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Conserved domains on  [gi|61221144|sp|P0A2L4|]
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RecName: Full=Magnesium and cobalt efflux protein CorC

Protein Classification

HlyC/CorC family transporter( domain architecture ID 11487637)

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
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
1-292 0e+00

magnesium/cobalt transporter CorC;


:

Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 578.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144    1 MSDDNSHSSDTVNSKKGFFSLLLSQLFHGEPKNRDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
Cdd:PRK15094   1 MSDDNSHSSDTPSPKKGFFSLLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRS 160
Cdd:PRK15094  81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIG 240
Cdd:PRK15094 161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61221144  241 GLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPKLDE 292
Cdd:PRK15094 241 GLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPDDSPQPKLDE 292
 
Name Accession Description Interval E-value
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
1-292 0e+00

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 578.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144    1 MSDDNSHSSDTVNSKKGFFSLLLSQLFHGEPKNRDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
Cdd:PRK15094   1 MSDDNSHSSDTPSPKKGFFSLLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRS 160
Cdd:PRK15094  81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIG 240
Cdd:PRK15094 161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61221144  241 GLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPKLDE 292
Cdd:PRK15094 241 GLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPDDSPQPKLDE 292
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
1-291 6.85e-168

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: 466.51  E-value: 6.85e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   1 MSDDNSHSSdtvNSKKGFFSLLlSQLFHGEPKNRDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
Cdd:COG4535   1 MSDDRPSSG---SSKRSWLERL-SQLFSGEPEDREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRS 160
Cdd:COG4535  77 VIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAEEFDLRDLLRPAVFVPESKRLNVLLREFRS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144 161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDF-RQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTI 239
Cdd:COG4535 157 NRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIEDEHDEDEDEDNiRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTI 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 61221144 240 GGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPKLD 291
Cdd:COG4535 237 GGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTRLPPAAEPDAE 288
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
68-186 5.64e-49

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 158.43  E-value: 5.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  68 RVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPE 147
Cdd:cd04590   1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 61221144 148 SKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILE 186
Cdd:cd04590  81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
205-282 3.75e-26

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: 98.28  E-value: 3.75e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61221144    205 RQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIP 282
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTRP 78
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
205-283 3.45e-21

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: 85.29  E-value: 3.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   205 RQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGHLPARGE--TIDIDGYQFKVAMADSRRIIQVHVRIP 282
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDkvEVELGGLRFTVLEMDGRRIKKVRITKL 80

                  .
gi 61221144   283 D 283
Cdd:pfam03471  81 E 81
 
Name Accession Description Interval E-value
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
1-292 0e+00

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 578.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144    1 MSDDNSHSSDTVNSKKGFFSLLLSQLFHGEPKNRDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
Cdd:PRK15094   1 MSDDNSHSSDTPSPKKGFFSLLLSQLFHGEPKNRDELLALIRDSEQNDLIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRS 160
Cdd:PRK15094  81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRQAVVVPESKRVDRMLKEFRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIG 240
Cdd:PRK15094 161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTVRALASIEDFNEAFGTHFSDEEVDTIG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61221144  241 GLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPKLDE 292
Cdd:PRK15094 241 GLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVKIPDDSPQPKLDE 292
CorC COG4535
Mg2+ and Co2+ transporter CorC, contains CBS pair and CorC-HlyC domains [Inorganic ion ...
1-291 6.85e-168

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: 466.51  E-value: 6.85e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   1 MSDDNSHSSdtvNSKKGFFSLLlSQLFHGEPKNRDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMI 80
Cdd:COG4535   1 MSDDRPSSG---SSKRSWLERL-SQLFSGEPEDREELLELLRDAEERELIDADTLSMIEGVLQVSELRVRDIMIPRSQMV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  81 TLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRS 160
Cdd:COG4535  77 VIDIDQPLEEILPVVIESAHSRFPVIGEDRDEVIGILLAKDLLRYLAQDAEEFDLRDLLRPAVFVPESKRLNVLLREFRS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144 161 QRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDF-RQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTI 239
Cdd:COG4535 157 NRNHMAIVVDEYGGVAGLVTIEDVLEQIVGEIEDEHDEDEDEDNiRPLSDGSYRVKALTPIEDFNEYFGTDFSDEEFDTI 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 61221144 240 GGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPKLD 291
Cdd:COG4535 237 GGLVAQEFGHLPKRGESIEIDGLRFKVLRADSRRIHLLRVTRLPPAAEPDAE 288
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
22-289 2.07e-92

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 280.47  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  22 LLSQLFHGEPKN------RDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVI 95
Cdd:COG1253 163 LLLRLLGIEPAEeepavtEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEEALELI 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  96 IESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDaEAFSMDKVLRTAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGV 175
Cdd:COG1253 243 LESGHSRIPVYEGDLDDIVGVVHVKDLLRALLEG-EPFDLRDLLRPPLFVPETKPLDDLLEEFRRERVHMAIVVDEYGGT 321
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144 176 SGLVTIEDILELIVGeIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHF-SDEEVDTIGGLVMQAFGHLPARG 254
Cdd:COG1253 322 AGLVTLEDILEEIVG-EIRDEYDEEEPEIVKLDDGSYLVDGRLPIDELNELLGLDLpEEEDYETLGGLVLEQLGRIPEVG 400
                       250       260       270
                ....*....|....*....|....*....|....*
gi 61221144 255 ETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPK 289
Cdd:COG1253 401 ETVEVDGLRFEVLDMDGRRIDKVLVTRLPEEEEEE 435
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
18-283 2.49e-64

