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Conserved domains on  [gi|501624767|ref|WP_012603382|]
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MULTISPECIES: CNNM family magnesium/cobalt transport protein CorC [Vibrio]

Protein Classification

HlyC/CorC family transporter( domain architecture ID 11468252)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 1-295 4.54e-161

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: 449.56  E-value: 4.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767   1 MNEGNPptsegskkSEGPSRKSFFERLGQLFQGEVKDRQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPR 80
Cdd:COG4535    1 MSDDRP--------SSGSSKRSWLERLSQLFSGEPEDREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  81 SQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPESKRVDRLLK 160
Cdd:COG4535   73 SQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAEEFDLRDLLRPAVFVPESKRLNVLLR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 161 EFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVGE-IEDEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDE 239
Cdd:COG4535  153 EFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEiEDEHDEDEDEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEE 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501624767 240 VDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIPDEQPLPTIE 295
Cdd:COG4535  233 FDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTRLPPAAEPDAE 288
 
Name Accession Description Interval E-value
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 1-295 4.54e-161

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: 449.56  E-value: 4.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767   1 MNEGNPptsegskkSEGPSRKSFFERLGQLFQGEVKDRQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPR 80
Cdd:COG4535    1 MSDDRP--------SSGSSKRSWLERLSQLFSGEPEDREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  81 SQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPESKRVDRLLK 160
Cdd:COG4535   73 SQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAEEFDLRDLLRPAVFVPESKRLNVLLR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 161 EFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVGE-IEDEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDE 239
Cdd:COG4535  153 EFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEiEDEHDEDEDEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEE 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501624767 240 VDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIPDEQPLPTIE 295
Cdd:COG4535  233 FDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTRLPPAAEPDAE 288
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
12-296 3.20e-134

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 381.85  E-value: 3.20e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  12 SKKSEGPS-RKSFFE-RLGQLFQGEVKDRQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPRSQMVTVERT 89
Cdd:PRK15094   6 SHSSDTPSpKKGFFSlLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  90 DDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPESKRVDRLLKEFQEERYHM 169
Cdd:PRK15094  86 QTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 170 SIVVDEFGGVSGLVTIEDILEEIVGEIEDEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMT 249
Cdd:PRK15094 166 AIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQ 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 501624767 250 ALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIPDEQPLPTIEE 296
Cdd:PRK15094 246 AFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPDDSPQPKLDE 292
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 72-190 1.66e-48

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: 157.27  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  72 RVRDIMLPRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPE 151
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501624767 152 SKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILE 190
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 209-286 6.04e-24

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: 92.50  E-value: 6.04e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501624767   209 RKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIP 286
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTRP 78
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 209-287 2.05e-19

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: 80.67  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  209 RKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMTALGHLPVRGEIVEIE--NYHFKITSADNRRVIQLQVTIP 286
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKVEVElgGLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 501624767  287 D 287
Cdd:pfam03471  81 E 81
 
Name Accession Description Interval E-value
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
 1-295 4.54e-161

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: 449.56  E-value: 4.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767   1 MNEGNPptsegskkSEGPSRKSFFERLGQLFQGEVKDRQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPR 80
Cdd:COG4535    1 MSDDRP--------SSGSSKRSWLERLSQLFSGEPEDREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  81 SQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPESKRVDRLLK 160
Cdd:COG4535   73 SQMVVIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAEEFDLRDLLRPAVFVPESKRLNVLLR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 161 EFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVGE-IEDEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDE 239
Cdd:COG4535  153 EFRSNRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEiEDEHDEDEDEDNIRPLSDGSYRVKALTPIEDFNEYFGTDFSDEE 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501624767 240 VDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIPDEQPLPTIE 295
Cdd:COG4535  233 FDTIGGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTRLPPAAEPDAE 288
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
12-296 3.20e-134

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 381.85  E-value: 3.20e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  12 SKKSEGPS-RKSFFE-RLGQLFQGEVKDRQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPRSQMVTVERT 89
Cdd:PRK15094   6 SHSSDTPSpKKGFFSlLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  90 DDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPESKRVDRLLKEFQEERYHM 169
Cdd:PRK15094  86 QTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRSQRYHM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 170 SIVVDEFGGVSGLVTIEDILEEIVGEIEDEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMT 249
Cdd:PRK15094 166 AIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIGGLVMQ 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 501624767 250 ALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIPDEQPLPTIEE 296
Cdd:PRK15094 246 AFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPDDSPQPKLDE 292
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 38-290 3.81e-92

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 279.70  E-value: 3.81e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  38 RQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHV 117
Cdd:COG1253  181 EEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELILESGHSRIPVYEGDLDDI 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 118 EGILLAKDLLKYLgSESAPFDIEQVIRPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVGeIE 197
Cdd:COG1253  261 VGVVHVKDLLRAL-LEGEPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIVG-EI 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 198 DEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAF-SDDEVDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNR 276
Cdd:COG1253  339 RDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIPEVGETVEVDGLRFEVLDMDGR 418

