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Conserved domains on  [gi|586063394|gb|EWO71570|]
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hemolysin [Staphylococcus aureus M1272]

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 ...
 21-428 6.04e-175

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


:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 496.95  E-value: 6.04e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  21 VFVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVTSLGLGWLGEPTFEKLLHPIFEAINLPTA 100
Cdd:COG1253   19 FFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLPAA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 101 LTTTISFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVNPDAQTDA 180
Cdd:COG1253   99 LAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 181 MSEEEIKIIINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITdDGDK 260
Cdd:COG1253  179 VTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVY-EGDL 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 261 DHIKGFINVKEFLTEYASGKTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGE 340
Cdd:COG1253  258 DDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGE 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 341 IRDEFDDDEvNDIVKIDNKTFQVNGRVLLDDLTEEFGIEFDDSEDIDTIGGWLQSRNTSL-QKDDYVdtTYDRW--VVSE 417
Cdd:COG1253  338 IRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIpEVGETV--EVDGLrfEVLD 414

                        410
                 ....*....|.
gi 586063394 418 IDNHQIIWVML 428
Cdd:COG1253  415 MDGRRIDKVLV 425
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 21-428 6.04e-175

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 496.95  E-value: 6.04e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  21 VFVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVTSLGLGWLGEPTFEKLLHPIFEAINLPTA 100
Cdd:COG1253   19 FFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLPAA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 101 LTTTISFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVNPDAQTDA 180
Cdd:COG1253   99 LAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 181 MSEEEIKIIINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITdDGDK 260
Cdd:COG1253  179 VTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVY-EGDL 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 261 DHIKGFINVKEFLTEYASGKTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGE 340
Cdd:COG1253  258 DDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGE 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 341 IRDEFDDDEvNDIVKIDNKTFQVNGRVLLDDLTEEFGIEFDDSEDIDTIGGWLQSRNTSL-QKDDYVdtTYDRW--VVSE 417
Cdd:COG1253  338 IRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIpEVGETV--EVDGLrfEVLD 414

                        410
                 ....*....|.
gi 586063394 418 IDNHQIIWVML 428
Cdd:COG1253  415 MDGRRIDKVLV 425
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 22-203 5.51e-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: 183.57  E-value: 5.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394   22 FVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVTSLGLGWLGEPTFEKLLHPIfeainlptal 101
Cdd:pfam01595  13 FSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL---------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  102 tTTISFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVNPDAQTDAM 181
Cdd:pfam01595  83 -GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAV 161

                         170       180
                  ....*....|....*....|..
gi 586063394  182 SEEEIKIIINNSYNGGEINQTE 203
Cdd:pfam01595 162 TEEELRSLVEESAEEGVIEEEE 183
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 217-335 1.04e-41

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 143.79  E-value: 1.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 217 HAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITDdGDKDHIKGFINVKEFLTEYASGK-TIKIANYIHELPMIS 295
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYE-GDLDNIIGVLHVKDLLAALLEGReKLDLRALLRPPLFVP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 586063394 296 ETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILE 335
Cdd:cd04590   80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 24-426 4.69e-39

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: 145.57  E-value: 4.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394   24 GSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQ-----LGITVTSLglgwlgeptFEKLLHPIFEAINLP 98
Cdd:TIGR03520  12 GSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILiannfINIAIVLL---------FTSLSDNLFGSFNTE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394   99 TAltttiSFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFG------- 171
Cdd:TIGR03520  83 LL-----RFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGkqksnis 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  172 VNPDAQ----TD--AMSEEEIKIiinnsynggeinqtelayMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIK 245
Cdd:TIGR03520 158 VDQLSQalelTDeeDTTKEEQKI------------------LQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKII 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  246 EHQFTRYPITDDgDKDHIKGFINVKEFLTeYASGKTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTA 325
Cdd:TIGR03520 220 ENGYSRIPVYKE-TIDNITGVLYIKDLLP-HLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  326 GILTMEDILEEIVGEIRDEFDDDEVNdIVKIDNKTFQVNGRVLLDDLTEEFGIE---FDDSE-DIDTIGGWLQSRNTSL- 400
Cdd:TIGR03520 298 GLVTLEDIIEEIVGDISDEFDDEDLI-YSKIDDNNYVFEGKTSLKDFYKILKLEedmFDEVKgEAETLAGFLLEISGGFp 376

