NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6324512|ref|NP_014581|]
View 

Mam3p [Saccharomyces cerevisiae S288C]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 66-388 3.28e-41

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: 156.05  E-value: 3.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   66 IISIILVLLGGVFAGLTLGLMGQDEVYLKVISTSGSnsekKLAKRVLDLISRgKHWVLVTLLLSNVITN--------ETL 137
Cdd:COG1253   8 LLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGD----KGARRALKLLED-PDRFLSTIQIGITLAGllagalgeAAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  138 PIVLDRCLGG-GWQ-----------AVVSSTILIVIFGEIIPQSVCVKYGLQVGAFFCPFVLVLMYLMYPVAYP---IAT 202
Cdd:COG1253  83 AALLAPLLGSlGLPaalahtlalvlAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLlngSTN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  203 LLDYMLG---EDHGTMYKKSGLKTLVTLHRTMGVerLTKDEVTIISAVLDLKAKRVEEIMTPIENVFTMSADTILDDkTV 279
Cdd:COG1253 163 LLLRLLGiepAEEEPAVTEEELRALVEESEESGV--IEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEE-AL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  280 EKIFNSGFSRIPIFLpNEPNNFIGMLLVRVLISYDPDDclpiSHFPLATL-------PETspnTSCLNILNYFQEGKAHM 352
Cdd:COG1253 240 ELILESGHSRIPVYE-GDLDDIVGVVHVKDLLRALLEG----EPFDLRDLlrpplfvPET---KPLDDLLEEFRRERVHM 311

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6324512  353 CVVSKEPGsshGAIGVLTLEDVIEELIGeEIVDESD 388
Cdd:COG1253 312 AIVVDEYG---GTAGLVTLEDILEEIVG-EIRDEYD 343
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 66-388 3.28e-41

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 156.05  E-value: 3.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   66 IISIILVLLGGVFAGLTLGLMGQDEVYLKVISTSGSnsekKLAKRVLDLISRgKHWVLVTLLLSNVITN--------ETL 137
Cdd:COG1253   8 LLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGD----KGARRALKLLED-PDRFLSTIQIGITLAGllagalgeAAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  138 PIVLDRCLGG-GWQ-----------AVVSSTILIVIFGEIIPQSVCVKYGLQVGAFFCPFVLVLMYLMYPVAYP---IAT 202
Cdd:COG1253  83 AALLAPLLGSlGLPaalahtlalvlAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLlngSTN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  203 LLDYMLG---EDHGTMYKKSGLKTLVTLHRTMGVerLTKDEVTIISAVLDLKAKRVEEIMTPIENVFTMSADTILDDkTV 279
Cdd:COG1253 163 LLLRLLGiepAEEEPAVTEEELRALVEESEESGV--IEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEE-AL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  280 EKIFNSGFSRIPIFLpNEPNNFIGMLLVRVLISYDPDDclpiSHFPLATL-------PETspnTSCLNILNYFQEGKAHM 352
Cdd:COG1253 240 ELILESGHSRIPVYE-GDLDDIVGVVHVKDLLRALLEG----EPFDLRDLlrpplfvPET---KPLDDLLEEFRRERVHM 311

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6324512  353 CVVSKEPGsshGAIGVLTLEDVIEELIGeEIVDESD 388
Cdd:COG1253 312 AIVVDEYG---GTAGLVTLEDILEEIVG-EIRDEYD 343
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 66-233 7.21e-30

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: 116.55  E-value: 7.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512     66 IISIILVLLGGVFAGLTLGLMGQDEVYLKVISTSGsnseKKLAKRVLDLISRGkHWVLVTLLLSNVITNETLPIVLDRCL 145
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKG----NKGAKRLLKLLANP-DRLLSTLLIGNTLANILLGALATALF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512    146 -----GGGWQAVVSS----TILIVIFGEIIPQSVCVKYGLQVGAFFCPFVLVLMYLMYPVAYPIATLLDYML------GE 210
Cdd:pfam01595  76 aellaPLGALGVAIAtvlvTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILrlfgvkGG 155

