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Conserved domains on  [gi|442619566|ref|NP_001262661|]
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uncharacterized protein Dmel_CG5292, isoform B [Drosophila melanogaster]

Protein Classification

nucleoside deaminase( domain architecture ID 10001752)

nucleoside deaminase such as adenosine, guanine, or cytosine deaminase is a Zn-dependent enzyme which catalyzes the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer

EC:  3.5.4.-
Gene Ontology:  GO:0008270|GO:0019239|GO:0009116
PubMed:  38524700
SCOP:  3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-146 6.38e-41

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


:

Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 134.09  E-value: 6.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   1 MAAFMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEficIDAILASCRER---RLparqlfSEI 77
Cdd:COG0590    4 DEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAE---ILAIRAAARKLgnwRL------SGC 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619566  78 TVVVTVEPCIMCSAALHTLGVKEIIYGCENDRFGG-KTVVDVAA--VVGHRIEITGGVRADEAMALLKDFYK 146
Cdd:COG0590   75 TLYVTLEPCPMCAGAIVWARIGRVVYGASDPKAGAaGSIYDLLAdpRLNHRVEVVGGVLAEECAALLRDFFA 146
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-146 6.38e-41

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 134.09  E-value: 6.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   1 MAAFMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEficIDAILASCRER---RLparqlfSEI 77
Cdd:COG0590    4 DEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAE---ILAIRAAARKLgnwRL------SGC 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619566  78 TVVVTVEPCIMCSAALHTLGVKEIIYGCENDRFGG-KTVVDVAA--VVGHRIEITGGVRADEAMALLKDFYK 146
Cdd:COG0590   75 TLYVTLEPCPMCAGAIVWARIGRVVYGASDPKAGAaGSIYDLLAdpRLNHRVEVVGGVLAEECAALLRDFFA 146
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 5-112 1.05e-35

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 119.64  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   5 MEEALVEARRARDAGEVPVGCVFVHGD-KVVARGGNEVNVHRNATRHAEFICIDAILASCRERRLparqlfSEITVVVTV 83
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLL------SGCTLYTTL 74

                         90       100
                 ....*....|....*....|....*....
gi 442619566  84 EPCIMCSAALHTLGVKEIIYGCENDRFGG 112
Cdd:cd01285   75 EPCPMCAGALLWARIKRVVYGASDPKLGG 103
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 4-146 7.33e-25

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 94.10  E-value: 7.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   4 FMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEFICIDAILASCRERRLparqlfSEITVVVTV 83
Cdd:PRK10860  16 WMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRL------LDATLYVTL 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619566  84 EPCIMCSAALHTLGVKEIIYGCENDRFGGK-TVVDVAAVVG--HRIEITGGVRADEAMALLKDFYK 146
Cdd:PRK10860  90 EPCVMCAGAMVHSRIGRLVFGARDAKTGAAgSLMDVLHHPGmnHRVEITEGVLADECAALLSDFFR 155
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 3-146 1.29e-21

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 84.88  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566    3 AFMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEficIDAILASCRERrlpARQLFSEITVVVT 82
Cdd:pfam14437   5 KWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAE---ILAIQQAAKKL---GSWRLDDATLYVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442619566   83 VEPCIMCSAALHTLGVKEIIYGCENDRFGG-KTVVDVAAVV--GHRIEitggVRADEAMALLKDFYK 146
Cdd:pfam14437  79 LEPCPMCAGAIVQAGLKSLVYGAGNPKGGAvGSVLNKLVIVlwNHRVE----LVEEDCSEILKGFFK 141
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-146 6.38e-41

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 134.09  E-value: 6.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   1 MAAFMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEficIDAILASCRER---RLparqlfSEI 77
Cdd:COG0590    4 DEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAE---ILAIRAAARKLgnwRL------SGC 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619566  78 TVVVTVEPCIMCSAALHTLGVKEIIYGCENDRFGG-KTVVDVAA--VVGHRIEITGGVRADEAMALLKDFYK 146
Cdd:COG0590   75 TLYVTLEPCPMCAGAIVWARIGRVVYGASDPKAGAaGSIYDLLAdpRLNHRVEVVGGVLAEECAALLRDFFA 146
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 5-112 1.05e-35

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 119.64  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   5 MEEALVEARRARDAGEVPVGCVFVHGD-KVVARGGNEVNVHRNATRHAEFICIDAILASCRERRLparqlfSEITVVVTV 83
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDDgKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLL------SGCTLYTTL 74