                         410       420
                  ....*....|....*....|....*...
gi 586063394  401 QKDDYVdtTYDRW--VVSEIDNHQIIWV 426
Cdd:TIGR03520 377 KKGEKI--TFENFefTIEAMDKKRIKQV 402
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
189-441 7.53e-38

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 139.17  E-value: 7.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 189 IINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITDDgDKDHIKGFIN 268
Cdd:PRK15094  40 LIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISE-DKDHIEGILM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 269 VKEFLTEYASG-KTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRDEFDD 347
Cdd:PRK15094 119 AKDLLPFMRSDaEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDE 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 348 DEVNDIVKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGW-------LQSRNTSLQKDDYvdttydRWVVSEIDN 420
Cdd:PRK15094 199 EDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSD-EEVDTIGGLvmqafghLPARGETIDIDGY------QFKVAMADS 271

                        250       260
                 ....*....|....*....|.
gi 586063394 421 HQIIWVMLNYEFNEARPTIGQ 441
Cdd:PRK15094 272 RRIIQVHVKIPDDSPQPKLDE 292
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 354-428 2.03e-11

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: 59.38  E-value: 2.03e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586063394   354 VKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGWLQSRNTSL-QKDDYVDTTYDRWVVSEIDNHQIIWVML 428
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPE-EEYDTLGGLVLEELGRIpEVGDSVEIGGLRFEVLEVDGRRIDKVRV 75
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 21-428 6.04e-175

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 496.95  E-value: 6.04e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  21 VFVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVTSLGLGWLGEPTFEKLLHPIFEAINLPTA 100
Cdd:COG1253   19 FFSASEFALVSLRRSRLEQLAEEGDKGARRALKLLEDPDRFLSTIQIGITLAGLLAGALGEAALAALLAPLLGSLGLPAA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 101 LTTTISFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVNPDAQTDA 180
Cdd:COG1253   99 LAHTLALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNGSTNLLLRLLGIEPAEEEPA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 181 MSEEEIKIIINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITdDGDK 260
Cdd:COG1253  179 VTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVY-EGDL 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 261 DHIKGFINVKEFLTEYASGKTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGE 340
Cdd:COG1253  258 DDIVGVVHVKDLLRALLEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVGE 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 341 IRDEFDDDEvNDIVKIDNKTFQVNGRVLLDDLTEEFGIEFDDSEDIDTIGGWLQSRNTSL-QKDDYVdtTYDRW--VVSE 417
Cdd:COG1253  338 IRDEYDEEE-PEIVKLDDGSYLVDGRLPIDELNELLGLDLPEEEDYETLGGLVLEQLGRIpEVGETV--EVDGLrfEVLD 414

                        410
                 ....*....|.
gi 586063394 418 IDNHQIIWVML 428
Cdd:COG1253  415 MDGRRIDKVLV 425
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 22-423 1.34e-84

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: 265.40  E-value: 1.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  22 FVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVtslglgwlgeptfekllhpifeaIN-LPTA 100
Cdd:COG4536   23 FSGSETALMALNRYRLRHLAKKGHKGAKRVLKLLERPDRLIGTILLGNNL-----------------------VNiLASS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 101 LTTTISF--------AVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGV 172
Cdd:COG4536   80 LATVIAIrlfgdagvAIATLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNLIVRGLLRLFGV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 173 NPDAQT-DAMSEEEIKIIINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTR 251
Cdd:COG4536  160 KPDADAsDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 252 YPITDDgDKDHIKGFINVKEFLTEYASGKT--IKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILT 329
Cdd:COG4536  240 LPVYRG-DIDNIVGVLHVRDLLRALRKGDLskEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVT 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 330 MEDILEEIVGEIRDEFDDDEvNDIVKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGW----LQS---RNTSLQK 402
Cdd:COG4536  319 LEDILEEIVGEITDEHDPDA-EEIRPQEDGSYLVDGSATIRDLNRALDWNLPD-DGAKTLNGLiieeLEDipeAGQSFTI 396

                        410       420
                 ....*....|....*....|.
gi 586063394 403 DDYvdttydRWVVSEIDNHQI 423
Cdd:COG4536  397 HGY------RFEILQVQDNRI 411
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 22-203 5.51e-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: 183.57  E-value: 5.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394   22 FVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVTSLGLGWLGEPTFEKLLHPIfeainlptal 101
Cdd:pfam01595  13 FSAAETALVSLRRSRLEELAEKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFAELLAPL---------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  102 tTTISFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVNPDAQTDAM 181
Cdd:pfam01595  83 -GALGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILRLFGVKGGESEPAV 161

                         170       180
                  ....*....|....*....|..
gi 586063394  182 SEEEIKIIINNSYNGGEINQTE 203
Cdd:pfam01595 162 TEEELRSLVEESAEEGVIEEEE 183
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 182-428 6.30e-52

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: 176.45  E-value: 6.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 182 SEEEIKIIINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITDDgDKD 261
Cdd:COG4535   29 DREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMVVIDIDQPLEEILPVVIESAHSRFPVIGE-DRD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 262 HIKGFINVKEFLTEYASG-KTIKIANYIHELPMISETTRIsDALIRMQRE-HVHMSLIIDEYGGTAGILTMEDILEEIVG 339
Cdd:COG4535  108 EVIGILLAKDLLRYLAQDaEEFDLRDLLRPAVFVPESKRL-NVLLREFRSnRNHMAIVVDEYGGVAGLVTIEDVLEQIVG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 340 EIRDEFDDDEVND-IVKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGWLQS-------RNTSLQKDDYvdttyd 411
Cdd:COG4535  187 EIEDEHDEDEDEDnIRPLSDGSYRVKALTPIEDFNEYFGTDFSD-EEFDTIGGLVAQefghlpkRGESIEIDGL------ 259

                        250
                 ....*....|....*..
gi 586063394 412 RWVVSEIDNHQIIWVML 428
Cdd:COG4535  260 RFKVLRADSRRIHLLRV 276
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 217-335 1.04e-41

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 143.79  E-value: 1.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 217 HAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITDdGDKDHIKGFINVKEFLTEYASGK-TIKIANYIHELPMIS 295
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYE-GDLDNIIGVLHVKDLLAALLEGReKLDLRALLRPPLFVP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 586063394 296 ETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILE 335
Cdd:cd04590   80 ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
GldE TIGR03520
gliding motility-associated protein GldE; Members of this protein family are exclusive to the ...
 24-426 4.69e-39

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: 145.57  E-value: 4.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394   24 GSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQ-----LGITVTSLglgwlgeptFEKLLHPIFEAINLP 98
Cdd:TIGR03520  12 GSEVALFSLSPTDLDDEEEDNSKKEQIVINLLDRPKKLLATILiannfINIAIVLL---------FTSLSDNLFGSFNTE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394   99 TAltttiSFAVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFG------- 171
Cdd:TIGR03520  83 LL-----RFLIEVVIVTFLILLFGEILPKVYANRNNLKFAKFMAYPINILDKLFSPISLPLRAITNFIHKKFGkqksnis 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  172 VNPDAQ----TD--AMSEEEIKIiinnsynggeinqtelayMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIK 245
Cdd:TIGR03520 158 VDQLSQalelTDeeDTTKEEQKI------------------LQGIVSFGNTDTKQVMRPRLDIFALDIETSFSEIIPKII 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  246 EHQFTRYPITDDgDKDHIKGFINVKEFLTeYASGKTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTA 325
Cdd:TIGR03520 220 ENGYSRIPVYKE-TIDNITGVLYIKDLLP-HLNKKNFDWQSLLREPYFVPENKKLDDLLRDFQEKKNHLAIVVDEYGGTS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  326 GILTMEDILEEIVGEIRDEFDDDEVNdIVKIDNKTFQVNGRVLLDDLTEEFGIE---FDDSE-DIDTIGGWLQSRNTSL- 400
Cdd:TIGR03520 298 GLVTLEDIIEEIVGDISDEFDDEDLI-YSKIDDNNYVFEGKTSLKDFYKILKLEedmFDEVKgEAETLAGFLLEISGGFp 376

                         410       420
                  ....*....|....*....|....*...
gi 586063394  401 QKDDYVdtTYDRW--VVSEIDNHQIIWV 426
Cdd:TIGR03520 377 KKGEKI--TFENFefTIEAMDKKRIKQV 402
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
189-441 7.53e-38

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 139.17  E-value: 7.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 189 IINNSYNGGEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRYPITDDgDKDHIKGFIN 268
Cdd:PRK15094  40 LIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISE-DKDHIEGILM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 269 VKEFLTEYASG-KTIKIANYIHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRDEFDD 347
Cdd:PRK15094 119 AKDLLPFMRSDaEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDE 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 348 DEVNDIVKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGW-------LQSRNTSLQKDDYvdttydRWVVSEIDN 420
Cdd:PRK15094 199 EDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSD-EEVDTIGGLvmqafghLPARGETIDIDGY------QFKVAMADS 271

