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Conserved domains on  [gi|1912229890|ref|NP_690005|]
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retroviral-like aspartic protease 1 [Homo sapiens]

Protein Classification

retropepsin-like aspartic protease( domain architecture ID 10084770)

retropepsin-like (A2 family) peptidase is an aspartic protease that hydrolyzes the peptide bonds of substrates; similar to Mus musculus retroviral-like aspartic protease 1

CATH:  2.40.70.10
EC:  3.4.23.-
Gene Ontology:  GO:0004190
MEROPS:  A2
PubMed:  1851433
SCOP:  4002288

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 114-206 5.43e-15

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


:

Pssm-ID: 133136  Cd Length: 92  Bit Score: 68.52  E-value: 5.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 114 LKGKIGKVPVRFLVDSGAQVSVVHPNLWEEvtDGDLDTLQPFENVVKVANGAEMKILGVWDTA-VSLGKLKLKAQFLVAN 192
Cdd:cd00303     1 LKGKINGVPVRALVDSGASVNFISESLAKK--LGLPPRLLPTPLKVKGANGSSVKTLGVILPVtIGIGGKTFTVDFYVLD 78

                          90
                  ....*....|....
gi 1912229890 193 ASAEEAIIGTDVLQ 206
Cdd:cd00303    79 LLSYDVILGRPWLE 92
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 114-206 5.43e-15

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 68.52  E-value: 5.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 114 LKGKIGKVPVRFLVDSGAQVSVVHPNLWEEvtDGDLDTLQPFENVVKVANGAEMKILGVWDTA-VSLGKLKLKAQFLVAN 192
Cdd:cd00303     1 LKGKINGVPVRALVDSGASVNFISESLAKK--LGLPPRLLPTPLKVKGANGSSVKTLGVILPVtIGIGGKTFTVDFYVLD 78

                          90
                  ....*....|....
gi 1912229890 193 ASAEEAIIGTDVLQ 206
Cdd:cd00303    79 LLSYDVILGRPWLE 92
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 114-206 1.23e-12

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 62.21  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 114 LKGKIGKVPVRFLVDSGAQVSVVHPNLWEEVtdgDLDTLQ-PFENVVKVANGAEMKILGVWDTaVSLGKLKLKA-QFLVA 191
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERL---GLDRLVdAYPVTVRTANGTVRAARVRLDS-VKIGGIELRNvPAVVL 76

                          90
                  ....*....|....*
gi 1912229890 192 NASAEEAIIGTDVLQ 206
Cdd:pfam13975  77 PGDLDDVLLGMDFLK 91
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
91-214 4.64e-04

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 39.55  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890  91 PGAAPSH-LPKEIVFANSMGKGYYLKGKIGKVPVRFLVDSGAQVSVVHPNLWEE--VTDGDLDTLQPfenvVKVANGAEM 167
Cdd:COG3577    20 PGQAPVStGGGEVVLKRDRDGHFVVEGTINGQPVRFLVDTGASTVVLSESDARRlgLDPEDLGRPVR----VQTANGVVR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1912229890 168 KILGVWDTaVSLGKLKLK-AQFLVANASA-EEAIIGTDVLQDHNAILDF 214
Cdd:COG3577    96 AARVRLDS-VRIGGITLRnVRAVVLPGGElDDGLLGMSFLGRLDFEIDG 143
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 114-206 5.43e-15

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 68.52  E-value: 5.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 114 LKGKIGKVPVRFLVDSGAQVSVVHPNLWEEvtDGDLDTLQPFENVVKVANGAEMKILGVWDTA-VSLGKLKLKAQFLVAN 192
Cdd:cd00303     1 LKGKINGVPVRALVDSGASVNFISESLAKK--LGLPPRLLPTPLKVKGANGSSVKTLGVILPVtIGIGGKTFTVDFYVLD 78

                          90
                  ....*....|....
gi 1912229890 193 ASAEEAIIGTDVLQ 206
Cdd:cd00303    79 LLSYDVILGRPWLE 92
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 114-206 1.23e-12

