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Conserved domains on  [gi|1277140764|gb|PIR42135|]
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MAG: deaminase [Candidatus Yanofskybacteria bacterium CG10_big_fil_rev_8_21_14_0_10_37_15]

Protein Classification

deoxycytidylate deaminase( domain architecture ID 10788416)

deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase

CATH:  3.40.140.10
EC:  3.5.4.12
Gene Ontology:  GO:0004132|GO:0008270|GO:0009972|GO:0006220
PubMed:  2247612
SCOP:  4000564

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-143 4.64e-71

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 210.08  E-value: 4.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   1 MRPKWDEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEI--------VDGHCVRTVHAEA 72
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLReklgipsgERGECCRTVHAEQ 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277140764  73 NAVIQAARNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGRYGLSksvlvLAKKSGVKIREFK 143
Cdd:COG2131    84 NAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKE-----LLKEAGVEVRQLE 149
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-143 4.64e-71

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 210.08  E-value: 4.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   1 MRPKWDEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEI--------VDGHCVRTVHAEA 72
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLReklgipsgERGECCRTVHAEQ 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277140764  73 NAVIQAARNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGRYGLSksvlvLAKKSGVKIREFK 143
Cdd:COG2131    84 NAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKE-----LLKEAGVEVRQLE 149
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 6-118 3.16e-55

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: 169.38  E-value: 3.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   6 DEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEI------VDGHCVRTVHAEANAVIQAA 79
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERddlpsgEDQKCCRTVHAEQNAILQAA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1277140764  80 RNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFY 118
Cdd:cd01286    81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPY 119
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 2-141 5.18e-43

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 138.84  E-value: 5.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   2 RPKWDEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEIVDGHCVRTVHAEANAVIQAARN 81
Cdd:TIGR02571   2 RIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAKF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277140764  82 GVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGR-YGLSksvlvLAKKSGVKIRE 141
Cdd:TIGR02571  82 GVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHpYAIE-----LFEQAGVELKK 137
cd PHA02588
deoxycytidylate deaminase; Provisional
 9-143 1.05e-29

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 105.61  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   9 FIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEIV-------------DGHC----VRTVHAE 71
Cdd:PHA02588    6 YLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGwlddegklkkehrPEHSawssKNEIHAE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277140764  72 ANAVIQAARNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGRYGLSKSVLvlaKKSGVKIREFK 143
Cdd:PHA02588   86 LNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGPGWDDIL---RKSGIEVIQIP 154
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
5-114 3.52e-24

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 89.28  E-value: 3.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   5 WDEYFIKIAEIVALRS-TCDRAHVGAVI-TKNKVILSTGYNGSSRGLPhcddigheivdghcvRTVHAEANAVIQAARNG 82
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIvKKDGEIIATGYNGENAGYD---------------PTIHAERNAIRQAGKRG 65

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277140764  83 VAID--GSILYLTISPCYDCFKMIVNAGIREVVY 114
Cdd:pfam00383  66 EGVRleGATLYVTLEPCGMCAQAIIESGIKRVVF 99
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
1-143 4.64e-71

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 210.08  E-value: 4.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   1 MRPKWDEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEI--------VDGHCVRTVHAEA 72
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLReklgipsgERGECCRTVHAEQ 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277140764  73 NAVIQAARNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGRYGLSksvlvLAKKSGVKIREFK 143
Cdd:COG2131    84 NAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKE-----LLKEAGVEVRQLE 149
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 6-118 3.16e-55

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: 169.38  E-value: 3.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   6 DEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEI------VDGHCVRTVHAEANAVIQAA 79
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERddlpsgEDQKCCRTVHAEQNAILQAA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1277140764  80 RNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFY 118
Cdd:cd01286    81 RHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPY 119
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 2-141 5.18e-43

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 138.84  E-value: 5.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   2 RPKWDEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEIVDGHCVRTVHAEANAVIQAARN 81
Cdd:TIGR02571   2 RIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCYVVDGHCVRTIHAEMNALLQCAKF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277140764  82 GVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGR-YGLSksvlvLAKKSGVKIRE 141
Cdd:TIGR02571  82 GVSTEGAEIYVTHFPCLQCTKSIIQAGIKKIYYAQDYHNHpYAIE-----LFEQAGVELKK 137
cd PHA02588
deoxycytidylate deaminase; Provisional
 9-143 1.05e-29

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 105.61  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   9 FIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSRGLPHCDDIGHEIV-------------DGHC----VRTVHAE 71
Cdd:PHA02588    6 YLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCDHANEQGwlddegklkkehrPEHSawssKNEIHAE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277140764  72 ANAVIQAARNGVAIDGSILYLTISPCYDCFKMIVNAGIREVVYKQFYSGRYGLSKSVLvlaKKSGVKIREFK 143
Cdd:PHA02588   86 LNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGPGWDDIL---RKSGIEVIQIP 154
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
5-114 3.52e-24