                         170       180
                  ....*....|....*....|...
gi 6324512    211 DHGTMYKKSGLKTLVTLHRTMGV 233
Cdd:pfam01595 156 ESEPAVTEEELRSLVEESAEEGV 178
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 254-376 2.11e-26

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: 104.11  E-value: 2.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  254 RVEEIMTPIENVFTMSADTiLDDKTVEKIFNSGFSRIPIFlPNEPNNFIGMLLVRVLISYDPDDCLPIS----HFPLATL 329
Cdd:cd04590   1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVY-EGDLDNIIGVLHVKDLLAALLEGREKLDlralLRPPLFV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6324512  330 PETspnTSCLNILNYFQEGKAHMCVVSKEPGsshGAIGVLTLEDVIE 376
Cdd:cd04590  79 PET---TPLDDLLEEFRKERSHMAIVVDEYG---GTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
243-388 1.65e-08

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 56.35  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   243 IISAVLDLKAKRVEEIMTPIENVFTMSADTILDDkTVEKIFNSGFSRIPIfLPNEPNNFIGMLLVRVLISYDPDDCLPIS 322
Cdd:PRK15094  57 MLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDE-CLDVIIESAHSRFPV-ISEDKDHIEGILMAKDLLPFMRSDAEAFS 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   323 H----FPLATLPETSPNTsclNILNYFQEGKAHMCVVSKEPGsshGAIGVLTLEDVIEELIGeEIVDESD 388
Cdd:PRK15094 135 MdkvlRQAVVVPESKRVD---RMLKEFRSQRYHMAIVIDEFG---GVSGLVTIEDILELIVG-EIEDEYD 197
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 66-388 3.28e-41

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 156.05  E-value: 3.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   66 IISIILVLLGGVFAGLTLGLMGQDEVYLKVISTSGSnsekKLAKRVLDLISRgKHWVLVTLLLSNVITN--------ETL 137
Cdd:COG1253   8 LLILLLILLNGFFSASEFALVSLRRSRLEQLAEEGD----KGARRALKLLED-PDRFLSTIQIGITLAGllagalgeAAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  138 PIVLDRCLGG-GWQ-----------AVVSSTILIVIFGEIIPQSVCVKYGLQVGAFFCPFVLVLMYLMYPVAYP---IAT 202
Cdd:COG1253  83 AALLAPLLGSlGLPaalahtlalvlAVVLITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLlngSTN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  203 LLDYMLG---EDHGTMYKKSGLKTLVTLHRTMGVerLTKDEVTIISAVLDLKAKRVEEIMTPIENVFTMSADTILDDkTV 279
Cdd:COG1253 163 LLLRLLGiepAEEEPAVTEEELRALVEESEESGV--IEEEEREMIENVFEFGDRTVREVMTPRTDVVALDLDDTLEE-AL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  280 EKIFNSGFSRIPIFLpNEPNNFIGMLLVRVLISYDPDDclpiSHFPLATL-------PETspnTSCLNILNYFQEGKAHM 352
Cdd:COG1253 240 ELILESGHSRIPVYE-GDLDDIVGVVHVKDLLRALLEG----EPFDLRDLlrpplfvPET---KPLDDLLEEFRRERVHM 311

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6324512  353 CVVSKEPGsshGAIGVLTLEDVIEELIGeEIVDESD 388
Cdd:COG1253 312 AIVVDEYG---GTAGLVTLEDILEEIVG-EIRDEYD 343
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
 66-233 7.21e-30

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: 116.55  E-value: 7.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512     66 IISIILVLLGGVFAGLTLGLMGQDEVYLKVISTSGsnseKKLAKRVLDLISRGkHWVLVTLLLSNVITNETLPIVLDRCL 145
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKG----NKGAKRLLKLLANP-DRLLSTLLIGNTLANILLGALATALF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512    146 -----GGGWQAVVSS----TILIVIFGEIIPQSVCVKYGLQVGAFFCPFVLVLMYLMYPVAYPIATLLDYML------GE 210
Cdd:pfam01595  76 aellaPLGALGVAIAtvlvTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILrlfgvkGG 155

                         170       180
                  ....*....|....*....|...
gi 6324512    211 DHGTMYKKSGLKTLVTLHRTMGV 233
Cdd:pfam01595 156 ESEPAVTEEELRSLVEESAEEGV 178
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 254-376 2.11e-26

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: 104.11  E-value: 2.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512  254 RVEEIMTPIENVFTMSADTiLDDKTVEKIFNSGFSRIPIFlPNEPNNFIGMLLVRVLISYDPDDCLPIS----HFPLATL 329
Cdd:cd04590   1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVY-EGDLDNIIGVLHVKDLLAALLEGREKLDlralLRPPLFV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6324512  330 PETspnTSCLNILNYFQEGKAHMCVVSKEPGsshGAIGVLTLEDVIE 376
Cdd:cd04590  79 PET---TPLDDLLEEFRKERSHMAIVVDEYG---GTAGIVTLEDILE 119
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
243-388 1.65e-08

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 56.35  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   243 IISAVLDLKAKRVEEIMTPIENVFTMSADTILDDkTVEKIFNSGFSRIPIfLPNEPNNFIGMLLVRVLISYDPDDCLPIS 322
Cdd:PRK15094  57 MLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDE-CLDVIIESAHSRFPV-ISEDKDHIEGILMAKDLLPFMRSDAEAFS 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   323 H----FPLATLPETSPNTsclNILNYFQEGKAHMCVVSKEPGsshGAIGVLTLEDVIEELIGeEIVDESD 388
Cdd:PRK15094 135 MdkvlRQAVVVPESKRVD---RMLKEFRSQRYHMAIVIDEFG---GVSGLVTIEDILELIVG-EIEDEYD 197
PRK11573 PRK11573
hypothetical protein; Provisional
 71-392 7.78e-08

hypothetical protein; Provisional


Pssm-ID: 236933 [Multi-domain]  Cd Length: 413  Bit Score: 55.14  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512    71 LVLLGGVFAGLTLGLMGQDEVYLKVISTSGSNSEK---KLAKRVLDLISrgkhWVLVTLLLSNVITNETLPIVLDRCLGG 147
Cdd:PRK11573   1 MVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKrveKLLRKPDRLIS----LVLIGNNLVNILASALGTIVGMRLYGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   148 GWQAVVSS--TILIVIFGEIIPQSVCVKYGLQVgAFFCPFVLV-LMYLMYPVAY---PIATLLDYMLG----EDHGTMYK 217
Cdd:PRK11573  77 AGVAIATGvlTFVVLVFAEVLPKTIAALYPEKV-AYPSSFLLApLQILMMPLVWllnTITRLLMRLMGiktdIVVSGALS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   218 KSGLKTLVTLHRTMgVERLTKDevtIISAVLDLKAKRVEEIMTPIENVFTMSadtILDD--KTVEKIFNSGFSRIPIFlP 295
Cdd:PRK11573 156 KEELRTIVHESRSQ-ISRRNQD---MLLSVLDLEKVTVDDIMVPRNEIVGID---INDDwkSILRQLTHSPHGRIVLY-R 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324512   296 NEPNNFIGMLLVRV---LISYDPD---DCLPISHFPLATLPETSPntscLNI-LNYFQEGKAHMCVVSKEPGSSHGAIgv 368
Cdd:PRK11573 228 DSLDDAISMLRVREayrLMTEKKEftkENMLRAADEIYFVPEGTP----LSTqLVKFQRNKKKVGLVVDEYGDIQGLV-- 301

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 6324512   369 lTLEDVIEELIG-----------EEIVDESD--VFVD 392
Cdd:PRK11573 302 -TVEDILEEIVGdfttsmsptlaEEVTPQNDgsVIID 337
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH