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Conserved domains on  [gi|17562080|ref|NP_507927|]
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Peptidase A2 domain-containing protein [Caenorhabditis elegans]

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 human retroviral-like aspartic protease 1

CATH:  2.40.70.10
Gene Ontology:  GO:0004190|GO:0006508
MEROPS:  A2

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 ...
29-118 7.78e-16

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: 67.36  E-value: 7.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  29 VQVGVNGKVVHVLLDTGAGISYLP---ISKINLKDLDPTYQLQAHAANGTPILFHG-IVKLALRMGNRVFEHTLHVSDDK 104
Cdd:cd00303   1 LKGKINGVPVRALVDSGASVNFISeslAKKLGLPPRLLPTPLKVKGANGSSVKTLGvILPVTIGIGGKTFTVDFYVLDLL 80
                        90
                ....*....|....
gi 17562080 105 DCPteMLLGTDFMK 118
Cdd:cd00303  81 SYD--VILGRPWLE 92
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
29-118 7.78e-16

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: 67.36  E-value: 7.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  29 VQVGVNGKVVHVLLDTGAGISYLP---ISKINLKDLDPTYQLQAHAANGTPILFHG-IVKLALRMGNRVFEHTLHVSDDK 104
Cdd:cd00303   1 LKGKINGVPVRALVDSGASVNFISeslAKKLGLPPRLLPTPLKVKGANGSSVKTLGvILPVTIGIGGKTFTVDFYVLDLL 80
                        90
                ....*....|....
gi 17562080 105 DCPteMLLGTDFMK 118
Cdd:cd00303  81 SYD--VILGRPWLE 92
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
29-119 9.22e-14

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: 61.82  E-value: 9.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080    29 VQVGVNGKVVHVLLDTGAGISYLP---ISKINLKDLDPTYQLQAHAANGTPILFHGIVKlALRMGNRVFEH-TLHVSDDK 104
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISealAERLGLDRLVDAYPVTVRTANGTVRAARVRLD-SVKIGGIELRNvPAVVLPGD 79
                          90
                  ....*....|....*
gi 17562080   105 dcPTEMLLGTDFMKK 119
Cdd:pfam13975  80 --LDDVLLGMDFLKR 92
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
17-119 1.75e-10

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 54.95  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  17 ILHKNNRGRlPVVQVGVNGKVVHVLLDTGAGISYLPIS---KINLKDLDPTYQLQAHAANGTPILFHGIVKlALRMGNRV 93
Cdd:COG3577  33 VLKRDRDGH-FVVEGTINGQPVRFLVDTGASTVVLSESdarRLGLDPEDLGRPVRVQTANGVVRAARVRLD-SVRIGGIT 110
                        90       100
                ....*....|....*....|....*..
gi 17562080  94 FEH-TLHVSDDKDcPTEMLLGTDFMKK 119
Cdd:COG3577 111 LRNvRAVVLPGGE-LDDGLLGMSFLGR 136
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
29-118 7.78e-16

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: 67.36  E-value: 7.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  29 VQVGVNGKVVHVLLDTGAGISYLP---ISKINLKDLDPTYQLQAHAANGTPILFHG-IVKLALRMGNRVFEHTLHVSDDK 104
Cdd:cd00303   1 LKGKINGVPVRALVDSGASVNFISeslAKKLGLPPRLLPTPLKVKGANGSSVKTLGvILPVTIGIGGKTFTVDFYVLDLL 80
                        90
                ....*....|....
gi 17562080 105 DCPteMLLGTDFMK 118
Cdd:cd00303  81 SYD--VILGRPWLE 92
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
29-119 9.22e-14

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: 61.82  E-value: 9.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080    29 VQVGVNGKVVHVLLDTGAGISYLP---ISKINLKDLDPTYQLQAHAANGTPILFHGIVKlALRMGNRVFEH-TLHVSDDK 104
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISealAERLGLDRLVDAYPVTVRTANGTVRAARVRLD-SVKIGGIELRNvPAVVLPGD 79
                          90
                  ....*....|....*
gi 17562080   105 dcPTEMLLGTDFMKK 119
Cdd:pfam13975  80 --LDDVLLGMDFLKR 92
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
17-119 1.75e-10

