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Conserved domains on  [gi|516455754|ref|WP_017844595|]
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MULTISPECIES: arginase [Pseudomonas]

Protein Classification

arginase family protein( domain architecture ID 98571)

arginase family protein is a metal-dependent enzyme that catalyzes the hydrolysis of an amide bond, such as arginase-like amidino hydrolases and histone/histone-like deacetylases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
6-223 2.16e-09

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


The actual alignment was detected with superfamily member cd09990:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 275  Bit Score: 57.18  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754   6 LDHSLTGQ-----APIARRLASGHATR------------LDLLDLGP-KLRLWSTEKTWKRFTERLAARPRpTDARPeiL 67
Cdd:cd09990    8 FDGGSTSRpgarfGPRAIREASAGYSTyspdlgvddfddLTVVDYGDvPVDPGDIEKTFDRIREAVAEIAE-AGAIP--I 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754  68 FVGsGDyHHLTP----AFLADLKEPISLIHFDNHPDW--VRFAPKRHCGSWVNRALKMPAI--KRIVTLGpcsddlhnpq 139
Cdd:cd09990   85 VLG-GD-HSITYpavrGLAERHKGKVGVIHFDAHLDTrdTDGGGELSHGTPFRRLLEDGNVdgENIVQIG---------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754 140 LRGgnlgaltrgqlqlfPWQHPPSKVWGRvgdGAGHqqqeNYLYWRNLAELDWAAFLEQMIS--SLPTEAIWITIDKDVL 217
Cdd:cd09990  153 IRG--------------FWNSPEYVEYAR---EQGV----TVITMRDVRERGLDAVIEEALEiaSDGTDAVYVSVDIDVL 211

                 ....*.
gi 516455754 218 aseDAA 223
Cdd:cd09990  212 ---DPA 214
 
Name Accession Description Interval E-value
Agmatinase-like cd09990
Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as ...
6-223 2.16e-09

Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as agmatinase, guanidinobutyrase, guanidopropionase, formimidoylglutamase and proclavaminate amidinohydrolase. Agmatinase (agmatine ureohydrolase; SpeB; EC=3.5.3.11) is the key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield putrescine and urea. This enzyme has been found in bacteria, archaea and eukaryotes, requiring divalent Mn and sometimes Zn, Co or Ca for activity. In mammals, the highest level of agmatinase mRNA was found in liver and kidney. However, catabolism of agmatine via agmatinase apparently is a not major path; it is mostly catabolized via diamine oxidase. Agmatinase has been shown to be down-regulated in tumor renal cells. Guanidinobutyrase (Gbh, EC=3.5.3.7) catalyzes hydrolysis of 4-guanidinobutanoate to yield 4-aminobutanoate and urea in arginine degradation pathway. Activity has been shown for purified enzyme from Arthrobacter sp. KUJ 8602. Additionally, guanidinobutyrase is able to hydrolyze D-arginine, 3-guanidinopropionate, 5-guanidinovaleriate and L-arginine with much less affinity, having divalent Zn ions for catalysis. Proclavaminate amidinohydrolase (Pah, EC 3.5.3.22) hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Activity has been shown for purified enzyme from Streptomyces clavuligerus. Clavulanic acid is the effective inhibitor of beta-lactamases. This acid is used in combination with the penicillin amoxicillin to prevent antibiotic's beta-lactam rings from hydrolysis, thus keeping the antibiotics biologically active.


Pssm-ID: 212516 [Multi-domain]  Cd Length: 275  Bit Score: 57.18  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754   6 LDHSLTGQ-----APIARRLASGHATR------------LDLLDLGP-KLRLWSTEKTWKRFTERLAARPRpTDARPeiL 67
Cdd:cd09990    8 FDGGSTSRpgarfGPRAIREASAGYSTyspdlgvddfddLTVVDYGDvPVDPGDIEKTFDRIREAVAEIAE-AGAIP--I 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754  68 FVGsGDyHHLTP----AFLADLKEPISLIHFDNHPDW--VRFAPKRHCGSWVNRALKMPAI--KRIVTLGpcsddlhnpq 139
Cdd:cd09990   85 VLG-GD-HSITYpavrGLAERHKGKVGVIHFDAHLDTrdTDGGGELSHGTPFRRLLEDGNVdgENIVQIG---------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754 140 LRGgnlgaltrgqlqlfPWQHPPSKVWGRvgdGAGHqqqeNYLYWRNLAELDWAAFLEQMIS--SLPTEAIWITIDKDVL 217
Cdd:cd09990  153 IRG--------------FWNSPEYVEYAR---EQGV----TVITMRDVRERGLDAVIEEALEiaSDGTDAVYVSVDIDVL 211

                 ....*.
gi 516455754 218 aseDAA 223
Cdd:cd09990  212 ---DPA 214
 
Name Accession Description Interval E-value
Agmatinase-like cd09990
Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as ...
6-223 2.16e-09

Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as agmatinase, guanidinobutyrase, guanidopropionase, formimidoylglutamase and proclavaminate amidinohydrolase. Agmatinase (agmatine ureohydrolase; SpeB; EC=3.5.3.11) is the key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield putrescine and urea. This enzyme has been found in bacteria, archaea and eukaryotes, requiring divalent Mn and sometimes Zn, Co or Ca for activity. In mammals, the highest level of agmatinase mRNA was found in liver and kidney. However, catabolism of agmatine via agmatinase apparently is a not major path; it is mostly catabolized via diamine oxidase. Agmatinase has been shown to be down-regulated in tumor renal cells. Guanidinobutyrase (Gbh, EC=3.5.3.7) catalyzes hydrolysis of 4-guanidinobutanoate to yield 4-aminobutanoate and urea in arginine degradation pathway. Activity has been shown for purified enzyme from Arthrobacter sp. KUJ 8602. Additionally, guanidinobutyrase is able to hydrolyze D-arginine, 3-guanidinopropionate, 5-guanidinovaleriate and L-arginine with much less affinity, having divalent Zn ions for catalysis. Proclavaminate amidinohydrolase (Pah, EC 3.5.3.22) hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Activity has been shown for purified enzyme from Streptomyces clavuligerus. Clavulanic acid is the effective inhibitor of beta-lactamases. This acid is used in combination with the penicillin amoxicillin to prevent antibiotic's beta-lactam rings from hydrolysis, thus keeping the antibiotics biologically active.


Pssm-ID: 212516 [Multi-domain]  Cd Length: 275  Bit Score: 57.18  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754   6 LDHSLTGQ-----APIARRLASGHATR------------LDLLDLGP-KLRLWSTEKTWKRFTERLAARPRpTDARPeiL 67
Cdd:cd09990    8 FDGGSTSRpgarfGPRAIREASAGYSTyspdlgvddfddLTVVDYGDvPVDPGDIEKTFDRIREAVAEIAE-AGAIP--I 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754  68 FVGsGDyHHLTP----AFLADLKEPISLIHFDNHPDW--VRFAPKRHCGSWVNRALKMPAI--KRIVTLGpcsddlhnpq 139
Cdd:cd09990   85 VLG-GD-HSITYpavrGLAERHKGKVGVIHFDAHLDTrdTDGGGELSHGTPFRRLLEDGNVdgENIVQIG---------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455754 140 LRGgnlgaltrgqlqlfPWQHPPSKVWGRvgdGAGHqqqeNYLYWRNLAELDWAAFLEQMIS--SLPTEAIWITIDKDVL 217
Cdd:cd09990  153 IRG--------------FWNSPEYVEYAR---EQGV----TVITMRDVRERGLDAVIEEALEiaSDGTDAVYVSVDIDVL 211

                 ....*.
gi 516455754 218 aseDAA 223
Cdd:cd09990  212 ---DPA 214
 
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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