                        250       260
                 ....*....|....*....|.
gi 586063394 421 HQIIWVMLNYEFNEARPTIGQ 441
Cdd:PRK15094 272 RRIIQVHVKIPDDSPQPKLDE 292
PRK11573 PRK11573
hypothetical protein; Provisional
 22-340 3.04e-28

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 115.62  E-value: 3.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394  22 FVGSEFALVKIRATRIEQLADEGNKPAKIVKKMIANLDYYLSACQLGITVTSLglgwlgeptfekllhpifeainLPTAL 101
Cdd:PRK11573   8 FSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPDRLISLVLIGNNLVNI----------------------LASAL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 102 TTTISF--------AVSFIIVTYLHVVLGELAPKSIAIQHTEKLALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVN 173
Cdd:PRK11573  66 GTIVGMrlygdagvAIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWLLNTITRLLMRLMGIK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 174 PD-AQTDAMSEEEIKIIINNSYNggEINQTELAYMQNIFSFDERHAKDIMVPRTQMITLNEPFNVDELLETIKEHQFTRY 252
Cdd:PRK11573 146 TDiVVSGALSKEELRTIVHESRS--QISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRI 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 253 PITDDGDKDHIkGFINVKE---FLTE---YASGKTIKIANYIHELPmisETTRISDALIRMQREHVHMSLIIDEYGGTAG 326
Cdd:PRK11573 224 VLYRDSLDDAI-SMLRVREayrLMTEkkeFTKENMLRAADEIYFVP---EGTPLSTQLVKFQRNKKKVGLVVDEYGDIQG 299

                        330
                 ....*....|....
gi 586063394 327 ILTMEDILEEIVGE 340
Cdd:PRK11573 300 LVTVEDILEEIVGD 313
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 354-428 9.52e-13

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: 63.33  E-value: 9.52e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586063394  354 VKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGWLQSRNTSLQK-DDYVDTTYD--RWVVSEIDNHQIIWVML 428
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPE-EDYDTLGGLVLERLGRIPKvGDKVEVELGglRFTVLEMDGRRIKKVRI 77
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 354-428 2.03e-11

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: 59.38  E-value: 2.03e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586063394   354 VKIDNKTFQVNGRVLLDDLTEEFGIEFDDsEDIDTIGGWLQSRNTSL-QKDDYVDTTYDRWVVSEIDNHQIIWVML 428
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPE-EEYDTLGGLVLEELGRIpEVGDSVEIGGLRFEVLEVDGRRIDKVRV 75
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
137-337 2.80e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 62.59  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 137 LALVYARPLFYFGNIMKPLIWLMNGSARVIIRMFGVNPDAQTDAMSEEEIKIIINNSYNGGEINQTELAYMQNIFSFDER 216
Cdd:COG2524    7 LALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 217 HAKDIMVPRtqMITLNEPFNVDELLETIKEHQFTRYPITDDGdkdHIKGFI---NVKEFLTEYASGKTIKIANYIH-ELP 292
Cdd:COG2524   87 KVKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPVVDDG---KLVGIIterDLLKALAEGRDLLDAPVSDIMTrDVV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 586063394 293 MISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEI 337
Cdd:COG2524  162 TVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 229-334 1.70e-08