                         90       100
                 ....*....|....*....|....*....
gi 442619566  84 EPCIMCSAALHTLGVKEIIYGCENDRFGG 112
Cdd:cd01285   75 EPCPMCAGALLWARIKRVVYGASDPKLGG 103
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 4-146 7.33e-25

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 94.10  E-value: 7.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   4 FMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEFICIDAILASCRERRLparqlfSEITVVVTV 83
Cdd:PRK10860  16 WMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRL------LDATLYVTL 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619566  84 EPCIMCSAALHTLGVKEIIYGCENDRFGGK-TVVDVAAVVG--HRIEITGGVRADEAMALLKDFYK 146
Cdd:PRK10860  90 EPCVMCAGAMVHSRIGRLVFGARDAKTGAAgSLMDVLHHPGmnHRVEITEGVLADECAALLSDFFR 155
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 3-146 1.29e-21

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 84.88  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566    3 AFMEEALVEARRARDAGEVPVGCVFVHGDKVVARGGNEVNVHRNATRHAEficIDAILASCRERrlpARQLFSEITVVVT 82
Cdd:pfam14437   5 KWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAE---ILAIQQAAKKL---GSWRLDDATLYVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442619566   83 VEPCIMCSAALHTLGVKEIIYGCENDRFGG-KTVVDVAAVV--GHRIEitggVRADEAMALLKDFYK 146
Cdd:pfam14437  79 LEPCPMCAGAIVQAGLKSLVYGAGNPKGGAvGSVLNKLVIVlwNHRVE----LVEEDCSEILKGFFK 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
3-104 2.10e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 83.12  E-value: 2.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566    3 AFMEEALVEARRARDAGEVPVGCVFVHGD-KVVARGGNEVNVHRNATRHAEFICIDAILascrerRLPARQLFSEITVVV 81
Cdd:pfam00383   4 YFMRLALKAAKRAYPYSNFPVGAVIVKKDgEIIATGYNGENAGYDPTIHAERNAIRQAG------KRGEGVRLEGATLYV 77

                          90       100
                  ....*....|....*....|...
gi 442619566   82 TVEPCIMCSAALHTLGVKEIIYG 104
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRVVFG 100
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 4-103 1.56e-06

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 44.96  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   4 FMEEALVEARRARDAGeVPVGCVFVHGDKVVARGGN---------------------EVNVHRNATRHAEficIDAILAS 62
Cdd:cd01286    4 FMAIARLAALRSTCPR-RQVGAVIVKDKRIISTGYNgspsglphcaevgcerddlpsGEDQKCCRTVHAE---QNAILQA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442619566  63 CRERRLPARQlfseiTVVVTVEPCIMCSAALHTLGVKEIIY 103
Cdd:cd01286   80 ARHGVSLEGA-----TLYVTLFPCIECAKLIIQAGIKKVVY 115
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 5-106 2.19e-05

Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.


Pssm-ID: 238611 [Multi-domain]  Cd Length: 115  Bit Score: 41.45  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   5 MEEALVEARRARdaGEV----PVGCVFVHGD-KVVARGgnevnVHRNA-TRHAEficIDAiLASCRERRLPArqlfseIT 78
Cdd:cd01284    1 MRRALELAEKGR--GLTspnpPVGCVIVDDDgEIVGEG-----YHRKAgGPHAE---VNA-LASAGEKLARG------AT 63

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442619566  79 VVVTVEPCIM------CSAALHTLGVKEIIYGCE 106
Cdd:cd01284   64 LYVTLEPCSHhgktppCVDAIIEAGIKRVVVGVR 97
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 5-102 4.22e-04

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 37.53  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619566   5 MEEALVEARRARDA-GEVPVGCVFV--HGDKVVARGGNEVNVHRNATRHAEficIDAILASCRERRLPARQLFseitvvV 81
Cdd:cd00786    1 MTEALKAADLGYAKeSNFQVGACLVnkKDGGKVGRGCNIENAAYSMCNHAE---RTALFNAGSEGDTKGQMLY------V 71

                         90       100
                 ....*....|....*....|.
gi 442619566  82 TVEPCIMCSAALHTLGVKEII 102
Cdd:cd00786   72 ALSPCGACAQLIIELGIKDVI 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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