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Conserved domains on  [gi|569008127|ref|XP_006527553|]
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metal transporter CNNM2 isoform X1 [Mus musculus]

Protein Classification

CNNM metal transporter family protein( domain architecture ID 1000124)

CNNM metal transporter family protein containing tandem repeats of the cystathionine beta-synthase (CBS pair) domain and a transporter-associated domain; similar to Homo sapiens metal transporter CNNM2 that is a divalent metal cation transporter

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlyC super family cl34211
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 255-540 1.12e-34

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


The actual alignment was detected with superfamily member COG1253:

Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 135.63  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 255 FWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVQNcgtEKEKNyAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILL 334
Cdd:COG1253    3 LLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAE---EGDKG-ARRALKLLEDPDRFLSTIQIGITLAGLLAGALG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 335 DDIAG--------------------SGLVAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVS 394
Cdd:COG1253   79 EAALAallapllgslglpaalahtlALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 395 KLLDCVL------GQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMITGEAILDfN 468
Cdd:COG1253  159 GSTNLLLrllgiePAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLE-E 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008127 469 TMSEIMESGYTRIPVFEGERSNIVDLLFVKDL-AFVDPDDCTPLKTITkfynHPLHFVFNDTKLDAMLEEFKK 540
Cdd:COG1253  238 ALELILESGHSRIPVYEGDLDDIVGVVHVKDLlRALLEGEPFDLRDLL----RPPLFVPETKPLDDLLEEFRR 306
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 255-540 1.12e-34

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 135.63  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 255 FWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVQNcgtEKEKNyAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILL 334
Cdd:COG1253    3 LLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAE---EGDKG-ARRALKLLEDPDRFLSTIQIGITLAGLLAGALG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 335 DDIAG--------------------SGLVAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVS 394
Cdd:COG1253   79 EAALAallapllgslglpaalahtlALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 395 KLLDCVL------GQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMITGEAILDfN 468
Cdd:COG1253  159 GSTNLLLrllgiePAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLE-E 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008127 469 TMSEIMESGYTRIPVFEGERSNIVDLLFVKDL-AFVDPDDCTPLKTITkfynHPLHFVFNDTKLDAMLEEFKK 540
Cdd:COG1253  238 ALELILESGHSRIPVYEGDLDDIVGVVHVKDLlRALLEGEPFDLRDLL----RPPLFVPETKPLDDLLEEFRR 306
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 260-420 3.78e-26

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


Pssm-ID: 460260  Cd Length: 183  Bit Score: 104.99  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127  260 IFISLLLCLSGMFSGLNLGLMALDPMELRIVQncgtEKEKNYAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILLDDIAG 339
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELA----EKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127  340 ---------SGLVAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVSKLLDCVL------GQE 404
Cdd:pfam01595  77 ellaplgalGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILrlfgvkGGE 156

                         170
                  ....*....|....*.
gi 569008127  405 IGTVYNREKLLEMLRV 420
Cdd:pfam01595 157 SEPAVTEEELRSLVEE 172
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 445-540 2.70e-24

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: 97.95  E-value: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 445 TVEDVMTPLRDCFMITGEAiLDFNTMSEIMESGYTRIPVFEGERSNIVDLLFVKDLAFVDPDDCTplKTITKFYNHPLHF 524
Cdd:cd04590    1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGRE--KLDLRALLRPPLF 77

                         90
                 ....*....|....*.
gi 569008127 525 VFNDTKLDAMLEEFKK 540
Cdd:cd04590   78 VPETTPLDDLLEEFRK 93
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
410-539 5.37e-06

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 48.27  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 410 NREKLLEMLRVTDPyNDLVKEEL-NIIQGALELRTKTVEDVMTPLRDCFMITGEAILDfNTMSEIMESGYTRIPVFEGER 488
Cdd:PRK15094  33 NRDELLALIRDSEQ-NDLIDEDTrDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDK 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569008127 489 SNIVDLLFVKDLAFVDPDDCTPLkTITKFYnHPLHFVFNDTKLDAMLEEFK 539
Cdd:PRK15094 111 DHIEGILMAKDLLPFMRSDAEAF-SMDKVL-RQAVVVPESKRVDRMLKEFR 159
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 255-540 1.12e-34

