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Conserved domains on  [gi|1370459768|ref|XP_024304377|]
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nuclear receptor-interacting protein 3 isoform X1 [Homo sapiens]

Protein Classification

pepsin/retropepsin-like aspartic protease family protein; aspartic protease/reverse transcriptase family protein( domain architecture ID 10144466)

pepsin/retropepsin-like aspartic protease family protein| aspartic protease/reverse transcriptase (RT) family protein may hydrolyze the peptide bonds of substrates and/or catalyze the conversion of single-stranded RNA into double-stranded DNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NRIP_C cd05480
NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been ...
 42-144 3.76e-55

NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been described as probable nuclear receptor interacting proteins. The C-terminal domain of this family is homologous to the retroviral aspartyl protease domain. The domain is structurally related to one lobe of the pepsin molecule. The conserved active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. 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: 133147  Cd Length: 103  Bit Score: 169.27  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  42 VSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKHEGEKLSLPRHLKVVGQIEHLVITLGSLRLDCPAAVVDD 121
Cdd:cd05480     1 VSCQCAGKELRALVDTGCQYNLISAACLDRLGLKERVLKAKAEEEAPSLPTSVKVIGQIERLVLQLGQLTVECSAQVVDD 80

                          90       100
                  ....*....|....*....|...
gi 1370459768 122 NEKNLSLGLQTLRSLKCIINLDK 144
Cdd:cd05480    81 NEKNFSLGLQTLKSLKCVINLEK 103
 
Name Accession Description Interval E-value
NRIP_C cd05480
NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been ...
 42-144 3.76e-55

NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been described as probable nuclear receptor interacting proteins. The C-terminal domain of this family is homologous to the retroviral aspartyl protease domain. The domain is structurally related to one lobe of the pepsin molecule. The conserved active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. 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: 133147  Cd Length: 103  Bit Score: 169.27  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  42 VSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKHEGEKLSLPRHLKVVGQIEHLVITLGSLRLDCPAAVVDD 121
Cdd:cd05480     1 VSCQCAGKELRALVDTGCQYNLISAACLDRLGLKERVLKAKAEEEAPSLPTSVKVIGQIERLVLQLGQLTVECSAQVVDD 80

                          90       100
                  ....*....|....*....|...
gi 1370459768 122 NEKNLSLGLQTLRSLKCIINLDK 144
Cdd:cd05480    81 NEKNFSLGLQTLKSLKCVINLEK 103
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 39-141 2.14e-08

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: 50.04  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  39 MILVSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKH---EGEKLSlprhlKVVGQIEHLVITLGSLRLDCP 115
Cdd:pfam09668  24 MLYINCEINGVPVKAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAgiaKGVGTA-----RILGRIHMADVKIGGLFLPCS 98

                          90       100
                  ....*....|....*....|....*.
gi 1370459768 116 AAVVDDNEKNLSLGLQTLRSLKCIIN 141
Cdd:pfam09668  99 FSVIEGQDMDLLLGLDMLKRHQCCID 124
 
Name Accession Description Interval E-value
NRIP_C cd05480
NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been ...
 42-144 3.76e-55

NRIP_C; putative nuclear receptor interacting protein; Proteins in this family have been described as probable nuclear receptor interacting proteins. The C-terminal domain of this family is homologous to the retroviral aspartyl protease domain. The domain is structurally related to one lobe of the pepsin molecule. The conserved active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. 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: 133147  Cd Length: 103  Bit Score: 169.27  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  42 VSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKHEGEKLSLPRHLKVVGQIEHLVITLGSLRLDCPAAVVDD 121
Cdd:cd05480     1 VSCQCAGKELRALVDTGCQYNLISAACLDRLGLKERVLKAKAEEEAPSLPTSVKVIGQIERLVLQLGQLTVECSAQVVDD 80

                          90       100
                  ....*....|....*....|...
gi 1370459768 122 NEKNLSLGLQTLRSLKCIINLDK 144
Cdd:cd05480    81 NEKNFSLGLQTLKSLKCVINLEK 103
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 42-134 1.03e-09

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: 52.72  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  42 VSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKHegeKLSLP--RHLKVVGQIEHLVITLGSLRLDCPAAVV 119
Cdd:cd00303     1 LKGKINGVPVRALVDSGASVNFISESLAKKLGLPPRLLPTPL---KVKGAngSSVKTLGVILPVTIGIGGKTFTVDFYVL 77

                          90
                  ....*....|....*
gi 1370459768 120 DDNEKNLSLGLQTLR 134
Cdd:cd00303    78 DLLSYDVILGRPWLE 92
RP_DDI cd05479
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ...
 39-148 9.68e-09

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: 51.01  E-value: 9.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  39 MILVSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKShKHEGEKLSLPRHlKVVGQIeHLV-ITLGSLRLDCPAA 117
Cdd:cd05479    16 MLYINVEINGVPVKAFVDSGAQMTIMSKACAEKCGLMRLIDK-RFQGIAKGVGTQ-KILGRI-HLAqVKIGNLFLPCSFT 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370459768 118 VVDDNEKNLSLGLQTLRSLKCIINLDKHRLI 148
Cdd:cd05479    93 VLEDDDVDFLIGLDMLKRHQCVIDLKENVLR 123
Asp_protease pfam09668
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ...
 39-141 2.14e-08

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: 50.04  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  39 MILVSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKH---EGEKLSlprhlKVVGQIEHLVITLGSLRLDCP 115
Cdd:pfam09668  24 MLYINCEINGVPVKAFVDSGAQTSIMSPRCAERCGIMRLVDTRFAgiaKGVGTA-----RILGRIHMADVKIGGLFLPCS 98

                          90       100
                  ....*....|....*....|....*.
gi 1370459768 116 AAVVDDNEKNLSLGLQTLRSLKCIIN 141
Cdd:pfam09668  99 FSVIEGQDMDLLLGLDMLKRHQCCID 124
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 42-134 4.61e-06

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: 42.95  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459768  42 VSCQCAGKDVKALVDTGCLYNLISLACVDRLGLKehvkshkheGEKLSLPRHLK-VVGQIEHLVITLGSLRL------DC 114
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERLGLD---------RLVDAYPVTVRtANGTVRAARVRLDSVKIggielrNV 71

                          90       100
                  ....*....|....*....|
gi 1370459768 115 PAAVVDDNEKNLSLGLQTLR 134
Cdd:pfam13975  72 PAVVLPGDLDDVLLGMDFLK 91
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 48-123 3.31e-05

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: 40.73  E-value: 3.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459768  48 GKDVKALVDTGCLYNLISLACVDRLGLKEHVKSHKHEGEKLSLPRHLKVVgQIEHLviTLGSLRL-DCPAAVVDDNE 123
Cdd:pfam13650   7 GKPVRFLVDTGASGTVISPSLAERLGLKVRGLAYTVRVSTAGGRVSAARV-RLDSL--RLGGLTLeNVPALVLDLGD 80
 
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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