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Conserved domains on  [gi|485191051|ref|YP_007905979|]
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putative NS3 protein [Rodent pegivirus]

Protein Classification

DEAD/DEAH box-containing ATP-dependent helicase( domain architecture ID 1565721)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA, similar to mitochondrial ATP-dependent RNA helicase MRH4

CATH:  1.10.820.10
EC:  3.6.4.13|3.6.4.12
Gene Ontology:  GO:0005524|GO:0016887|GO:0004386
PubMed:  21779027|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 203-338 1.14e-23

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member cd17931:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 151  Bit Score: 97.23  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 203 APTGSGKSTKFPAKLAQDGHN----VLVLNPSVVTTKAMGPYMKklvGKTPNIFAGtgasAMQIKTGSK--ITYCTYGRF 276
Cdd:cd17931    8 LHPGAGKTTRVLPQIIREAIKkrlrTLVLAPTRVVAAEMYEALR---GLPIRYRTG----AVKEEHGGNeiVDYMCHGTF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485191051 277 LvnpQGFLDQKAV-----VVCDECHATDGTSILGIGVARALAEkAGVRLLVFATATPPGTQFTPHAS 338
Cdd:cd17931   81 T---CRLLSPKRVpnynlIIMDEAHFTDPASIAARGYIHTRVE-MGEAAVIFMTATPPGTVTPFPQS 143
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 339-471 8.80e-21

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd18806:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 145  Bit Score: 88.86  E-value: 8.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 339 ITEETLDGDGDIPFYGVSLkaSTYLKGRHVIFCHSKAECVRVAESLAGAGVKAVTYWRG---TRHDVLTDDADLTVVATD 415
Cdd:cd18806    1 IEDVALEIPGRIWFYGKAW--ITIYGGKTVWFVHSKKKGNEIAACLSGLGKNVIQLYRKlddTEYPKIKTIDWDFVVTTD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485191051 416 AISTGYTGNFATCTDCCSVVEETVDVDLNptFTINL-ITKAADAALRMQRRGRCGRG 471
Cdd:cd18806   79 ISEMGANFDADRVIDCRTCVKPTILFSGD--FRVILtGPVPQTAASAAQRRGRTGRN 133
 
Name Accession Description Interval E-value
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 203-338 1.14e-23

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 97.23  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 203 APTGSGKSTKFPAKLAQDGHN----VLVLNPSVVTTKAMGPYMKklvGKTPNIFAGtgasAMQIKTGSK--ITYCTYGRF 276
Cdd:cd17931    8 LHPGAGKTTRVLPQIIREAIKkrlrTLVLAPTRVVAAEMYEALR---GLPIRYRTG----AVKEEHGGNeiVDYMCHGTF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485191051 277 LvnpQGFLDQKAV-----VVCDECHATDGTSILGIGVARALAEkAGVRLLVFATATPPGTQFTPHAS 338
Cdd:cd17931   81 T---CRLLSPKRVpnynlIIMDEAHFTDPASIAARGYIHTRVE-MGEAAVIFMTATPPGTVTPFPQS 143
SF2_C_viral cd18806
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ...
 339-471 8.80e-21

C-terminal helicase domain of viral helicase; Viral helicases in this family here are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350193 [Multi-domain]  Cd Length: 145  Bit Score: 88.86  E-value: 8.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 339 ITEETLDGDGDIPFYGVSLkaSTYLKGRHVIFCHSKAECVRVAESLAGAGVKAVTYWRG---TRHDVLTDDADLTVVATD 415
Cdd:cd18806    1 IEDVALEIPGRIWFYGKAW--ITIYGGKTVWFVHSKKKGNEIAACLSGLGKNVIQLYRKlddTEYPKIKTIDWDFVVTTD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485191051 416 AISTGYTGNFATCTDCCSVVEETVDVDLNptFTINL-ITKAADAALRMQRRGRCGRG 471
Cdd:cd18806   79 ISEMGANFDADRVIDCRTCVKPTILFSGD--FRVILtGPVPQTAASAAQRRGRTGRN 133
DEXDc smart00487
DEAD-like helicases superfamily;
194-330 3.88e-13