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 89.28  E-value: 3.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   5 WDEYFIKIAEIVALRS-TCDRAHVGAVI-TKNKVILSTGYNGSSRGLPhcddigheivdghcvRTVHAEANAVIQAARNG 82
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIvKKDGEIIATGYNGENAGYD---------------PTIHAERNAIRQAGKRG 65

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1277140764  83 VAID--GSILYLTISPCYDCFKMIVNAGIREVVY 114
Cdd:pfam00383  66 EGVRleGATLYVTLEPCGMCAQAIIESGIKRVVF 99
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 5-136 9.04e-14

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: 64.08  E-value: 9.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   5 WDEYFIKIAEIVALRSTCDRAHVGAVITKNKVILSTGYNGSSrglphcddigheivdGHCVRTVHAEANAVIQAARNGVA 84
Cdd:pfam14437   3 HEKWFRKALGLAEKAYDAGEVPIGAVIVKDGKVIARGYNRKE---------------LNADTTAHAEILAIQQAAKKLGS 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277140764  85 I--DGSILYLTISPCYDCFKMIVNAGIREVVYKQFY--SGRYGLSKSVLVLAKKSG 136
Cdd:pfam14437  68 WrlDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGNpkGGAVGSVLNKLVIVLWNH 123
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 27-114 3.44e-10

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: 54.35  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764  27 VGAVITKNKVILSTGYNgssRGLPHCDdigheivdghcvRTVHAEANAVIQAAR--NGVAIDGSILYLTISPCYDCFKMI 104
Cdd:COG0590    26 VGAVLVKDGEIIARGHN---RVETLND------------PTAHAEILAIRAAARklGNWRLSGCTLYVTLEPCPMCAGAI 90

                          90
                  ....*....|
gi 1277140764 105 VNAGIREVVY 114
Cdd:COG0590    91 VWARIGRVVY 100
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 27-114 2.66e-08

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: 50.83  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764  27 VGAVITKNKVILSTGYngssrglphcddigHEIVDGHcvrtvHAEANAVIQAarnGVAIDGSILYLTISPC--YD----C 100
Cdd:COG0117    24 VGCVIVKDGRIVGEGY--------------HQRAGGP-----HAEVNALAQA---GEAARGATLYVTLEPCshHGrtppC 81

                          90
                  ....*....|....
gi 1277140764 101 FKMIVNAGIREVVY 114
Cdd:COG0117    82 ADALIEAGIKRVVI 95
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 26-114 3.54e-08

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: 48.38  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764  26 HVGAVITKNK-VILSTGYNgssRGLPHCDdigheivdghcvRTVHAEANAVIQAARNGVAID--GSILYLTISPCYDCFK 102
Cdd:cd01285    18 PFGAVIVDDDgKVIARGHN---RVEQDGD------------PTAHAEIVAIRNAARRLGSYLlsGCTLYTTLEPCPMCAG 82

                          90
                  ....*....|..
gi 1277140764 103 MIVNAGIREVVY 114
Cdd:cd01285    83 ALLWARIKRVVY 94
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 27-114 3.81e-07

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: 45.69  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764  27 VGAVITK-NKVILSTGYngsSRGLPhcddigheivdghcvrTVHAEANAVIQAARNGVAidGSILYLTISPCYD------ 99
Cdd:cd01284    21 VGCVIVDdDGEIVGEGY---HRKAG----------------GPHAEVNALASAGEKLAR--GATLYVTLEPCSHhgktpp 79

                          90
                  ....*....|....*
gi 1277140764 100 CFKMIVNAGIREVVY 114
Cdd:cd01284    80 CVDAIIEAGIKRVVV 94
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 27-114 2.14e-06

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: 45.59  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764  27 VGAVITKNKVILSTGYNGSSrGLPHcddigheivdghcvrtvhAEANAVIQAARNgvaIDGSILYLTISPCYD------C 100
Cdd:TIGR00326  21 VGCVIVKNGEIVGEGAHQKA-GEPH------------------AEVHALRQAGEN---AKGATAYVTLEPCSHqgrtppC 78

                          90
                  ....*....|....
gi 1277140764 101 FKMIVNAGIREVVY 114
Cdd:TIGR00326  79 AEAIIEAGIKKVVV 92
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 6-114 4.32e-05

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 41.33  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140764   6 DEYFIKIAEIVALRSTCDR-AHVGAVITKNKVILSTGYNgssRGLPHCDDigheivdghcvrTVHAEANAVIQ---AARN 81
Cdd:PRK10860   13 HEYWMRHALTLAKRAWDEReVPVGAVLVHNNRVIGEGWN---RPIGRHDP------------TAHAEIMALRQgglVLQN 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1277140764  82 GVAIDGSiLYLTISPCYDCFKMIVNAGIREVVY 114
Cdd:PRK10860   78 YRLLDAT-LYVTLEPCVMCAGAMVHSRIGRLVF 109
 
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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