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 54.95  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  17 ILHKNNRGRlPVVQVGVNGKVVHVLLDTGAGISYLPIS---KINLKDLDPTYQLQAHAANGTPILFHGIVKlALRMGNRV 93
Cdd:COG3577  33 VLKRDRDGH-FVVEGTINGQPVRFLVDTGASTVVLSESdarRLGLDPEDLGRPVRVQTANGVVRAARVRLD-SVRIGGIT 110
                        90       100
                ....*....|....*....|....*..
gi 17562080  94 FEH-TLHVSDDKDcPTEMLLGTDFMKK 119
Cdd:COG3577 111 LRNvRAVVLPGGE-LDDGLLGMSFLGR 136
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
29-116 4.35e-10

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: 52.29  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080    29 VQVGVNGKVVHVLLDTGAGISYLPIS---KINLKDLDPTYQLQAHAANGTPILFHGIVKlALRMGNRVFEH-TLHVSDDk 104
Cdd:pfam13650   1 VPVTINGKPVRFLVDTGASGTVISPSlaeRLGLKVRGLAYTVRVSTAGGRVSAARVRLD-SLRLGGLTLENvPALVLDL- 78
                          90
                  ....*....|..
gi 17562080   105 DCPTEMLLGTDF 116
Cdd:pfam13650  79 GDLIDGLLGMDF 90
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
27-118 3.79e-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: 47.62  E-value: 3.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  27 PVVQVGVNGKVVHVLLDTGAGISYLP---ISKINLkDLDPTYQLQAHAANGTpiLFHGIVKLA-LRMGNRVFEH-TLHVS 101
Cdd:cd05483   3 FVVPVTINGQPVRFLLDTGASTTVISeelAERLGL-PLTLGGKVTVQTANGR--VRAARVRLDsLQIGGITLRNvPAVVL 79
                        90
                ....*....|....*..
gi 17562080 102 DDKDCPTEMLLGTDFMK 118
Cdd:cd05483  80 PGDALGVDGLLGMDFLR 96
RP_Saci_like cd06094
RP_Saci_like, retropepsin family; Retropepsin on retrotransposons with long terminal repeats ...
41-118 9.72e-08

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: 46.08  E-value: 9.72e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17562080  41 LLDTGAGISYLPISKINLKDLDPTYQLQahAANGTPILFHGIVKLALRMG-NRVFEHTLHVSddkDCPTEmLLGTDFMK 118
Cdd:cd06094  13 LVDTGAAVSVLPASSTKKSLKPSPLTLQ--AANGTPIATYGTRSLTLDLGlRRPFAWNFVVA---DVPHP-ILGADFLQ 85
retropepsin_like_LTR_2 cd05484
Retropepsins_like_LTR, pepsin-like aspartate proteases; Retropepsin of retrotransposons with ...
29-117 2.69e-06

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: 42.58  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  29 VQVGVNGKVVHVLLDTGAGISYlpIS-----KINLKDLDPTYQlQAHAANGTPILFHGIVKLALRMGNRVFEHTLHVSDD 103
Cdd:cd05484   3 VTLLVNGKPLKFQLDTGSAITV--ISektwrKLGSPPLKPTKK-RLRTATGTKLSVLGQILVTVKYGGKTKVLTLYVVKN 79
                        90
                ....*....|....
gi 17562080 104 KDCPtemLLGTDFM 117
Cdd:cd05484  80 EGLN---LLGRDWL 90
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
22-119 3.64e-04

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: 37.53  E-value: 3.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080  22 NRGRLPVVQVGVNGKVVHVLLDTGAGISYLPIS---KINLKDL-DPTYQLQAHAANGTPILfhGIVKLA-LRMGNRVFEH 96
Cdd:cd05479  12 GKVPMLYINVEINGVPVKAFVDSGAQMTIMSKAcaeKCGLMRLiDKRFQGIAKGVGTQKIL--GRIHLAqVKIGNLFLPC 89
                        90       100
                ....*....|....*....|...
gi 17562080  97 TLHVSDDKDCptEMLLGTDFMKK 119
Cdd:cd05479  90 SFTVLEDDDV--DFLIGLDMLKR 110
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
27-119 1.72e-03

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 35.42  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562080    27 PVVQVGVNGKVVHVLLDTGAGISYLPISkinlkDLDPTYQLQAHAANgtpilFHGI---------VKLALRMGNRVFEHT 97
Cdd:pfam00077   5 PLLTVKIGGKYFTALLDTGADDTVISQN-----DWPTNWPKQKATTN-----IQGIggginvrqsDQILILIGEDKFRGT 74
                          90       100
                  ....*....|....*....|..
gi 17562080    98 LHVSDDKDCPTEmLLGTDFMKK 119
Cdd:pfam00077  75 VSPLILPTCPVN-IIGRDLLQQ 95
 
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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