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 62.21  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 114 LKGKIGKVPVRFLVDSGAQVSVVHPNLWEEVtdgDLDTLQ-PFENVVKVANGAEMKILGVWDTaVSLGKLKLKA-QFLVA 191
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERL---GLDRLVdAYPVTVRTANGTVRAARVRLDS-VKIGGIELRNvPAVVL 76

                          90
                  ....*....|....*
gi 1912229890 192 NASAEEAIIGTDVLQ 206
Cdd:pfam13975  77 PGDLDDVLLGMDFLK 91
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 112-206 4.75e-08

Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133150  Cd Length: 96  Bit Score: 49.55  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 112 YYLKGKIGKVPVRFLVDSGAQVSVVHPNLWEEVtdgDLDTLQPFENVVKVANGAEMKILGVWDTaVSLGKLKLK-AQFLV 190
Cdd:cd05483     3 FVVPVTINGQPVRFLLDTGASTTVISEELAERL---GLPLTLGGKVTVQTANGRVRAARVRLDS-LQIGGITLRnVPAVV 78

                          90
                  ....*....|....*...
gi 1912229890 191 ANASA--EEAIIGTDVLQ 206
Cdd:cd05483    79 LPGDAlgVDGLLGMDFLR 96
RP_Saci_like cd06094
RP_Saci_like, retropepsin family; Retropepsin on retrotransposons with long terminal repeats ...
 123-209 5.34e-07

RP_Saci_like, retropepsin family; Retropepsin on retrotransposons with long terminal repeats (LTR) including Saci-1, -2 and -3 of Schistosoma mansoni. Retropepsins are related to fungal and mammalian pepsins. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133158  Cd Length: 89  Bit Score: 46.46  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 123 VRFLVDSGAQVSVVHPNLWEEVTDGDLDTLQpfenvvkVANGAEMKILGVWDTAVSLG-KLKLKAQFLVANASaeEAIIG 201
Cdd:cd06094    10 LRFLVDTGAAVSVLPASSTKKSLKPSPLTLQ-------AANGTPIATYGTRSLTLDLGlRRPFAWNFVVADVP--HPILG 80


                  ....*...
gi 1912229890 202 TDVLQDHN 209
Cdd:cd06094    81 ADFLQHYG 88
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 114-204 1.49e-06

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.


Pssm-ID: 433378  Cd Length: 90  Bit Score: 45.35  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 114 LKGKIGKVPVRFLVDSGAQVSVVHPNLWEE----VTDGDLDTlqpfenVVKVANGAEMKILGVWDTaVSLGKLKLKA-QF 188
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVISPSLAERlglkVRGLAYTV------RVSTAGGRVSAARVRLDS-LRLGGLTLENvPA 73

                          90
                  ....*....|....*..
gi 1912229890 189 LVANASAE-EAIIGTDV 204
Cdd:pfam13650  74 LVLDLGDLiDGLLGMDF 90
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 113-216 3.02e-05

RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI.


Pssm-ID: 133146  Cd Length: 124  Bit Score: 42.54  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 113 YLKGKIGKVPVRFLVDSGAQVSVVHPNLWEEV-TDGDLDTlqpfeNVVKVANG-AEMKILG-VWDTAVSLGKLKLKAQFL 189
Cdd:cd05479    18 YINVEINGVPVKAFVDSGAQMTIMSKACAEKCgLMRLIDK-----RFQGIAKGvGTQKILGrIHLAQVKIGNLFLPCSFT 92

                          90       100
                  ....*....|....*....|....*..
gi 1912229890 190 VANASAEEAIIGTDVLQDHNAILDFEH 216
Cdd:cd05479    93 VLEDDDVDFLIGLDMLKRHQCVIDLKE 119
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 113-213 1.68e-04

Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to retroviral proteases which implies they function proteolytically during regulated protein turnover.