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 68.67  E-value: 3.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051   194 SGYKEVPYFAPTGSGKSTKFPAKLAQDGHN-----VLVLNPSVVTTKAMGPYMKKLVGKTPNIFAG--TGAS----AMQI 262
Cdd:smart00487  22 SGLRDVILAAPTGSGKTLAALLPALEALKRgkggrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGlyGGDSkreqLRKL 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485191051   263 KTG-SKITYCTYGRF---LVNPQGFLDQKAVVVCDECHATDGTSILGIgVARALAEKAGVRLLVFATATPPG 330
Cdd:smart00487 102 ESGkTDILVTTPGRLldlLENDKLSLSNVDLVILDEAHRLLDGGFGDQ-LEKLLKLLPKNVQLLLLSATPPE 172
Flavi_DEAD pfam07652
Flavivirus DEAD domain;
206-332 2.16e-05

Flavivirus DEAD domain;


Pssm-ID: 400138 [Multi-domain]  Cd Length: 146  Bit Score: 44.63  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051  206 GSGKSTKFPAKLAQD----GHNVLVLNPSVVTTKAMGPYMKKLvgktpNIFAGTGASAMQIKTGSKIT---YCTYGRFLV 278
Cdd:pfam07652  12 GAGKTRKVLPELVREcidrRLRTLVLAPTRVVLAEMEEALRGL-----PIRYHTPAVSSEHTGREIVDvmcHATFTQRLL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 485191051  279 NPQGFLDQkAVVVCDECHATDGTSILGIGVARALAEKaGVRLLVFATATPPGTQ 332
Cdd:pfam07652  87 SPVRVPNY-EVIIMDEAHFTDPASIAARGYISTLVEL-GEAAAIFMTATPPGTS 138
 
Name Accession Description Interval E-value
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 203-338 1.14e-23

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 97.23  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 203 APTGSGKSTKFPAKLAQDGHN----VLVLNPSVVTTKAMGPYMKklvGKTPNIFAGtgasAMQIKTGSK--ITYCTYGRF 276
Cdd:cd17931    8 LHPGAGKTTRVLPQIIREAIKkrlrTLVLAPTRVVAAEMYEALR---GLPIRYRTG----AVKEEHGGNeiVDYMCHGTF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485191051 277 LvnpQGFLDQKAV-----VVCDECHATDGTSILGIGVARALAEkAGVRLLVFATATPPGTQFTPHAS 338
Cdd:cd17931   81 T---CRLLSPKRVpnynlIIMDEAHFTDPASIAARGYIHTRVE-MGEAAVIFMTATPPGTVTPFPQS 143
SF2_C_viral cd18806
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ...
 339-471 8.80e-21

C-terminal helicase domain of viral helicase; Viral helicases in this family here are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350193 [Multi-domain]  Cd Length: 145  Bit Score: 88.86  E-value: 8.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 339 ITEETLDGDGDIPFYGVSLkaSTYLKGRHVIFCHSKAECVRVAESLAGAGVKAVTYWRG---TRHDVLTDDADLTVVATD 415
Cdd:cd18806    1 IEDVALEIPGRIWFYGKAW--ITIYGGKTVWFVHSKKKGNEIAACLSGLGKNVIQLYRKlddTEYPKIKTIDWDFVVTTD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485191051 416 AISTGYTGNFATCTDCCSVVEETVDVDLNptFTINL-ITKAADAALRMQRRGRCGRG 471
Cdd:cd18806   79 ISEMGANFDADRVIDCRTCVKPTILFSGD--FRVILtGPVPQTAASAAQRRGRTGRN 133
DEXDc smart00487
DEAD-like helicases superfamily;
194-330 3.88e-13

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 68.67  E-value: 3.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051   194 SGYKEVPYFAPTGSGKSTKFPAKLAQDGHN-----VLVLNPSVVTTKAMGPYMKKLVGKTPNIFAG--TGAS----AMQI 262
Cdd:smart00487  22 SGLRDVILAAPTGSGKTLAALLPALEALKRgkggrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGlyGGDSkreqLRKL 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485191051   263 KTG-SKITYCTYGRF---LVNPQGFLDQKAVVVCDECHATDGTSILGIgVARALAEKAGVRLLVFATATPPG 330
Cdd:smart00487 102 ESGkTDILVTTPGRLldlLENDKLSLSNVDLVILDEAHRLLDGGFGDQ-LEKLLKLLPKNVQLLLLSATPPE 172
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 203-327 8.37e-06

