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Conserved domains on  [gi|1718055098|ref|WP_144530367|]
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hemolysin family protein [Bacillus subtilis]

Protein Classification

hemolysin family protein( domain architecture ID 11441338)

hemolysin family protein containing tandem repeats of the cystathionine beta-synthase (CBS pair) domain and a transporter-associated domain, similar to Methanoculleus thermophilus hemolysin

Gene Ontology:  GO:0016020|GO:0005886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 25-442 1.93e-163

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 467.29  E-value: 1.93e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098  25 TGFFVAVEFSIVKVRRSKIDQLVAKGKKGAKAAKHVITHLDEYLSACQLGITVAALGLGWLGEPTVQTLLRPLFHKAGLN 104
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 105 ESLTHLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPASEH 184
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 185 ElAYTEEELRVLLAESYKSGEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSLDeESISNLQETVKQTKYTRYPVVR 264
Cdd:COG1253   177 P-AVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLD-DTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 265 EDKDNVIGVINMKEVLFSMLT-KDFSIKKhqiepFVQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVED 343
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRALLEgEPFDLRD-----LLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLED 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 344 IIEEIVGEIRDEFDaDEVPHIRELGKDHYLLNAKLLISDVNSLLGTDLSDA-EVDTLGGWFLTQNID-AEPESTIEYDGY 421
Cdd:COG1253   330 ILEEIVGEIRDEYD-EEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEeDYETLGGLVLEQLGRiPEVGETVEVDGL 408

                         410       420
                  ....*....|....*....|.
gi 1718055098 422 SFKVKDINSHHILFIEVKKAE 442
Cdd:COG1253   409 RFEVLDMDGRRIDKVLVTRLP 429
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 25-442 1.93e-163

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 467.29  E-value: 1.93e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098  25 TGFFVAVEFSIVKVRRSKIDQLVAKGKKGAKAAKHVITHLDEYLSACQLGITVAALGLGWLGEPTVQTLLRPLFHKAGLN 104
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 105 ESLTHLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPASEH 184
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 185 ElAYTEEELRVLLAESYKSGEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSLDeESISNLQETVKQTKYTRYPVVR 264
Cdd:COG1253   177 P-AVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLD-DTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 265 EDKDNVIGVINMKEVLFSMLT-KDFSIKKhqiepFVQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVED 343
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRALLEgEPFDLRD-----LLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLED 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 344 IIEEIVGEIRDEFDaDEVPHIRELGKDHYLLNAKLLISDVNSLLGTDLSDA-EVDTLGGWFLTQNID-AEPESTIEYDGY 421
Cdd:COG1253   330 ILEEIVGEIRDEYD-EEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEeDYETLGGLVLEQLGRiPEVGETVEVDGL 408

                         410       420
                  ....*....|....*....|.
gi 1718055098 422 SFKVKDINSHHILFIEVKKAE 442
Cdd:COG1253   409 RFEVLDMDGRRIDKVLVTRLP 429
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 26-210 8.05e-46

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 156.99  E-value: 8.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098  26 GFFVAVEFSIVKVRRSKIDQLVAKGKKGAKAAKHVITHLDEYLSACQLGITVAALGLGWLGEPTVQTLLRPLfhkaglne 105
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 106 sltHLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPaSEHE 185
Cdd:pfam01595  83 ---GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKG-GESE 158

                         170       180
                  ....*....|....*....|....*
gi 1718055098 186 LAYTEEELRVLLAESYKSGEIRKSE 210
Cdd:pfam01595 159 PAVTEEELRSLVEESAEEGVIEEEE 183
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
221-439 3.10e-45

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 158.82  E-value: 3.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 221 DKRMaKEIMVPRNEMVSLSLDEeSISNLQETVKQTKYTRYPVVREDKDNVIGVINMKEVLFSMLTKD--FSIKKhqiepF 298
Cdd:PRK15094   66 DQRV-RDIMIPRSQMITLKRNQ-TLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAeaFSMDK-----V 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 299 VQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEIVGEIRDEFDADEVPHIRELGKDHYLLNAKL 378
Cdd:PRK15094  139 LRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALA 218

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055098 379 LISDVNSLLGTDLSDAEVDTLGGwFLTQNIDAEPE--STIEYDGYSFKVKDINSHHILFIEVK 439
Cdd:PRK15094  219 SIEDFNEAFGTHFSDEEVDTIGG-LVMQAFGHLPArgETIDIDGYQFKVAMADSRRIIQVHVK 280
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 225-346 1.44e-44

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: 151.11  E-value: 1.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 225 AKEIMVPRNEMVSLSLDEeSISNLQETVKQTKYTRYPVVREDKDNVIGVINMKEVLFSMLTKDfsiKKHQIEPFVQPVIH 304
Cdd:cd04590     2 VREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGR---EKLDLRALLRPPLF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1718055098 305 VIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIE 346
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 108-440 2.26e-40

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: 149.03  E-value: 2.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 108 THLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPAS----- 182
Cdd:TIGR03520  81 TELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQKSNisvdq 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 183 -EHELAYTEEElrvllaesyksgEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSlDEESISNLQETVKQTKYTRYP 261
Cdd:TIGR03520 161 lSQALELTDEE------------DTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALD-IETSFSEIIPKIIENGYSRIP 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 262 VVREDKDNVIGVINMKEVLFSMLTKDFSIKKHQIEPFVQPvihviETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTV 341
Cdd:TIGR03520 228 VYKETIDNITGVLYIKDLLPHLNKKNFDWQSLLREPYFVP-----ENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTL 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 342 EDIIEEIVGEIRDEFDADEVPHiRELGKDHYLLNAKLLISDVNSLLGT-----DLSDAEVDTLGGWFLTQNID-AEPEST 415
Cdd:TIGR03520 303 EDIIEEIVGDISDEFDDEDLIY-SKIDDNNYVFEGKTSLKDFYKILKLeedmfDEVKGEAETLAGFLLEISGGfPKKGEK 381

                         330       340
                  ....*....|....*....|....*
gi 1718055098 416 IEYDGYSFKVKDINSHHILFIEVKK 440
Cdd:TIGR03520 382 ITFENFEFTIEAMDKKRIKQVKVTI 406
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 365-440 8.32e-16

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: 72.09  E-value: 8.32e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055098  365 RELGKDHYLLNAKLLISDVNSLLGTDLSDAEVDTLGGWFLTQNID-AEPESTIEYDGYSFKVKDINSHHILFIEVKK 440
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRiPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 25-442 1.93e-163

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 467.29  E-value: 1.93e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098  25 TGFFVAVEFSIVKVRRSKIDQLVAKGKKGAKAAKHVITHLDEYLSACQLGITVAALGLGWLGEPTVQTLLRPLFHKAGLN 104
Cdd:COG1253    17 NGFFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 105 ESLTHLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPASEH 184
Cdd:COG1253    97 AALAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEE 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 185 ElAYTEEELRVLLAESYKSGEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSLDeESISNLQETVKQTKYTRYPVVR 264
Cdd:COG1253   177 P-AVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLD-DTLEEALELILESGHSRIPVYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 265 EDKDNVIGVINMKEVLFSMLT-KDFSIKKhqiepFVQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVED 343
Cdd:COG1253   255 GDLDDIVGVVHVKDLLRALLEgEPFDLRD-----LLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLED 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 344 IIEEIVGEIRDEFDaDEVPHIRELGKDHYLLNAKLLISDVNSLLGTDLSDA-EVDTLGGWFLTQNID-AEPESTIEYDGY 421
Cdd:COG1253   330 ILEEIVGEIRDEYD-EEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEeDYETLGGLVLEQLGRiPEVGETVEVDGL 408

                         410       420
                  ....*....|....*....|.
gi 1718055098 422 SFKVKDINSHHILFIEVKKAE 442
Cdd:COG1253   409 RFEVLDMDGRRIDKVLVTRLP 429
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 113-442 1.27e-81

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: 257.70  E-value: 1.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 113 LVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPASEHELAYTEEE 192
Cdd:COG4536    94 VAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGVKPDADASDLLSEEE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 193 LRVLLAESYKSGEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSLDeESISNLQETVKQTKYTRYPVVREDKDNVIG 272
Cdd:COG4536   174 LRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLD-DPWEEILKQLLTSPHTRLPVYRGDIDNIVG 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 273 VINMKEVLFSMLTKDFSikKHQIEPFVQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEIVGEI 352
Cdd:COG4536   253 VLHVRDLLRALRKGDLS--KEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVGEI 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 353 RDEFDADEvPHIRELGKDHYLLNAKLLISDVNSLLGTDLSDAEVDTLGGWFL--TQNIDAEPEStIEYDGYSFKVKDINS 430
Cdd:COG4536   331 TDEHDPDA-EEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIeeLEDIPEAGQS-FTIHGYRFEILQVQD 408

                         330
                  ....*....|..
gi 1718055098 431 HHILFIEVKKAE 442
Cdd:COG4536   409 NRIKTVRIRPLP 420
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 191-442 3.05e-56

Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion transport and metabolism];


Pssm-ID: 443601 [Multi-domain]  Cd Length: 288  Bit Score: 187.63  E-value: 3.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 191 EELRVLLAESYKSGEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSLDEeSISNLQETVKQTKYTRYPVVREDKDNV 270
Cdd:COG4535    31 EELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQ-PLEEILPVVIESAHSRFPVIGEDRDEV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 271 IGVINMKEVLFSMLT--KDFSIKKHqiepfVQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEI 348
Cdd:COG4535   110 IGILLAKDLLRYLAQdaEEFDLRDL-----LRPAVFVPESKRLNVLLREFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 349 VGEIRDEFDADEVP-HIRELGKDHYLLNAKLLISDVNSLLGTDLSDAEVDTLGGWfLTQNIDAEPE--STIEYDGYSFKV 425
Cdd:COG4535   185 VGEIEDEHDEDEDEdNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTIGGL-VAQEFGHLPKrgESIEIDGLRFKV 263

                         250
                  ....*....|....*..
gi 1718055098 426 KDINSHHILFIEVKKAE 442
Cdd:COG4535   264 LRADSRRIHLLRVTRLP 280
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 26-210 8.05e-46

Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal transporter proteins such as cyclin M 1/2 (CNNM). CNNMs are integral membrane proteins that are conserved from bacteria to humans. CNNM family members influence metal ion homeostasis through mechanisms that may not involve direct membrane transport of the ions. Structurally, CNNMs are complex proteins that contain an extracellular N-terminal domain preceding a transmembrane domain, a 'Bateman module', which consists of two cystathionine- beta-synthase (CBS) domains pfam00571, and a C-terminal cNMP (cyclic nucleotide monophosphate) binding domain. This entry describes the CNNM transmembrane domain which contains four hydrophobic regions and forms a dimer through hydrophobic contacts between TM2 and TM3, in which each chain is composed of three transmembrane helices (TM1-3), a pair of short helices exposed on the intracellular side, and a juxtamembrane (JM) helix that forms a belt-like structure. The homodimer adopts an inward-facing conformation with a negatively charged cavity containing a conserved pi-helical turn in TM3 that coordinates a Mg2 ion.


Pssm-ID: 460260  Cd Length: 183  Bit Score: 156.99  E-value: 8.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098  26 GFFVAVEFSIVKVRRSKIDQLVAKGKKGAKAAKHVITHLDEYLSACQLGITVAALGLGWLGEPTVQTLLRPLfhkaglne 105
Cdd:pfam01595  11 AFFSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 106 sltHLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPaSEHE 185
Cdd:pfam01595  83 ---GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKG-GESE 158

                         170       180
                  ....*....|....*....|....*
gi 1718055098 186 LAYTEEELRVLLAESYKSGEIRKSE 210
Cdd:pfam01595 159 PAVTEEELRSLVEESAEEGVIEEEE 183
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
221-439 3.10e-45

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 158.82  E-value: 3.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 221 DKRMaKEIMVPRNEMVSLSLDEeSISNLQETVKQTKYTRYPVVREDKDNVIGVINMKEVLFSMLTKD--FSIKKhqiepF 298
Cdd:PRK15094   66 DQRV-RDIMIPRSQMITLKRNQ-TLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAeaFSMDK-----V 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 299 VQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEIVGEIRDEFDADEVPHIRELGKDHYLLNAKL 378
Cdd:PRK15094  139 LRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALA 218

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055098 379 LISDVNSLLGTDLSDAEVDTLGGwFLTQNIDAEPE--STIEYDGYSFKVKDINSHHILFIEVK 439
Cdd:PRK15094  219 SIEDFNEAFGTHFSDEEVDTIGG-LVMQAFGHLPArgETIDIDGYQFKVAMADSRRIIQVHVK 280
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 225-346 1.44e-44

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: 151.11  E-value: 1.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 225 AKEIMVPRNEMVSLSLDEeSISNLQETVKQTKYTRYPVVREDKDNVIGVINMKEVLFSMLTKDfsiKKHQIEPFVQPVIH 304
Cdd:cd04590     2 VREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGR---EKLDLRALLRPPLF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1718055098 305 VIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIE 346
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 108-440 2.26e-40

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: 149.03  E-value: 2.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 108 THLLSLVIAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPAS----- 182
Cdd:TIGR03520  81 TELLRFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGKQKSNisvdq 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 183 -EHELAYTEEElrvllaesyksgEIRKSELKYMNNIFTFDKRMAKEIMVPRNEMVSLSlDEESISNLQETVKQTKYTRYP 261
Cdd:TIGR03520 161 lSQALELTDEE------------DTTKEEQKILQGIVSFGNTDTKQVMRPRLDIFALD-IETSFSEIIPKIIENGYSRIP 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 262 VVREDKDNVIGVINMKEVLFSMLTKDFSIKKHQIEPFVQPvihviETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTV 341
Cdd:TIGR03520 228 VYKETIDNITGVLYIKDLLPHLNKKNFDWQSLLREPYFVP-----ENKKLDDLLRDFQEKKNHLAIVVDEYGGTSGLVTL 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 342 EDIIEEIVGEIRDEFDADEVPHiRELGKDHYLLNAKLLISDVNSLLGT-----DLSDAEVDTLGGWFLTQNID-AEPEST 415
Cdd:TIGR03520 303 EDIIEEIVGDISDEFDDEDLIY-SKIDDNNYVFEGKTSLKDFYKILKLeedmfDEVKGEAETLAGFLLEISGGfPKKGEK 381

                         330       340
                  ....*....|....*....|....*
gi 1718055098 416 IEYDGYSFKVKDINSHHILFIEVKK 440
Cdd:TIGR03520 382 ITFENFEFTIEAMDKKRIKQVKVTI 406
PRK11573 PRK11573
hypothetical protein; Provisional
 115-433 1.52e-26

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 110.61  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 115 IAFLVVTYLNVVIGELAPKSFAIQKAESITLLFAKPLIWFYKIMFPFIWLLNHSARLITGVFGLKPASEHELAYTEEELR 194
Cdd:PRK11573   81 IATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIKTDIVVSGALSKEELR 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 195 VLLAESYKSGEIRKSELkyMNNIFTFDKRMAKEIMVPRNEMVSLSLDEESISNLQEtVKQTKYTRYPVVREDKDNVIGVI 274
Cdd:PRK11573  161 TIVHESRSQISRRNQDM--LLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQ-LTHSPHGRIVLYRDSLDDAISML 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 275 NMKEVLFSMLTKDFSIKKHQIEPfVQPVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEIVGEIRD 354
Cdd:PRK11573  238 RVREAYRLMTEKKEFTKENMLRA-ADEIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTT 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 355 EFDADEVPHIRELGKDHYLLNAKLLISDVNSLLGTDLSDAEVDTLGGWFLTQNID-AEPESTIEYDGYSFKVKDINSHHI 433
Cdd:PRK11573  317 SMSPTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEiPVAGTRVRIGEYDIDILDVQDNMI 396
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 365-440 8.32e-16