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 135.63  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 255 FWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVQNcgtEKEKNyAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILL 334
Cdd:COG1253    3 LLLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAE---EGDKG-ARRALKLLEDPDRFLSTIQIGITLAGLLAGALG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 335 DDIAG--------------------SGLVAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVS 394
Cdd:COG1253   79 EAALAallapllgslglpaalahtlALVLAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 395 KLLDCVL------GQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMITGEAILDfN 468
Cdd:COG1253  159 GSTNLLLrllgiePAEEEPAVTEEELRALVEESEESGVIEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLE-E 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569008127 469 TMSEIMESGYTRIPVFEGERSNIVDLLFVKDL-AFVDPDDCTPLKTITkfynHPLHFVFNDTKLDAMLEEFKK 540
Cdd:COG1253  238 ALELILESGHSRIPVYEGDLDDIVGVVHVKDLlRALLEGEPFDLRDLL----RPPLFVPETKPLDDLLEEFRR 306
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 253-540 7.26e-29

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: 118.64  E-value: 7.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 253 LPFWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVqncgtEKEKNY-AKRIEPVRRQGNYLLCSLLLGNVLVN---T 328
Cdd:COG4536    4 ISLSLLIGILVLLLLLSAFFSGSETALMALNRYRLRHL-----AKKGHKgAKRVLKLLERPDRLIGTILLGNNLVNilaS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 329 TL-TILLDDIAGSGLVAV--VVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVS-------KLLD 398
Cdd:COG4536   79 SLaTVIAIRLFGDAGVAIatLVLTLLILIFAEVTPKTLAALYPEKIALPVSPPLRPLLKLLYPLVWLVNlivrgllRLFG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 399 CVLGQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMI----TGEAILDfntmsEIM 474
Cdd:COG4536  159 VKPDADASDLLSEEELRTVVDLGEAGGVIPKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIdlddPWEEILK-----QLL 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569008127 475 ESGYTRIPVFEGERSNIVDLLFVKD-LAFVDPDDCTP--LKTITKfynhPLHFVFNDTKLDAMLEEFKK 540
Cdd:COG4536  234 TSPHTRLPVYRGDIDNIVGVLHVRDlLRALRKGDLSKedLRKIAR----EPYFIPETTPLSTQLQNFQK 298
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 260-420 3.78e-26

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


Pssm-ID: 460260  Cd Length: 183  Bit Score: 104.99  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127  260 IFISLLLCLSGMFSGLNLGLMALDPMELRIVQncgtEKEKNYAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILLDDIAG 339
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELA----EKGNKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127  340 ---------SGLVAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVSKLLDCVL------GQE 404
Cdd:pfam01595  77 ellaplgalGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILrlfgvkGGE 156

                         170
                  ....*....|....*.
gi 569008127  405 IGTVYNREKLLEMLRV 420
Cdd:pfam01595 157 SEPAVTEEELRSLVEE 172
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 445-540 2.70e-24

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: 97.95  E-value: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 445 TVEDVMTPLRDCFMITGEAiLDFNTMSEIMESGYTRIPVFEGERSNIVDLLFVKDLAFVDPDDCTplKTITKFYNHPLHF 524
Cdd:cd04590    1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGRE--KLDLRALLRPPLF 77

                         90
                 ....*....|....*.
gi 569008127 525 VFNDTKLDAMLEEFKK 540
Cdd:cd04590   78 VPETTPLDDLLEEFRK 93
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
410-539 5.37e-06

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 48.27  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 410 NREKLLEMLRVTDPyNDLVKEEL-NIIQGALELRTKTVEDVMTPLRDCFMITGEAILDfNTMSEIMESGYTRIPVFEGER 488
Cdd:PRK15094  33 NRDELLALIRDSEQ-NDLIDEDTrDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDK 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569008127 489 SNIVDLLFVKDLAFVDPDDCTPLkTITKFYnHPLHFVFNDTKLDAMLEEFK 539
Cdd:PRK15094 111 DHIEGILMAKDLLPFMRSDAEAF-SMDKVL-RQAVVVPESKRVDRMLKEFR 159
PRK11573 PRK11573
hypothetical protein; Provisional
 265-452 3.34e-04

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 43.20  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 265 LLCLSGMFSGLNLGLMALDPMELRIVQNCGTEKeknyAKRIEPVRRQGNYLLCSLLLGNVLVNtTLTILLDDIAGSGL-- 342
Cdd:PRK11573   1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRS----AKRVEKLLRKPDRLISLVLIGNNLVN-ILASALGTIVGMRLyg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008127 343 -----VAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASY---PVSKLLDCVLGQEIGTVYNREKL 414
Cdd:PRK11573  76 dagvaIATGVLTFVVLVFAEVLPKTIAALYPEKVAYPSSFLLAPLQILMMPLVWllnTITRLLMRLMGIKTDIVVSGALS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 569008127 415 LEMLR--VTDPYNDLVKEELNIIQGALELRTKTVEDVMTP 452
Cdd:PRK11573 156 KEELRtiVHESRSQISRRNQDMLLSVLDLEKVTVDDIMVP 195
 
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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