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: 52.25  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 229 ITLNEPFNVDELLETIKEHQFTRYPITDDGDKdhIKGFI---NVKEFLTEYASGKTIKIANYIHELPM-ISETTRISDAL 304
Cdd:cd02205    5 VTVDPDTTVREALELMAENGIGALPVVDDDGK--LVGIVterDILRALVEGGLALDTPVAEVMTPDVItVSPDTDLEEAL 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 586063394 305 IRMQREHVHMSLIIDEYGGTAGILTMEDIL 334
Cdd:cd02205   83 ELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
217-335 1.69e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 49.91  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 217 HAKDIMVpRTQMITLNEPFNVDELLETIKEHQFTRYPITDDGDKdhIKGFINVKEFLTEYASGKTIKIANyiHELPMISE 296
Cdd:COG4109   17 LVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGR--LVGIVTSKDILGKDDDTPIEDVMT--KNPITVTP 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 586063394 297 TTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILE 335
Cdd:COG4109   92 DTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
218-344 2.08e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 49.86  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 218 AKDIMVprTQMITLNEPFNVDELLETIKEHQFTRYPITDdgDKDHIKGFINVKEFLTEYASGKTIKIANYIHELP----M 293
Cdd:COG3448    4 VRDIMT--RDVVTVSPDTTLREALELMREHGIRGLPVVD--EDGRLVGIVTERDLLRALLPDRLDELEERLLDLPvedvM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 586063394 294 ------ISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRDE 344
Cdd:COG3448   80 trpvvtVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS COG0517
CBS domain [Signal transduction mechanisms];
217-342 4.37e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 48.71  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 217 HAKDIMVPRTQMITLNEPfnVDELLETIKEHQFTRYPITDDGDKdhIKGFIN----VKEFLTEYASGKTIKIANYI-HEL 291
Cdd:COG0517    2 KVKDIMTTDVVTVSPDAT--VREALELMSEKRIGGLPVVDEDGK--LVGIVTdrdlRRALAAEGKDLLDTPVSEVMtRPP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 586063394 292 PMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIR 342
Cdd:COG0517   78 VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 293-336 3.61e-06

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


Pssm-ID: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 46.02  E-value: 3.61e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 586063394 293 MISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEE 336
Cdd:cd04640    9 TIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGE 52
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 289-339 1.35e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 42.59  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 586063394  289 HELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVG 339
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 289-353 1.89e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 44.05  E-value: 1.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586063394 289 HELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRDeFDDDEVNDI 353
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLD-PLDTPVSEV 70
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 225-336 1.16e-04

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 41.36  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 225 RTQMITLNEPFNVDELLETIKEHQFTRYPITDDGdkdHIKGFINVKEFLTEYASGK-TIKIANYI-HELPMISETTRISD 302
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDG---KLVGIVTLTDIAKALAEGKeNAKVKDIMtKDVITIDKDEKIYD 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 586063394 303 ALIRMQREHVHMSLIIDEYGGTAGILTMEDILEE 336
Cdd:cd04588   78 AIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 218-334 3.17e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 40.20  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 218 AKDIMvpRTQMITLNEPFNVDELLETIKEHQFTRYPITDDGDKdhIKGFIN----VKEFLTEYASGKTIKIANY-IHELP 292
Cdd:COG2905    1 VKDIM--SRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGR--LVGIITdrdlRRRVLAEGLDPLDTPVSEVmTRPPI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 586063394 293 MISETTRISDALIRMQREHVHmSLIIDEYGGTAGILTMEDIL 334
Cdd:COG2905   77 TVSPDDSLAEALELMEEHRIR-HLPVVDDGKLVGIVSITDLL 117
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 220-334 5.14e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 39.47  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586063394 220 DIMVPRTQMITLNepFNVDELLETIKEHQFTRYPITDDGdkdHIKGFI------NVKEflTEYASGKTIKIANyiHELPM 293
Cdd:cd04801    1 DIMTPEVVTVTPE--MTVSELLDRMFEEKHLGYPVVENG---RLVGIVtledirKVPE--VEREATRVRDVMT--KDVIT 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 586063394 294 ISETTRISDALIRMQREHVHMSLIIDEyGGTAGILTMEDIL 334
Cdd:cd04801   72 VSPDADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
288-346 6.77e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.46  E-value: 6.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586063394 288 IHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRDEFD 346
Cdd:COG0517    8 TTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLD 66
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
288-355 1.36e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 38.69  E-value: 1.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586063394 288 IHELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRDEFDDDEVNDIVK 355
Cdd:COG3448    9 TRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVE 76
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 289-353 2.30e-03

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 37.61  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586063394 289 HELPMISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGeiRDEFDDDEVNDI 353
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE--GGLALDTPVAEV 64
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 294-343 5.20e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. 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: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 36.80  E-value: 5.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 586063394 294 ISETTRISDALIRMQREHVHMSLIIDEYGGTAGILTMEDILEEIVGEIRD 343
Cdd:cd17781    7 VPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLD 56
CBS COG0517
CBS domain [Signal transduction mechanisms];
212-277 7.92e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 36.38  E-value: 7.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586063394 212 SFDERHAKDIMvpRTQMITLNEPFNVDELLETIKEHQFTRYPITDDGDKdhIKGFINVKEFLTEYA 277
Cdd:COG0517   63 DLLDTPVSEVM--TRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGR--LVGIITIKDLLKALL 124
 
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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