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Conserved domains on  [gi|1083629108|gb|OGH19643|]
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MAG: hypothetical protein A2868_04280 [Candidatus Levybacteria bacterium RIFCSPHIGHO2_01_FULL_40_15b]

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
PubMed:  1851433|2194475|7674916

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 ...
 32-108 1.55e-08

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: 48.87  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  32 PTYALVDSGASISVISTVIADELDIDWMKIPVKTGLAVA----STVRYHPAKVTAEIYGHKFNLLINIAEGLSaHQCILG 107
Cdd:cd00303     9 PVRALVDSGASVNFISESLAKKLGLPPRLLPTPLKVKGAngssVKTLGVILPVTIGIGGKTFTVDFYVLDLLS-YDVILG 87


                  .
gi 1083629108 108 Q 108
Cdd:cd00303    88 R 88
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 32-108 1.55e-08

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: 48.87  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  32 PTYALVDSGASISVISTVIADELDIDWMKIPVKTGLAVA----STVRYHPAKVTAEIYGHKFNLLINIAEGLSaHQCILG 107
Cdd:cd00303     9 PVRALVDSGASVNFISESLAKKLGLPPRLLPTPLKVKGAngssVKTLGVILPVTIGIGGKTFTVDFYVLDLLS-YDVILG 87


                  .
gi 1083629108 108 Q 108
Cdd:cd00303    88 R 88
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 35-114 1.40e-07

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: 46.03  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  35 ALVDSGASISVISTVIADELDIDWMKIPVKTGLAVAS-TVRYHPAKV-TAEIYGHKF-NLLINIAEGlSAHQCILGQrDL 111
Cdd:pfam13975  12 FLVDTGASVTVISEALAERLGLDRLVDAYPVTVRTANgTVRAARVRLdSVKIGGIELrNVPAVVLPG-DLDDVLLGM-DF 89


                  ...
gi 1083629108 112 FQR 114
Cdd:pfam13975  90 LKR 92
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
32-120 3.84e-03

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 35.31  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  32 PTYALVDSGASISVISTVIADELDIDWMKIPVKTGLAVAS-TVRYHPAKV-TAEIYGHKF-NLLINIAEGLSAHQCILGQ 108
Cdd:COG3577    52 PVRFLVDTGASTVVLSESDARRLGLDPEDLGRPVRVQTANgVVRAARVRLdSVRIGGITLrNVRAVVLPGGELDDGLLGM 131

                          90
                  ....*....|..
gi 1083629108 109 rDLFQRAKITFE 120
Cdd:COG3577   132 -SFLGRLDFEID 142
 
Name Accession Description Interval E-value
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 32-108 1.55e-08

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: 48.87  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  32 PTYALVDSGASISVISTVIADELDIDWMKIPVKTGLAVA----STVRYHPAKVTAEIYGHKFNLLINIAEGLSaHQCILG 107
Cdd:cd00303     9 PVRALVDSGASVNFISESLAKKLGLPPRLLPTPLKVKGAngssVKTLGVILPVTIGIGGKTFTVDFYVLDLLS-YDVILG 87


                  .
gi 1083629108 108 Q 108
Cdd:cd00303    88 R 88
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 35-114 1.40e-07

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: 46.03  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  35 ALVDSGASISVISTVIADELDIDWMKIPVKTGLAVAS-TVRYHPAKV-TAEIYGHKF-NLLINIAEGlSAHQCILGQrDL 111
Cdd:pfam13975  12 FLVDTGASVTVISEALAERLGLDRLVDAYPVTVRTANgTVRAARVRLdSVKIGGIELrNVPAVVLPG-DLDDVLLGM-DF 89


                  ...
gi 1083629108 112 FQR 114
Cdd:pfam13975  90 LKR 92
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
32-120 3.84e-03

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 35.31  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  32 PTYALVDSGASISVISTVIADELDIDWMKIPVKTGLAVAS-TVRYHPAKV-TAEIYGHKF-NLLINIAEGLSAHQCILGQ 108
Cdd:COG3577    52 PVRFLVDTGASTVVLSESDARRLGLDPEDLGRPVRVQTANgVVRAARVRLdSVRIGGITLrNVRAVVLPGGELDDGLLGM 131

                          90
                  ....*....|..
gi 1083629108 109 rDLFQRAKITFE 120
Cdd:COG3577   132 -SFLGRLDFEID 142
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 20-108 4.80e-03

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: 34.18  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  20 VPVIFKNKKSEFptyaLVDSGASISVISTVIADELDIDWMKIPVKTGLAVAS-TVRYHPAKV-TAEIYGHKF-NLLINIA 96
Cdd:pfam13650   1 VPVTINGKPVRF----LVDTGASGTVISPSLAERLGLKVRGLAYTVRVSTAGgRVSAARVRLdSLRLGGLTLeNVPALVL 76

                          90
                  ....*....|..
gi 1083629108  97 EGLSAHQCILGQ 108
Cdd:pfam13650  77 DLGDLIDGLLGM 88
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 20-108 6.77e-03

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: 33.76  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083629108  20 VPVIFKNKKSEFptyaLVDSGASISVISTVIADELDIDWMKIPVKTGLAVASTVRYHPAKV-TAEIYGHKF-NLLINIAE 97
Cdd:cd05483     5 VPVTINGQPVRF----LLDTGASTTVISEELAERLGLPLTLGGKVTVQTANGRVRAARVRLdSLQIGGITLrNVPAVVLP 80

                          90
                  ....*....|..
gi 1083629108  98 GLSAH-QCILGQ 108
Cdd:cd05483    81 GDALGvDGLLGM 92
 
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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