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Conserved domains on  [gi|1883607505|ref|WP_181364625|]
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MULTISPECIES: ATP-dependent zinc protease [Aeromonas]

Protein Classification

ATP-dependent zinc protease( domain architecture ID 10008226)

ATP-dependent zinc protease such as retroviral-like aspartic protease, which contains a conserved active site motif (Asp-Thr/Ser-Gly-Ser) and belongs to a family that includes both cellular and retroviral pepsin-like aspartate proteases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4067 COG4067
Uncharacterized conserved protein [Function unknown];
105-247 2.44e-64

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443244  Cd Length: 150  Bit Score: 197.33  E-value: 2.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 105 TVDGKLLVGEAEWIWVDAAN-DAFQARVDTGATTSSISAQDITIFERNGKNWVRFFLSHQEMDDK--IQIEAPLVRHVRV 181
Cdd:COG4067     6 PAADKLIIGWREWVALPELGiPAIKAKIDTGARTSSLHAFNIEEFERDGEDWVRFTVHPPQGDTDteVECEAPVVRRRKI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883607505 182 RQASADdLDRRPVVRLAVRIGDMTEKAEFTLKDRSDMTFPVLLGREFLKDIAVVDVAREYIQPKPK 247
Cdd:COG4067    86 KSSGGH-AERRPVVETPLCLGGQTWEIEFTLTDRSDMNYPMLLGRTALRGRFLVDPSRSFLQGKPC 150
 
Name Accession Description Interval E-value
COG4067 COG4067
Uncharacterized conserved protein [Function unknown];
105-247 2.44e-64

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443244  Cd Length: 150  Bit Score: 197.33  E-value: 2.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 105 TVDGKLLVGEAEWIWVDAAN-DAFQARVDTGATTSSISAQDITIFERNGKNWVRFFLSHQEMDDK--IQIEAPLVRHVRV 181
Cdd:COG4067     6 PAADKLIIGWREWVALPELGiPAIKAKIDTGARTSSLHAFNIEEFERDGEDWVRFTVHPPQGDTDteVECEAPVVRRRKI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883607505 182 RQASADdLDRRPVVRLAVRIGDMTEKAEFTLKDRSDMTFPVLLGREFLKDIAVVDVAREYIQPKPK 247
Cdd:COG4067    86 KSSGGH-AERRPVVETPLCLGGQTWEIEFTLTDRSDMNYPMLLGRTALRGRFLVDPSRSFLQGKPC 150
Zn_protease pfam05618
Putative ATP-dependant zinc protease; Proteins in this family are annotated as being ...
 111-246 1.13e-45

Putative ATP-dependant zinc protease; Proteins in this family are annotated as being ATP-dependant zinc proteases.


Pssm-ID: 283308  Cd Length: 138  Bit Score: 149.60  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 111 LVGEAEWIWVDAANDAFQARVDTGATTSSISAQDITIFERNGKNWVRFFLSHQEMDDKI--QIEAPLVRHVRVRQaSADD 188
Cdd:pfam05618   1 VVGWIEELFLPGLKIQLKAKIDTGALTSSLSAGDIWSFERDGESWVRFKETRLDTKNQRgyTLEAPVLRIVKIRQ-SGGD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1883607505 189 LDRRPVVRLAVRIGDMTEKAEFTLKDRSDMTFPVLLG-REFLKDIAVVDVAREYIQPKP 246
Cdd:pfam05618  80 AERRPVIKLYLCLGPKIERIEFTLTDRSLMKYPVLLGsRALRKHLAEVDPSRKYIRIKE 138
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 131-230 1.31e-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: 37.22  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 131 VDTGATTSSISAQDItiferngknwvrfflshqemdDKIQIEAPLVRHVRVRqaSADDLDRRPVVRLA-VRIGDMT-EKA 208
Cdd:cd05483    18 LDTGASTTVISEELA---------------------ERLGLPLTLGGKVTVQ--TANGRVRAARVRLDsLQIGGITlRNV 74

                          90       100
                  ....*....|....*....|..
gi 1883607505 209 EFTLKDRSDMTFPVLLGREFLK 230
Cdd:cd05483    75 PAVVLPGDALGVDGLLGMDFLR 96
 
Name Accession Description Interval E-value
COG4067 COG4067
Uncharacterized conserved protein [Function unknown];
105-247 2.44e-64

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443244  Cd Length: 150  Bit Score: 197.33  E-value: 2.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 105 TVDGKLLVGEAEWIWVDAAN-DAFQARVDTGATTSSISAQDITIFERNGKNWVRFFLSHQEMDDK--IQIEAPLVRHVRV 181
Cdd:COG4067     6 PAADKLIIGWREWVALPELGiPAIKAKIDTGARTSSLHAFNIEEFERDGEDWVRFTVHPPQGDTDteVECEAPVVRRRKI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883607505 182 RQASADdLDRRPVVRLAVRIGDMTEKAEFTLKDRSDMTFPVLLGREFLKDIAVVDVAREYIQPKPK 247
Cdd:COG4067    86 KSSGGH-AERRPVVETPLCLGGQTWEIEFTLTDRSDMNYPMLLGRTALRGRFLVDPSRSFLQGKPC 150
Zn_protease pfam05618
Putative ATP-dependant zinc protease; Proteins in this family are annotated as being ...
 111-246 1.13e-45

Putative ATP-dependant zinc protease; Proteins in this family are annotated as being ATP-dependant zinc proteases.


Pssm-ID: 283308  Cd Length: 138  Bit Score: 149.60  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 111 LVGEAEWIWVDAANDAFQARVDTGATTSSISAQDITIFERNGKNWVRFFLSHQEMDDKI--QIEAPLVRHVRVRQaSADD 188
Cdd:pfam05618   1 VVGWIEELFLPGLKIQLKAKIDTGALTSSLSAGDIWSFERDGESWVRFKETRLDTKNQRgyTLEAPVLRIVKIRQ-SGGD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1883607505 189 LDRRPVVRLAVRIGDMTEKAEFTLKDRSDMTFPVLLG-REFLKDIAVVDVAREYIQPKP 246
Cdd:pfam05618  80 AERRPVIKLYLCLGPKIERIEFTLTDRSLMKYPVLLGsRALRKHLAEVDPSRKYIRIKE 138
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 131-230 1.31e-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: 37.22  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 131 VDTGATTSSISAQDItiferngknwvrfflshqemdDKIQIEAPLVRHVRVRqaSADDLDRRPVVRLA-VRIGDMT-EKA 208
Cdd:cd05483    18 LDTGASTTVISEELA---------------------ERLGLPLTLGGKVTVQ--TANGRVRAARVRLDsLQIGGITlRNV 74

                          90       100
                  ....*....|....*....|..
gi 1883607505 209 EFTLKDRSDMTFPVLLGREFLK 230
Cdd:cd05483    75 PAVVLPGDALGVDGLLGMDFLR 96
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 128-230 1.79e-03

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: 36.55  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883607505 128 QARVDTGATTSSISAQditIFERNGknwvrffLSHQEMDDKIQIEAPLVRHVRVRQAsaddldrrpVVRLAVRIGDMTEK 207
Cdd:cd00303    11 RALVDSGASVNFISES---LAKKLG-------LPPRLLPTPLKVKGANGSSVKTLGV---------ILPVTIGIGGKTFT 71

                          90       100
                  ....*....|....*....|...
gi 1883607505 208 AEFTLKDrsDMTFPVLLGREFLK 230
Cdd:cd00303    72 VDFYVLD--LLSYDVILGRPWLE 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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