                         90       100
                 ....*....|....*....|
gi 495667922 234 LPVYEGSKdHVVGIVYFKDV 253
Cdd:COG0517  101 LPVVDDDG-RLVGIITIKDL 119
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 200-253 3.70e-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: 43.74  E-value: 3.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495667922  200 AKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVYEgSKDHVVGIVYFKDV 253
Cdd:pfam00571   1 VKDIMTK--DVVTVSPDTTLEEALELMREHGISRLPVVD-EDGKLVGIVTLKDL 51
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 200-316 2.47e-05

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 43.47  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 200 AKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKdhVVGIVYFKDVYFYRSQHRG---------EIFH---L 267
Cdd:cd17778    2 VKEFMTT--PVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK--LVGIVTAMDIVKYFGSHEAkkrlttgdiDEAYstpV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495667922 268 KDVLRKPFFTY-ETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDI 316
Cdd:cd17778   78 EEIMSKEVVTIePDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 206-253 4.59e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; 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: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 39.63  E-value: 4.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 495667922 206 PRIDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKDHVVGIVYFKDV 253
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKETGKLVGIVTRKDL 48
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 267-322 8.40e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.19  E-value: 8.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 495667922  267 LKDVLRKPFFT-YETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFG 322
Cdd:pfam00571   1 VKDIMTKDVVTvSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 209-318 1.90e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 38.08  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 209 DVTFVSVDASYDEVLDIFREAGYSRLPVYeGSKDHVVGIVYFKDV--YFYRSQHR-------GEIFHL-----KDVLRKP 274
Cdd:cd04632    3 EVITVNEDDTIGKAINLLREHGISRLPVV-DDNGKLVGIVTTYDIvdFVVRPGTKtrggdrgGEKERMldlpvYDIMSSP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495667922 275 FFTYETQK-VSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVE 318
Cdd:cd04632   82 VVTVTRDAtVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 200-248 2.29e-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: 37.40  E-value: 2.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 495667922 200 AKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSKdHVVGIV 248
Cdd:cd04622   62 VREVMTG--DVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDG-RLVGIV 107
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 200-317 4.47e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.12  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495667922 200 AKDIMIPriDVTFVSVDASYDEVLDIFREAGYSRLPVYEGSkDHVVGIVYFKDVYfYRSQHRGEIFH---LKDVLRKPFF 276
Cdd:COG2905    1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLR-RRVLAEGLDPLdtpVSEVMTRPPI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495667922 277 T-YETQKVSSLLAQMREKSVSFSIVLDEyGVTAGLITLEDIV 317
Cdd:COG2905   77 TvSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 267-329 4.60e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.12  E-value: 4.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495667922 267 LKDVLRKPFFT-YETQKVSSLLAQMREKSVSFSIVLDEYGVTAGLITLEDIVEEIFGELRDEYD 329
Cdd:COG2905    1 VKDIMSRDVVTvSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLD 64
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH