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Conserved domains on  [gi|1043914325|ref|NP_001316462|]
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probable inactive tRNA-specific adenosine deaminase-like protein 3 isoform 2 [Homo sapiens]

Protein Classification

nucleoside deaminase( domain architecture ID 10101196)

nucleoside deaminase (such as as adenosine, guanine, or cytosine deaminase) is a Zn-dependent enzyme which catalyzes the deamination of nucleosides

CATH:  3.40.140.10
EC:  3.5.4.-
Gene Ontology:  GO:0019239|GO:0009116|GO:0008270|GO:0001882
PubMed:  7599282|7599282|12637534
SCOP:  3001838|3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 195-322 5.67e-25

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: 97.30  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDPaSDRVLATGHDCSCADN-PLLHAVMVCVDLVARGQGrgtydfrpfpacsfapaaapqavragavrkldaded 273
Cdd:cd01285    19 FGAVIVDD-DGKVIARGHNRVEQDGdPTAHAEIVAIRNAARRLG------------------------------------ 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1043914325 274 glPYLCTGYDLYVTREPCAMCAMALVHARILRVFYGAPSPD-GALGTRFR 322
Cdd:cd01285    62 --SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPKlGGIGFLIE 109
 
Name Accession Description Interval E-value
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 195-322 5.67e-25

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: 97.30  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDPaSDRVLATGHDCSCADN-PLLHAVMVCVDLVARGQGrgtydfrpfpacsfapaaapqavragavrkldaded 273
Cdd:cd01285    19 FGAVIVDD-DGKVIARGHNRVEQDGdPTAHAEIVAIRNAARRLG------------------------------------ 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1043914325 274 glPYLCTGYDLYVTREPCAMCAMALVHARILRVFYGAPSPD-GALGTRFR 322
Cdd:cd01285    62 --SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPKlGGIGFLIE 109
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 195-345 5.15e-24

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: 95.96  E-value: 5.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDpaSDRVLATGHDCSCADN-PLLHAVMVcvdlvargqgrgtydfrpfpacsfapaaapqAVRAgAVRKLdaded 273
Cdd:COG0590    26 VGAVLVK--DGEIIARGHNRVETLNdPTAHAEIL-------------------------------AIRA-AARKL----- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1043914325 274 GLPYLcTGYDLYVTREPCAMCAMALVHARILRVFYGAPSPD-GALGTRFRIHARPDLNHRFQVFRGVLEEQCR 345
Cdd:COG0590    67 GNWRL-SGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPKaGAAGSIYDLLADPRLNHRVEVVGGVLAEECA 138
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 284-344 1.41e-13

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 67.91  E-value: 1.41e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1043914325 284 LYVTREPCAMCAMALVHARILRVFYGA-PSPDGALGTRFRIHARPDLNHRFQVFRGVLEEQC 344
Cdd:PRK10860   85 LYVTLEPCVMCAGAMVHSRIGRLVFGArDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADEC 146
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
195-309 6.65e-12

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 61.16  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDPaSDRVLATGHDCSCADNPL-LHAVMVCVDlvargqgrgtydfrpfpacsfapaaapQAVRAGAVRKLDaded 273
Cdd:pfam00383  24 VGAVIVKK-DGEIIATGYNGENAGYDPtIHAERNAIR---------------------------QAGKRGEGVRLE---- 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1043914325 274 glpylctGYDLYVTREPCAMCAMALVHARILRVFYG 309
Cdd:pfam00383  72 -------GATLYVTLEPCGMCAQAIIESGIKRVVFG 100
 
Name Accession Description Interval E-value
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 195-322 5.67e-25

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: 97.30  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDPaSDRVLATGHDCSCADN-PLLHAVMVCVDLVARGQGrgtydfrpfpacsfapaaapqavragavrkldaded 273
Cdd:cd01285    19 FGAVIVDD-DGKVIARGHNRVEQDGdPTAHAEIVAIRNAARRLG------------------------------------ 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1043914325 274 glPYLCTGYDLYVTREPCAMCAMALVHARILRVFYGAPSPD-GALGTRFR 322
Cdd:cd01285    62 --SYLLSGCTLYTTLEPCPMCAGALLWARIKRVVYGASDPKlGGIGFLIE 109
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 195-345 5.15e-24

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: 95.96  E-value: 5.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDpaSDRVLATGHDCSCADN-PLLHAVMVcvdlvargqgrgtydfrpfpacsfapaaapqAVRAgAVRKLdaded 273
Cdd:COG0590    26 VGAVLVK--DGEIIARGHNRVETLNdPTAHAEIL-------------------------------AIRA-AARKL----- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1043914325 274 GLPYLcTGYDLYVTREPCAMCAMALVHARILRVFYGAPSPD-GALGTRFRIHARPDLNHRFQVFRGVLEEQCR 345
Cdd:COG0590    67 GNWRL-SGCTLYVTLEPCPMCAGAIVWARIGRVVYGASDPKaGAAGSIYDLLADPRLNHRVEVVGGVLAEECA 138
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 284-344 1.41e-13

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 67.91  E-value: 1.41e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1043914325 284 LYVTREPCAMCAMALVHARILRVFYGA-PSPDGALGTRFRIHARPDLNHRFQVFRGVLEEQC 344
Cdd:PRK10860   85 LYVTLEPCVMCAGAMVHSRIGRLVFGArDAKTGAAGSLMDVLHHPGMNHRVEITEGVLADEC 146
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
195-309 6.65e-12

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 61.16  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDPaSDRVLATGHDCSCADNPL-LHAVMVCVDlvargqgrgtydfrpfpacsfapaaapQAVRAGAVRKLDaded 273
Cdd:pfam00383  24 VGAVIVKK-DGEIIATGYNGENAGYDPtIHAERNAIR---------------------------QAGKRGEGVRLE---- 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1043914325 274 glpylctGYDLYVTREPCAMCAMALVHARILRVFYG 309
Cdd:pfam00383  72 -------GATLYVTLEPCGMCAQAIIESGIKRVVFG 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 284-342 4.43e-08

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: 51.75  E-value: 4.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1043914325 284 LYVTREPCAMCAMALVHARILRVFYGAPSPD-GALG---TRFRIHARpdlNHRFQVFRGVLEE 342
Cdd:pfam14437  75 LYVTLEPCPMCAGAIVQAGLKSLVYGAGNPKgGAVGsvlNKLVIVLW---NHRVELVEEDCSE 134
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 195-315 4.62e-07

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: 48.42  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043914325 195 VGAVVVDpaSDRVLATGHDCS------CADnpllhaVMVCVDLVARGQGRGtydfrpFPACSFAPA-AAPQAVRAGAVRK 267
Cdd:cd01286    22 VGAVIVK--DKRIISTGYNGSpsglphCAE------VGCERDDLPSGEDQK------CCRTVHAEQnAILQAARHGVSLE 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1043914325 268 ldadedglpylctGYDLYVTREPCAMCAMALVHARILRVFYGAPSPDG 315
Cdd:cd01286    88 -------------GATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDD 122
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
284-316 1.08e-05

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 44.83  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1043914325 284 LYVTREPCAMCAMALVHARILRVFYGAPSPDGA 316
Cdd:COG2131   101 LYVTHFPCLECAKMIIQAGIKRVVYLEDYPDEL 133
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 283-347 4.98e-03

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 38.50  E-value: 4.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1043914325 283 DLYVTREPCAM------CAMALVHARILRVFYGAPSPD------GAlgTRFRiharpdlNHRFQVFRGVLEEQCRWL 347
Cdd:COG0117    64 TLYVTLEPCSHhgrtppCADALIEAGIKRVVIAMLDPNplvagkGI--ARLR-------AAGIEVEVGVLEEEARAL 131
 
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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