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 45.86  E-value: 8.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 203 APTGSGKSTKFPAKLAQD----GHNVLVLNPSVVTTKAMGPYMKKLVGKTPNIFAGTGASAMQIKTG-----SKITYCTY 273
Cdd:cd00046    8 APTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEEREKnklgdADIIIATP 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485191051 274 GRF----LVNPQGFLDQKAVVVCDECHATDGTS----ILGIGVARALAEKAGVrllVFATAT 327
Cdd:cd00046   88 DMLlnllLREDRLFLKDLKLIIVDEAHALLIDSrgalILDLAVRKAGLKNAQV---ILLSAT 146
Flavi_DEAD pfam07652
Flavivirus DEAD domain;
206-332 2.16e-05

Flavivirus DEAD domain;


Pssm-ID: 400138 [Multi-domain]  Cd Length: 146  Bit Score: 44.63  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051  206 GSGKSTKFPAKLAQD----GHNVLVLNPSVVTTKAMGPYMKKLvgktpNIFAGTGASAMQIKTGSKIT---YCTYGRFLV 278
Cdd:pfam07652  12 GAGKTRKVLPELVREcidrRLRTLVLAPTRVVLAEMEEALRGL-----PIRYHTPAVSSEHTGREIVDvmcHATFTQRLL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 485191051  279 NPQGFLDQkAVVVCDECHATDGTSILGIGVARALAEKaGVRLLVFATATPPGTQ 332
Cdd:pfam07652  87 SPVRVPNY-EVIIMDEAHFTDPASIAARGYISTLVEL-GEAAAIFMTATPPGTS 138
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 203-329 1.64e-04

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 42.61  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051  203 APTGSGKSTKF--PA----KLAQDGHNVLVLNPsvvtTKA--------MGPYMKKLVGKTPNIFAGTGASAMQIK-TGSK 267
Cdd:pfam00270  21 APTGSGKTLAFllPAlealDKLDNGPQALVLAP----TRElaeqiyeeLKKLGKGLGLKVASLLGGDSRKEQLEKlKGPD 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485191051  268 ITYCTYGRFL--VNPQGFLDQKAVVVCDECHATDGTSiLGIGVARALAEKAGVRLLVFATATPP 329
Cdd:pfam00270  97 ILVGTPGRLLdlLQERKLLKNLKLLVLDEAHRLLDMG-FGPDLEEILRRLPKKRQILLLSATLP 159
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 203-328 4.89e-04

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 40.75  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 203 APTGSGKST---KFPAKLAQdgHNVLVLNPSVV-TTKAMGPYMKKLVGKTPNIFaGTGASAMqiKTGSKITYCTY---GR 275
Cdd:cd17926   25 LPTGSGKTLtalALIAYLKE--LRTLIVVPTDAlLDQWKERFEDFLGDSSIGLI-GGGKKKD--FDDANVVVATYqslSN 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 485191051 276 FLVNPQGFLDQKAVVVCDECHATDGTSIlgigvaRALAEKAGVRLLVFATATP 328
Cdd:cd17926  100 LAEEEKDLFDQFGLLIVDEAHHLPAKTF------SEILKELNAKYRLGLTATP 146
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 203-314 1.79e-03

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 39.62  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051 203 APTGSGKSTKFPAKLAQ----DGHNVLVLNPSVVTTKAMGPYMKKLVGKTPNIFAG---------TGASAMQIKTGSKIT 269
Cdd:cd17990   24 APPGAGKTTRVPLALLAelwiAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGyrvrgesrvGRRTRVEVVTEGVLL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 485191051 270 YctygRFLVNPQgfLDQKAVVVCDECHATDGTSILGIGVARALAE 314
Cdd:cd17990  104 R----RLQRDPE--LSGVGAVILDEFHERSLDADLALALLLEVQQ 142
ResIII pfam04851
Type III restriction enzyme, res subunit;
203-296 3.80e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.42  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485191051  203 APTGSGK---STKFPAKLAQDGH--NVLVLNPSV-VTTKAMGPYMKKLVGKTPNIFAGTGASAMQIKTGSKITYCTY--- 273
Cdd:pfam04851  30 MATGSGKtltAAKLIARLFKKGPikKVLFLVPRKdLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDDNKIVVTTIqsl 109

                          90       100
                  ....*....|....*....|....*
gi 485191051  274 GRFLVNP--QGFLDQKAVVVCDECH 296
Cdd:pfam04851 110 YKALELAslELLPDFFDVIIIDEAH 134
 
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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