Pssm-ID: 312981  Cd Length: 124  Bit Score: 40.41  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 113 YLKGKIGKVPVRFLVDSGAQVSVVHPNLWEEV-TDGDLDTlqpfeNVVKVANGAEM-KILG-VWDTAVSLGKLKLKAQFL 189
Cdd:pfam09668  26 YINCEINGVPVKAFVDSGAQTSIMSPRCAERCgIMRLVDT-----RFAGIAKGVGTaRILGrIHMADVKIGGLFLPCSFS 100

                          90       100
                  ....*....|....*....|....
gi 1912229890 190 VANASAEEAIIGTDVLQDHNAILD 213
Cdd:pfam09668 101 VIEGQDMDLLLGLDMLKRHQCCID 124
retropepsin_like_LTR_2 cd05484
Retropepsins_like_LTR, pepsin-like aspartate proteases; Retropepsin of retrotransposons with ...
 112-181 4.40e-04

Retropepsins_like_LTR, pepsin-like aspartate proteases; Retropepsin of retrotransposons with long terminal repeats are pepsin-like aspartate proteases. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133151  Cd Length: 91  Bit Score: 38.34  E-value: 4.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 112 YYLKGKIGKVPVRFLVDSGAQVSVVHPNLWEEVTDGDldtLQPFENVVKVANGAEMKILGVWDTAVSLGK 181
Cdd:cd05484     1 KTVTLLVNGKPLKFQLDTGSAITVISEKTWRKLGSPP---LKPTKKRLRTATGTKLSVLGQILVTVKYGG 67
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
91-214 4.64e-04

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 39.55  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890  91 PGAAPSH-LPKEIVFANSMGKGYYLKGKIGKVPVRFLVDSGAQVSVVHPNLWEE--VTDGDLDTLQPfenvVKVANGAEM 167
Cdd:COG3577    20 PGQAPVStGGGEVVLKRDRDGHFVVEGTINGQPVRFLVDTGASTVVLSESDARRlgLDPEDLGRPVR----VQTANGVVR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1912229890 168 KILGVWDTaVSLGKLKLK-AQFLVANASA-EEAIIGTDVLQDHNAILDF 214
Cdd:COG3577    96 AARVRLDS-VRIGGITLRnVRAVVLPGGElDDGLLGMSFLGRLDFEIDG 143
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
 117-206 1.23e-03

Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133159  Cd Length: 86  Bit Score: 36.93  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 117 KIGKVPVRFLVDSGAQVSVVHPNLweevtdGDLDTLQPFENVVKVANGAEMKILGVWDTAVSLGKLKLKAQFLVANASAe 196
Cdd:cd06095     4 TVEGVPIVFLVDTGATHSVLKSDL------GPKQELSTTSVLIRGVSGQSQQPVTTYRTLVDLGGHTVSHSFLVVPNCP- 76

                          90
                  ....*....|
gi 1912229890 197 EAIIGTDVLQ 206
Cdd:cd06095    77 DPLLGRDLLS 86
retropepsin_like_LTR_1 cd05481
Retropepsins_like_LTR; pepsin-like aspartate protease from retrotransposons with long terminal ...
 119-201 1.42e-03

Retropepsins_like_LTR; pepsin-like aspartate protease from retrotransposons with long terminal repeats; Retropepsin of retrotransposons with long terminal repeats are pepsin-like aspartate proteases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133148  Cd Length: 93  Bit Score: 36.86  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229890 119 GKVPVRFLVDSGAQVSVVHPNLWEEVTDGDLDTLQPfENVVKVA-NGAEMKILGVWDTAVSLGKLKLKAQFLVANASaEE 197
Cdd:cd05481     7 GKQSVKFQLDTGATCNVLPLRWLKSLTPDKDPELRP-SPVRLTAyGGSTIPVEGGVKLKCRYRNPKYNLTFQVVKEE-GP 84


                  ....
gi 1912229890 198 AIIG 201
Cdd:cd05481    85 PLLG 88
 
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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