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: 207.62  E-value: 2.49e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  18 FFSLLLSQLFHGEPKN-------RDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDE 90
Cdd:COG4536 148 LIVRGLLRLFGVKPDAdasdllsEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEE 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  91 CLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMR-SDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRSQRYHMAIVI 169
Cdd:COG4536 228 ILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLLRALRkGDLSKEDLRKIAREPYFIPETTPLSTQLQNFQKRKRRFALVV 307
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144 170 DEFGGVSGLVTIEDILELIVGeIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGH 249
Cdd:COG4536 308 DEYGDVQGLVTLEDILEEIVG-EITDEHDPDAEEIRPQEDGSYLVDGSATIRDLNRALDWNLPDDGAKTLNGLIIEELED 386
                       250       260       270
                ....*....|....*....|....*....|....
gi 61221144 250 LPARGETIDIDGYQFKVAMADSRRIIQVHVRIPD 283
Cdd:COG4536 387 IPEAGQSFTIHGYRFEILQVQDNRIKTVRIRPLP 420
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
68-186 5.64e-49

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 158.43  E-value: 5.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  68 RVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPE 147
Cdd:cd04590   1 TVREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALLRPPLFVPE 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 61221144 148 SKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILE 186
Cdd:cd04590  81 TTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDILE 119
CorC_HlyC smart01091
Transporter associated domain; This small domain is found in a family of proteins with the ...
205-282 3.75e-26

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: 98.28  E-value: 3.75e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61221144    205 RQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIP 282
Cdd:smart01091   1 VKLDDGSYLVDGRTPIDDLNELLGLDLPEEEYDTLGGLVLEELGRIPEVGDSVEIGGLRFEVLEVDGRRIDKVRVTRP 78
PRK11573 PRK11573
hypothetical protein; Provisional
34-280 4.30e-25

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 103.29  E-value: 4.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   34 RDELLALIRDSgqNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHI 113
Cdd:PRK11573 156 KEELRTIVHES--RSQISRRNQDMLLSVLDLEKVTVDDIMVPRNEIVGIDINDDWKSILRQLTHSPHGRIVLYRDSLDDA 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  114 EGILMAKDLLPFMRSDAEaFSMDKVLRTA---VVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVG 190
Cdd:PRK11573 234 ISMLRVREAYRLMTEKKE-FTKENMLRAAdeiYFVPEGTPLSTQLVKFQRNKKKVGLVVDEYGDIQGLVTVEDILEEIVG 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  191 EIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMAD 270
Cdd:PRK11573 313 DFTTSMSPTLAEEVTPQNDGSVIIDGTANVREINKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQ 392
                        250
                 ....*....|
gi 61221144  271 SRRIIQVHVR 280
Cdd:PRK11573 393 DNMIKQVKVT 402
CorC_HlyC pfam03471
Transporter associated domain; This small domain is found in a family of proteins with the ...
205-283 3.45e-21

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: 85.29  E-value: 3.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144   205 RQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGHLPARGE--TIDIDGYQFKVAMADSRRIIQVHVRIP 282
Cdd:pfam03471   1 EKLDDGSYLVDGRAPLDDLNELLGLELPEEDYDTLGGLVLERLGRIPKVGDkvEVELGGLRFTVLEMDGRRIKKVRITKL 80

                  .
gi 61221144   283 D 283
Cdd:pfam03471  81 E 81
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
61-188 2.55e-12

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 64.52  E-value: 2.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  61 VMDIADQRVRDIMIPRsqMITLKRNQTLDECLDVIIESAHSRFPVIseDKDHIEGILMAKDLLPFMRSDAEAFSM---DK 137
Cdd:COG2524  80 LGLVLKMKVKDIMTKD--VITVSPDTTLEEALELMLEKGISGLPVV--DDGKLVGIITERDLLKALAEGRDLLDApvsDI 155
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 61221144 138 VLRTAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELI 188
Cdd:COG2524 156 MTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
68-189 3.01e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 56.80  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  68 RVRDIMIprSQMITLKRNQTLDECLDVIIESAHSRFPVISEDkDHIEGILMAKDLLPFMRSDAEAFSMDKV----LRTAV 143
Cdd:COG0517   2 KVKDIMT--TDVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRRALAAEGKDLLDTPVsevmTRPPV 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 61221144 144 VVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIV 189
Cdd:COG0517  79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
68-186 1.37e-09