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: 72.09  E-value: 8.32e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055098  365 RELGKDHYLLNAKLLISDVNSLLGTDLSDAEVDTLGGWFLTQNID-AEPESTIEYDGYSFKVKDINSHHILFIEVKK 440
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRiPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTR 77
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 365-440 1.38e-14

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: 68.73  E-value: 1.38e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055098 365 RELGKDHYLLNAKLLISDVNSLLGTDLSDAEVDTLGGWFLTQ--NIDAEPES-TIEYDGYSFKVKDINSHHILFIEVKK 440
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERlgRIPKVGDKvEVELGGLRFTVLEMDGRRIKKVRITK 79
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 241-345 5.98e-06

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 44.93  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 241 DEESISNLQETVKQTKYTRYPVVrEDKDNVIGVINMKEVLFSMLTKDFSIKKHQIEPFVQPVIHVIETIPIYKLLLKMQK 320
Cdd:cd02205     9 PDTTVREALELMAENGIGALPVV-DDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLE 87

                          90       100
                  ....*....|....*....|....*
gi 1718055098 321 ERTHMAILIDEYGGTSGLVTVEDII 345
Cdd:cd02205    88 HGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
225-348 2.09e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.26  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 225 AKEIMVPRneMVSLSLDEeSISNLQETVKQTKYTRYPVVreDKDNVIGVINMKEVLFSMLtKDFSIKKHQIEPF-VQPVI 303
Cdd:COG2524    88 VKDIMTKD--VITVSPDT-TLEEALELMLEKGISGLPVV--DDGKLVGIITERDLLKALA-EGRDLLDAPVSDImTRDVV 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1718055098 304 HVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEI 348
Cdd:COG2524   162 TVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 241-280 3.73e-04

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 39.76  E-value: 3.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1718055098 241 DEESISNLQETVKQTKYTRYPVVreDKDN-VIGVINMKEVL 280
Cdd:cd04596     9 ETDTVRDYKQLSEETGHSRFPVV--DEENrVVGIVTAKDVI 47
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
219-346 6.40e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 39.90  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 219 TFDKRM-AKEIMVpRNEMVSLSlDEESISNLQETVKQTKYTRYPVVREDKdNVIGVINMKEVLFSMltkdfsiKKHQIEP 297
Cdd:COG4109    11 TFKEILlVEDIMT-LEDVATLS-EDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKD-------DDTPIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718055098 298 FVQ-PVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIE 346
Cdd:COG4109    81 VMTkNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS COG0517
CBS domain [Signal transduction mechanisms];
225-353 1.41e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 38.69  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055098 225 AKEIMVPRNEMVSLsldEESISNLQETVKQTKYTRYPVVREDkDNVIGVINMKEVLFSMLTKDFSIKKHQIEPFV-QPVI 303
Cdd:COG0517     3 VKDIMTTDVVTVSP---DATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMtRPPV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718055098 304 HVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEIVGEIR 353
Cdd:COG0517    79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 301-350 2.11e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718055098 301 PVIHVIETIPIYKLLLKMQKERTHMAILIDEYGGTSGLVTVEDIIEEIVG 350
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 226-280 2.62e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; 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: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 37.42  E-value: 2.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1718055098 226 KEIMvpRNEMVSLSLDEeSISNLQETVKQTKYTRYPVVREDKdnVIGVINMKEVL 280
Cdd:cd04629    65 ADYM--STEVLTVSPDT-SIVDLAQLFLKNKPRRYPVVEDGK--LVGQISRRDVL 114
 
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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