                        250
                 ....*....|....
gi 501624767 277 RVIQLQVTIPDEQP 290
Cdd:COG1253  419 RIDKVLVTRLPEEE 432
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 38-287 5.63e-66

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: 212.24  E-value: 5.63e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  38 RQELVDVIRDSEINDLIDHDTRDMLEGVMEISEMRVRDIMLPRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHV 117
Cdd:COG4536  171 EEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEEILKQLLTSPHTRLPVYRGDIDNI 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 118 EGILLAKDLLKYLGSESA-PFDIEQVIRPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVGeI 196
Cdd:COG4536  251 VGVLHVRDLLRALRKGDLsKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVVDEYGDVQGLVTLEDILEEIVG-E 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 197 EDEFDDEEELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNR 276
Cdd:COG4536  330 ITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELEDIPEAGQSFTIHGYRFEILQVQDN 409

                        250
                 ....*....|.
gi 501624767 277 RVIQLQVTIPD 287
Cdd:COG4536  410 RIKTVRIRPLP 420
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 72-190 1.66e-48

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: 157.27  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  72 RVRDIMLPRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVPE 151
Cdd:cd04590    1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501624767 152 SKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILE 190
Cdd:cd04590   81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
PRK11573 PRK11573
hypothetical protein; Provisional
 48-284 1.87e-29

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 115.62  E-value: 1.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  48 SEINDLIDHDTRDMLEGVMEISEMRVRDIMLPRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKDHVEGILLAKDLL 127
Cdd:PRK11573 164 HESRSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDAISMLRVREAY 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 128 KyLGSESAPFDIEQVIRP---VVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVGEIEDEFDDEE 204
Cdd:PRK11573 244 R-LMTEKKEFTKENMLRAadeIYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVGDFTTSMSPTL 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 205 ELDIRKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVT 284
Cdd:PRK11573 323 AEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQVKVT 402
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
 209-286 6.04e-24

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: 92.50  E-value: 6.04e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501624767   209 RKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMTALGHLPVRGEIVEIENYHFKITSADNRRVIQLQVTIP 286
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTRP 78
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
 209-287 2.05e-19

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: 80.67  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  209 RKLSKHTFSVKALTTIEEFNDTFNTAFSDDEVDTVGGMVMTALGHLPVRGEIVEIE--NYHFKITSADNRRVIQLQVTIP 286
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDKVEVElgGLRFTVLEMDGRRIKKVRITKL 80


                  .
gi 501624767  287 D 287
Cdd:pfam03471  81 E 81
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
65-192 3.49e-12

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 64.13  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  65 VMEISEMRVRDIMLPRsqMVTVERTDDLDTLIALITDAQHSRYPVIseDKDHVEGILLAKDLLKYLGSESAPFD--IEQV 142
Cdd:COG2524   80 LGLVLKMKVKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPVV--DDGKLVGIITERDLLKALAEGRDLLDapVSDI 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501624767 143 I-RPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEI 192
Cdd:COG2524  156 MtRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
71-193 1.47e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 60.65  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  71 MRVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDkDHVEGILLAKDLLKYLGSESAPFD---IEQVI-RPV 146
Cdd:COG0517    1 MKVKDIM--TTDVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRRALAAEGKDLLdtpVSEVMtRPP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501624767 147 VVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIV 193
Cdd:COG0517   78 VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
71-189 1.17e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 58.34  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  71 MRVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDkDHVEGILLAKDLLKYLGSES--------APFDIEQV 142
Cdd:COG3448    2 MTVRDIM--TRDVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLPDRldeleerlLDLPVEDV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 501624767 143 -IRPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDIL 189
Cdd:COG3448   79 mTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLL 126
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 84-189 4.53e-10

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 56.10  E-value: 4.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  84 VTVERTDDLDTLIALITDAQHSRYPVIsEDKDHVEGILLAKDLLKYLGSESAPFDI---EQVIRPVVVVPESKRVDRLLK 160
Cdd:cd02205    5 VTVDPDTTVREALELMAENGIGALPVV-DDDGKLVGIVTERDILRALVEGGLALDTpvaEVMTPDVITVSPDTDLEEALE 83

                         90       100
                 ....*....|....*....|....*....
gi 501624767 161 EFQEERYHMSIVVDEFGGVSGLVTIEDIL 189
Cdd:cd02205   84 LMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
65-190 1.01e-09

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 55.69  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  65 VMEIseMRVRDIMLpRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKdHVEGILLAKDLLKYLGSESapfdIEQVI- 143
Cdd:COG4109   12 FKEI--LLVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDDTP----IEDVMt 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501624767 144 RPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILE 190
Cdd:COG4109   84 KNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 73-189 7.40e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 50.21  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  73 VRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVIsEDKDHVEGILLAKDLLKYLGSESAPFD---IEQV-IRPVVV 148
Cdd:COG2905    1 VKDIM--SRDVVTVSPDATVREAARLMTEKGVGSLVVV-DDDGRLVGIITDRDLRRRVLAEGLDPLdtpVSEVmTRPPIT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501624767 149 VPESKRVDRLLKEFQEERYHMSIVVDEfGGVSGLVTIEDIL 189
Cdd:COG2905   78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 72-189 9.15e-07

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 47.33  E-value: 9.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  72 RVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDKdhVEGILLAKDLLKYLGSESA-----PFDIEQVI--- 143
Cdd:cd17778    1 KVKEFM--TTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK--LVGIVTAMDIVKYFGSHEAkkrltTGDIDEAYstp 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501624767 144 ------RPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDIL 189
Cdd:cd17778   77 veeimsKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
52-130 9.77e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.17  E-value: 9.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  52 DLIDHDTRDML-EGVMEISEMRVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDkDHVEGILLAKDLLKYL 130
Cdd:COG3448   53 DLLRALLPDRLdELEERLLDLPVEDVM--TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLRAL 129
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 75-190 5.72e-06

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


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 44.48  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  75 DIMLPRSQMVTVERTddLDTLI--ALITDAQHSRYPVISEDkDHVEGILLAKDLLKYLGSESAPFDIEQVIRPVVVVP-- 150
Cdd:cd04639    1 DAMVTEFPIVDADLT--LREFAddYLIGKKSWREFLVTDEA-GRLVGLITVDDLRAIPTSQWPDTPVRELMKPLEEIPtv 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501624767 151 -ESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILE 190
Cdd:cd04639   78 aADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIE 118
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 144-194 1.29e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.82  E-value: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501624767  144 RPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVG 194
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 73-130 1.88e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 41.43  E-value: 1.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 501624767   73 VRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVISEDkDHVEGILLAKDLLKYL 130
Cdd:pfam00571   1 VKDIM--TKDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRAL 55
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
55-130 4.36e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 43.72  E-value: 4.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501624767  55 DHDTRDMLEGVMEISEMRVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVIsEDKDHVEGILLAKDLLKYL 130
Cdd:COG2524  134 ERDLLKALAEGRDLLDAPVSDIM--TRDVVTVSEDDSLEEALRLMLEHGIGRLPVV-DDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 59-134 8.36e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.66  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  59 RDMLEGVME----ISEMRVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPVIseDKDHVEGILLAKDLLKYLGSES 134
Cdd:COG2905   49 RDLRRRVLAegldPLDTPVSEVM--TRPPITVSPDDSLAEALELMEEHRIRHLPVV--DDGKLVGIVSITDLLRALSEEL 124
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 138-191 4.06e-03

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: 36.77  E-value: 4.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501624767 138 DIEQVirPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEE 191
Cdd:cd04640    1 DFRRV--PPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGE 52
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 35-129 5.56e-03

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 36.16  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767  35 VKDRQELVDVIRDSEINDLIDHDTRDMLEG-----VMEISEMRVRDIMlpRSQMVTVERTDDLDTLIALITDAQHSRYPV 109
Cdd:cd04632   31 VDDNGKLVGIVTTYDIVDFVVRPGTKTRGGdrggeKERMLDLPVYDIM--SSPVVTVTRDATVADAVERMLENDISGLVV 108

                         90       100
                 ....*....|....*....|
gi 501624767 110 ISEDkDHVEGILLAKDLLKY 129
Cdd:cd04632  109 TPDD-NMVIGILTKTDVLRA 127
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
143-226 5.57e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 36.38  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 143 IRPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIV-GEIEDEFDDEEELDIRKL-SKHTFSVKA 220
Cdd:COG3448    9 TRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLpDRLDELEERLLDLPVEDVmTRPVVTVTP 88


                 ....*.
gi 501624767 221 LTTIEE 226
Cdd:COG3448   89 DTPLEE 94
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 109-192 6.82e-03

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 35.60  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501624767 109 VISEDKDHVEGILLAKDLLKYLGSESAPFD---IEQVI-RPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVT 184
Cdd:cd17775   30 VVVEEDGKPVGIVTDRDIVVEVVAKGLDPKdvtVGDIMsADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVT 109


                 ....*...
gi 501624767 185 IEDILEEI 192
Cdd:cd17775  110 LDDILELL 117
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 144-194 7.71e-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: 35.68  E-value: 7.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501624767 144 RPVVVVPESKRVDRLLKEFQEERYHMSIVVDEFGGVSGLVTIEDILEEIVG 194
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE 52
 
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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