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 55.30  E-value: 1.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  68 RVRDIMIpRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKdHIEGILMAKDLLPFMRSDaeafSMDKVL-RTAVVVP 146
Cdd:COG4109  17 LVEDIMT-LEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDDT----PIEDVMtKNPITVT 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 61221144 147 ESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILE 186
Cdd:COG4109  91 PDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
68-189 2.59e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 54.49  E-value: 2.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  68 RVRDIMIPrsQMITLKRNQTLDECLDVIIESAHSRFPVISEDkDHIEGILMAKDLLPFMRSDAEAFSMDKVLRT------ 141
Cdd:COG3448   3 TVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLPDRLDELEERLLDLpvedvm 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 61221144 142 ---AVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIV 189
Cdd:COG3448  80 trpVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
80-185 9.45e-09

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: 9.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  80 ITLKRNQTLDECLDVIIESAHSRFPVIsEDKDHIEGILMAKDLL--PFMRSDAEAFSMDKVLRTAVV-VPESKRVDRMLK 156
Cdd:cd02205   5 VTVDPDTTVREALELMAENGIGALPVV-DDDGKLVGIVTERDILraLVEGGLALDTPVAEVMTPDVItVSPDTDLEEALE 83
                        90       100
                ....*....|....*....|....*....
gi 61221144 157 EFRSQRYHMAIVIDEFGGVSGLVTIEDIL 185
Cdd:cd02205  84 LMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
69-123 6.99e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 42.59  E-value: 6.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 61221144    69 VRDIMipRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDkDHIEGILMAKDLL 123
Cdd:pfam00571   1 VKDIM--TKDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLL 52
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
71-188 8.20e-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: 44.10  E-value: 8.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  71 DIMIPRSQmiTLKRNQTLDECLD--VIIESAHSRFPVISEDkDHIEGILMAKDLLPFMRSDAEAFSMDKVLRT---AVVV 145
Cdd:cd04639   1 DAMVTEFP--IVDADLTLREFADdyLIGKKSWREFLVTDEA-GRLVGLITVDDLRAIPTSQWPDTPVRELMKPleeIPTV 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 61221144 146 PESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELI 188
Cdd:cd04639  78 AADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIELL 120
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
69-188 4.27e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.12  E-value: 4.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61221144  69 VRDIMipRSQMITLKRNQTLDECLDVIIESAHSRFPVIsEDKDHIEGILMAKDLLPFMRSDAEAFSMDKV----LRTAVV 144
Cdd:COG2905   1 VKDIM--SRDVVTVSPDATVREAARLMTEKGVGSLVVV-DDDGRLVGIITDRDLRRRVLAEGLDPLDTPVsevmTRPPIT 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61221144 145 VPESKRVDRMLKEFRSQRYHMAIVIDEfGGVSGLVTIEDILELI 188
Cdd:COG2905  78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRAL 120
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
66-123 2.04e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 40.09  E-value: 2.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 61221144  66 DQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISeDKDHIEGILMAKDLL 123
Cdd:cd04601  53 STPVSEVMTPDERLVTAPEGITLEEAKEILHKHKIEKLPIVD-DNGELVGLITRKDIE 109
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
69-126 4.31e-04

signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. 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: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 39.52  E-value: 4.31e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 61221144  69 VRDIMipRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDkDHIEGILMAKDLLPFM 126
Cdd:cd17779  82 VREIM--TRDVISVKENASIDDAIELMLEKNVGGLPIVDKD-GKVIGIVTERDFLKFL 136
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
55-123 4.58e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 4.58e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61221144  55 RDMLEGVMDIADQRVRDIMipRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDkDHIEGILMAKDLL 123
Cdd:COG3448  61 DRLDELEERLLDLPVEDVM--TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLL 126
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
143-190 5.16e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.58  E-value: 5.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 61221144   143 VVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVG 190
Cdd:pfam00571  10 VTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS COG0517
CBS domain [Signal transduction mechanisms];
55-123 8.07e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 38.69  E-value: 8.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61221144  55 RDMLEGVMDIADQRVRDIMipRSQMITLKRNQTLDECLDVIIESAHSRFPVIsEDKDHIEGILMAKDLL 123
Cdd:COG0517  55 RALAAEGKDLLDTPVSEVM--TRPPVTVSPDTSLEEAAELMEEHKIRRLPVV-DDDGRLVGIITIKDLL 120
PRK07107 PRK07107
IMP dehydrogenase;
54-121 1.95e-03

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 39.68  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61221144   54 TRDMLEGVMDIaDQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDkDHIEGILMAKD 121
Cdd:PRK07107 149 SRDYRISRMSL-DTKVKDFMTPFEKLVTANEGTTLKEANDIIWDHKLNTLPIVDKN-GNLVYLVFRKD 214
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
51-123 4.63e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.56  E-value: 4.63e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61221144  51 DEDTRDMLEGVMDIADQRVRDIMIPRsqMITLKRNQTLDECLDVIIESAHSRFPVIsEDKDHIEGILMAKDLL 123
Cdd:COG2524 134 ERDLLKALAEGRDLLDAPVSDIMTRD--VVTVSEDDSLEEALRLMLEHGIGRLPVV-DDDGKLVGIITRTDIL 203
 
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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