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Conserved domains on  [gi|1017483950|ref|NP_001309670|]
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Metal transporter cnnm-3 [Caenorhabditis elegans]

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 ...
198-491 6.32e-33

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: 132.55  E-value: 6.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 198 WLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGteqeKRDAGRILPIRKKGNQLLCTLLI-------------- 263
Cdd:COG1253     4 LLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEG----DKGARRALKLLEDPDRFLSTIQIgitlagllagalge 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 264 ---GNVVVNVGVSLLMDQLVGSGFAVLVA---ATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISK 337
Cdd:COG1253    80 aalAALLAPLLGSLGLPAALAHTLALVLAvvlITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 338 VLDIFLK--------EELTRSLERnkLVEMLKLSEKS-IIggQSDEFKMVLGALELYDKTVAHAMT-RyEDIFMLPHTLT 407
Cdd:COG1253   160 STNLLLRllgiepaeEEPAVTEEE--LRALVEESEESgVI--EEEEREMIENVFEFGDRTVREVMTpR-TDVVALDLDDT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 408 LGAgMVTQILDMGYTRIPIYENDRKNIVALLFVKDL-ALLDPDDNHNVMKIAsiynHEVRRVLVDMPLRNMLEEFKRGEY 486
Cdd:COG1253   235 LEE-ALELILESGHSRIPVYEGDLDDIVGVVHVKDLlRALLEGEPFDLRDLL----RPPLFVPETKPLDDLLEEFRRERV 309

                  ....*
gi 1017483950 487 HMALV 491
Cdd:COG1253   310 HMAIV 314
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
198-491 6.32e-33

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 132.55  E-value: 6.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 198 WLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGteqeKRDAGRILPIRKKGNQLLCTLLI-------------- 263
Cdd:COG1253     4 LLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEG----DKGARRALKLLEDPDRFLSTIQIgitlagllagalge 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 264 ---GNVVVNVGVSLLMDQLVGSGFAVLVA---ATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISK 337
Cdd:COG1253    80 aalAALLAPLLGSLGLPAALAHTLALVLAvvlITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 338 VLDIFLK--------EELTRSLERnkLVEMLKLSEKS-IIggQSDEFKMVLGALELYDKTVAHAMT-RyEDIFMLPHTLT 407
Cdd:COG1253   160 STNLLLRllgiepaeEEPAVTEEE--LRALVEESEESgVI--EEEEREMIENVFEFGDRTVREVMTpR-TDVVALDLDDT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 408 LGAgMVTQILDMGYTRIPIYENDRKNIVALLFVKDL-ALLDPDDNHNVMKIAsiynHEVRRVLVDMPLRNMLEEFKRGEY 486
Cdd:COG1253   235 LEE-ALELILESGHSRIPVYEGDLDDIVGVVHVKDLlRALLEGEPFDLRDLL----RPPLFVPETKPLDDLLEEFRRERV 309

                  ....*
gi 1017483950 487 HMALV 491
Cdd:COG1253   310 HMAIV 314
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
388-512 2.52e-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: 98.34  E-value: 2.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 388 TVAHAMTRYEDIFMLPHTLTLGAgMVTQILDMGYTRIPIYENDRKNIVALLFVKDLALLDPDDnhNVMKIASIYNHEVRR 467
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEE-LLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEG--REKLDLRALLRPPLF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1017483950 468 VLVDMPLRNMLEEFKRGEYHMALVErlveqedkDPIYELCGLITL 512
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTL 114
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
202-344 2.65e-22

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: 94.98  E-value: 2.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 202 ICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGteqeKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVSLLMDQLVG 281
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKG----NKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017483950 282 ---------SGFAVLVAATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISKVLDIFLK 344
Cdd:pfam01595  77 ellaplgalGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILR 148
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
353-491 2.05e-04

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 44.03  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 353 RNKLVEMLKLSEKSIIGGQsDEFKMVLGALELYDKTVAHAMTRYEDIFMLPHTLTLGAGMVTqILDMGYTRIPIYENDRK 432
Cdd:PRK15094   34 RDELLALIRDSEQNDLIDE-DTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDV-IIESAHSRFPVISEDKD 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017483950 433 NIVALLFVKDLALL-----DPDDNHNVMKIASIYNhEVRRVlvdmplRNMLEEFKRGEYHMALV 491
Cdd:PRK15094  112 HIEGILMAKDLLPFmrsdaEAFSMDKVLRQAVVVP-ESKRV------DRMLKEFRSQRYHMAIV 168
 
Name Accession Description Interval E-value
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
198-491 6.32e-33

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 132.55  E-value: 6.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 198 WLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGteqeKRDAGRILPIRKKGNQLLCTLLI-------------- 263
Cdd:COG1253     4 LLELLLILLLILLNGFFSASEFALVSLRRSRLEQLAEEG----DKGARRALKLLEDPDRFLSTIQIgitlagllagalge 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 264 ---GNVVVNVGVSLLMDQLVGSGFAVLVA---ATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISK 337
Cdd:COG1253    80 aalAALLAPLLGSLGLPAALAHTLALVLAvvlITFLSLVFGELVPKRLALQNPERVALLVAPPLRLFSRLFRPLVWLLNG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 338 VLDIFLK--------EELTRSLERnkLVEMLKLSEKS-IIggQSDEFKMVLGALELYDKTVAHAMT-RyEDIFMLPHTLT 407
Cdd:COG1253   160 STNLLLRllgiepaeEEPAVTEEE--LRALVEESEESgVI--EEEEREMIENVFEFGDRTVREVMTpR-TDVVALDLDDT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 408 LGAgMVTQILDMGYTRIPIYENDRKNIVALLFVKDL-ALLDPDDNHNVMKIAsiynHEVRRVLVDMPLRNMLEEFKRGEY 486
Cdd:COG1253   235 LEE-ALELILESGHSRIPVYEGDLDDIVGVVHVKDLlRALLEGEPFDLRDLL----RPPLFVPETKPLDDLLEEFRRERV 309

                  ....*
gi 1017483950 487 HMALV 491
Cdd:COG1253   310 HMAIV 314
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
198-512 7.05e-25

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: 108.24  E-value: 7.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 198 WLSWICLLILLCFSGLFSGLNLGLMTLSPYELQlYIAsgtEQEKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVS---- 273
Cdd:COG4536     7 SLLIGILVLLLLLSAFFSGSETALMALNRYRLR-HLA---KKGHKGAKRVLKLLERPDRLIGTILLGNNLVNILASslat 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 274 LLMDQLVGSGfAVLVAA---TSCIVVFGEIIPQALCV----KLGLPIGartiPITQVLLFLMYPLTWPISKVLDIFLK-- 344
Cdd:COG4536    83 VIAIRLFGDA-GVAIATlvlTLLILIFAEVTPKTLAAlypeKIALPVS----PPLRPLLKLLYPLVWLVNLIVRGLLRlf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 345 --------------EELtRSLernklVEMLKlSEKSIiggQSDEFKMVLGALELYDKTVAHAMTRYEDIFMLPHTLTLGA 410
Cdd:COG4536   158 gvkpdadasdllseEEL-RTV-----VDLGE-AGGVI---PKEHRDMLLNILDLEDVTVEDIMVPRNEIEGIDLDDPWEE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 411 gMVTQILDMGYTRIPIYENDRKNIVALLFVKDL--ALLDPDDNH-NVMKIASiynhEVRRVLVDMPLRNMLEEFKRGEYH 487
Cdd:COG4536   228 -ILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDLlrALRKGDLSKeDLRKIAR----EPYFIPETTPLSTQLQNFQKRKRR 302
                         330       340
                  ....*....|....*....|....*...
gi 1017483950 488 MALV--ErlveqedkdpiY-ELCGLITL 512
Cdd:COG4536   303 FALVvdE-----------YgDVQGLVTL 319
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
388-512 2.52e-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: 98.34  E-value: 2.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 388 TVAHAMTRYEDIFMLPHTLTLGAgMVTQILDMGYTRIPIYENDRKNIVALLFVKDLALLDPDDnhNVMKIASIYNHEVRR 467
Cdd:cd04590     1 TVREVMTPRTDVVALDADATLEE-LLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEG--REKLDLRALLRPPLF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1017483950 468 VLVDMPLRNMLEEFKRGEYHMALVErlveqedkDPIYELCGLITL 512
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTL 114
CNNM pfam01595
Cyclin M transmembrane N-terminal domain; This transmembrane domain is found in metal ...
202-344 2.65e-22

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: 94.98  E-value: 2.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 202 ICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGteqeKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVSLLMDQLVG 281
Cdd:pfam01595   1 LIALLLLLLSAFFSAAETALVSLRRSRLEELAEKG----NKGAKRLLKLLANPDRLLSTLLIGNTLANILLGALATALFA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017483950 282 ---------SGFAVLVAATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISKVLDIFLK 344
Cdd:pfam01595  77 ellaplgalGVAIATVLVTLLILVFGEILPKTLALRYAERIALRVAPPLLVLSKLLYPLVWLLNKLANLILR 148
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
353-491 2.05e-04

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 44.03  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483950 353 RNKLVEMLKLSEKSIIGGQsDEFKMVLGALELYDKTVAHAMTRYEDIFMLPHTLTLGAGMVTqILDMGYTRIPIYENDRK 432
Cdd:PRK15094   34 RDELLALIRDSEQNDLIDE-DTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDV-IIESAHSRFPVISEDKD 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017483950 433 NIVALLFVKDLALL-----DPDDNHNVMKIASIYNhEVRRVlvdmplRNMLEEFKRGEYHMALV 491
Cdd:PRK15094  112 HIEGILMAKDLLPFmrsdaEAFSMDKVLRQAVVVP-ESKRV------DRMLKEFRSQRYHMAIV 168
 
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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