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Conserved domains on  [gi|516050917|ref|WP_017481500|]
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MULTISPECIES: nucleoside deaminase [Acinetobacter]

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 ...
 1-133 7.36e-53

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: 164.52  E-value: 7.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   1 MEKGEQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASG 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516050917  81 HPCPMCMAGMRIAGIKSVSYAYSNEDGTPFGLstaeIYIELAKPFAEQSMKIQ 133
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGS----IYDLLADPRLNHRVEVV 129
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-133 7.36e-53

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: 164.52  E-value: 7.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   1 MEKGEQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASG 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516050917  81 HPCPMCMAGMRIAGIKSVSYAYSNEDGTPFGLstaeIYIELAKPFAEQSMKIQ 133
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGS----IYDLLADPRLNHRVEVV 129
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 8-106 1.27e-38

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: 126.96  E-value: 1.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   8 LRKAIELAYNNIEKGGRPFGAVVVKN-GEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPCPMC 86
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDdGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|
gi 516050917  87 MAGMRIAGIKSVSYAYSNED 106
Cdd:cd01285   81 AGALLWARIKRVVYGASDPK 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-121 1.96e-25

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: 94.51  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917    5 EQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPCP 84
Cdd:pfam14437   4 EKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPCP 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 516050917   85 MCMAGMRIAGIKSVSYAYSNEDGTPFGLSTAEIYIEL 121
Cdd:pfam14437  84 MCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVL 120
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 5-105 1.82e-18

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 77.54  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   5 EQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPCP 84
Cdd:PRK10860  14 EYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCV 93

                         90       100
                 ....*....|....*....|.
gi 516050917  85 MCMAGMRIAGIKSVSYAYSNE 105
Cdd:PRK10860  94 MCAGAMVHSRIGRLVFGARDA 114
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 25-101 3.93e-07

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 48.29  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   25 PFGAVVVKNGEIIASGVNQilvtNDPTAHAELLAIRAASqvlgtANLEGCSVYASGHPC------PMCMAGMRIAGIKSV 98
Cdd:TIGR00326  20 LVGCVIVKNGEIVGEGAHQ----KAGEPHAEVHALRQAG-----ENAKGATAYVTLEPCshqgrtPPCAEAIIEAGIKKV 90


                  ...
gi 516050917   99 SYA 101
Cdd:TIGR00326  91 VVS 93
 
Name Accession Description Interval E-value
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 1-133 7.36e-53

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: 164.52  E-value: 7.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   1 MEKGEQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASG 80
Cdd:COG0590    1 MEDDEEFMRRALELARKAVAEGEVPVGAVLVKDGEIIARGHNRVETLNDPTAHAEILAIRAAARKLGNWRLSGCTLYVTL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516050917  81 HPCPMCMAGMRIAGIKSVSYAYSNEDGTPFGLstaeIYIELAKPFAEQSMKIQ 133
Cdd:COG0590   81 EPCPMCAGAIVWARIGRVVYGASDPKAGAAGS----IYDLLADPRLNHRVEVV 129
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 8-106 1.27e-38

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: 126.96  E-value: 1.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   8 LRKAIELAYNNIEKGGRPFGAVVVKN-GEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPCPMC 86
Cdd:cd01285    1 MRLAIELARKALAEGEVPFGAVIVDDdGKVIARGHNRVEQDGDPTAHAEIVAIRNAARRLGSYLLSGCTLYTTLEPCPMC 80

                         90       100
                 ....*....|....*....|
gi 516050917  87 MAGMRIAGIKSVSYAYSNED 106
Cdd:cd01285   81 AGALLWARIKRVVYGASDPK 100
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-121 1.96e-25

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: 94.51  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917    5 EQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPCP 84
Cdd:pfam14437   4 EKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKELNADTTAHAEILAIQQAAKKLGSWRLDDATLYVTLEPCP 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 516050917   85 MCMAGMRIAGIKSVSYAYSNEDGTPFGLSTAEIYIEL 121
Cdd:pfam14437  84 MCAGAIVQAGLKSLVYGAGNPKGGAVGSVLNKLVIVL 120
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
5-101 6.22e-25

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 91.98  E-value: 6.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917    5 EQFLRKAIELAYNNIEKGGRPFGAVVVK-NGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPC 83
Cdd:pfam00383   3 EYFMRLALKAAKRAYPYSNFPVGAVIVKkDGEIIATGYNGENAGYDPTIHAERNAIRQAGKRGEGVRLEGATLYVTLEPC 82

                          90
                  ....*....|....*...
gi 516050917   84 PMCMAGMRIAGIKSVSYA 101
Cdd:pfam00383  83 GMCAQAIIESGIKRVVFG 100
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 5-105 1.82e-18

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 77.54  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   5 EQFLRKAIELAYNNIEKGGRPFGAVVVKNGEIIASGVNQILVTNDPTAHAELLAIRAASQVLGTANLEGCSVYASGHPCP 84
Cdd:PRK10860  14 EYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVLQNYRLLDATLYVTLEPCV 93

                         90       100
                 ....*....|....*....|.
gi 516050917  85 MCMAGMRIAGIKSVSYAYSNE 105
Cdd:PRK10860  94 MCAGAMVHSRIGRLVFGARDA 114
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 24-111 3.14e-09

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: 52.28  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917  24 RPFGAVVVKNGEIIASGVNQIL--VTNDP-------------------TAHAELLAIRAASQVlgTANLEGCSVYASGHP 82
Cdd:cd01286   20 RQVGAVIVKDKRIISTGYNGSPsgLPHCAevgcerddlpsgedqkccrTVHAEQNAILQAARH--GVSLEGATLYVTLFP 97

                         90       100       110
                 ....*....|....*....|....*....|
gi 516050917  83 CPMCmAGMRI-AGIKSVSYAYSNEDGTPFG 111
Cdd:cd01286   98 CIEC-AKLIIqAGIKKVVYAEPYDDDDPAA 126
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 8-101 9.14e-09

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: 50.70  E-value: 9.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   8 LRKAIELAynniEKG-GR-----PFGAVVVK-NGEIIASGVNQilvtNDPTAHAELLAIRAASQVL---GTA--NLEGCS 75
Cdd:cd01284    1 MRRALELA----EKGrGLtspnpPVGCVIVDdDGEIVGEGYHR----KAGGPHAEVNALASAGEKLargATLyvTLEPCS 72

                         90       100
                 ....*....|....*....|....*.
gi 516050917  76 VYASGHPCPMCMAgmrIAGIKSVSYA 101
Cdd:cd01284   73 HHGKTPPCVDAII---EAGIKRVVVG 95
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 25-101 3.93e-07

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 48.29  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   25 PFGAVVVKNGEIIASGVNQilvtNDPTAHAELLAIRAASqvlgtANLEGCSVYASGHPC------PMCMAGMRIAGIKSV 98
Cdd:TIGR00326  20 LVGCVIVKNGEIVGEGAHQ----KAGEPHAEVHALRQAG-----ENAKGATAYVTLEPCshqgrtPPCAEAIIEAGIKKV 90


                  ...
gi 516050917   99 SYA 101
Cdd:TIGR00326  91 VVS 93
cd PHA02588
deoxycytidylate deaminase; Provisional
 27-101 2.67e-05

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 42.05  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917  27 GAVVVKNGEIIASGVN--------------QILVTNDPTA------------------HAELLAIRAASQvlGTANLEGC 74
Cdd:PHA02588  25 GAVIEKNGRIISTGYNgtpaggvnccdhanEQGWLDDEGKlkkehrpehsawsskneiHAELNAILFAAR--NGISIEGA 102

                         90       100
                 ....*....|....*....|....*..
gi 516050917  75 SVYASGHPCPMCMAGMRIAGIKSVSYA 101
Cdd:PHA02588 103 TMYVTASPCPDCAKAIAQSGIKKLVYC 129
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 22-98 4.34e-05

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: 40.23  E-value: 4.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516050917  22 GGRPFGAVVVKN--GEIIASGVNQILVTNDPTAHAELLAIRAASQvlgTANLEGCSVYASGHPCPMCMAGMRIAGIKSV 98
Cdd:cd00786   16 SNFQVGACLVNKkdGGKVGRGCNIENAAYSMCNHAERTALFNAGS---EGDTKGQMLYVALSPCGACAQLIIELGIKDV 91
PLN02807 PLN02807
diaminohydroxyphosphoribosylaminopyrimidine deaminase
 6-98 5.48e-04

diaminohydroxyphosphoribosylaminopyrimidine deaminase


Pssm-ID: 215433 [Multi-domain]  Cd Length: 380  Bit Score: 38.99  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516050917   6 QFLRKAIELAYNNIEKGG-RPF-GAVVVKNGEIIASGVNqilvtndPTA---HAELLAIRAASQVlgtanLEGCSVYASG 80
Cdd:PLN02807  34 FYMRRCVELARKAIGCTSpNPMvGCVIVKDGRIVGEGFH-------PKAgqpHAEVFALRDAGDL-----AENATAYVSL 101

                         90       100
                 ....*....|....*....|....
gi 516050917  81 HPC------PMCMAGMRIAGIKSV 98
Cdd:PLN02807 102 EPCnhygrtPPCTEALIKAKVKRV 125
 
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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