NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1352907378|ref|WP_104851964|]
View 

MULTISPECIES: uracil-DNA glycosylase family protein [Acinetobacter]

Protein Classification

Mug family protein( domain architecture ID 10790314)

Mug family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
11-186 1.13e-40

G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];


:

Pssm-ID: 442880  Cd Length: 157  Bit Score: 135.29  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  11 LEPFLPANAKLLMLGSFPPPKSrWKMDFYYPNYQNDMWRILGLCFFQDKNyfLDLEAKnfhlhkiIDFLNTTGIAISDTA 90
Cdd:COG3663     1 LPPVLAPGLRVLILGSNPGLAS-LAAGFYYAHPRNRFWPILGAAGGTDPR--LDYPER-------KAFLLEHGIGLWDVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  91 QQVIRLKGnASDKFLQIEKPMDIAALLSKIPLCQSIMTTGDKATDTLmlsmpESAEKPQIGQAthcyfakRELHLYRMPS 170
Cdd:COG3663    71 ARCTRRAG-SLDSAIRNAGPNDLAALLRYRPRIKTVAFNGKTAYRLF-----FKLVAPQPETI-------GGIELWVLPS 137
                         170
                  ....*....|....*..
gi 1352907378 171 SSRAYP-LALEKKAEAY 186
Cdd:COG3663   138 PSPANArFSLEEKLAAW 154
 
Name Accession Description Interval E-value
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
11-186 1.13e-40

G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 442880  Cd Length: 157  Bit Score: 135.29  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  11 LEPFLPANAKLLMLGSFPPPKSrWKMDFYYPNYQNDMWRILGLCFFQDKNyfLDLEAKnfhlhkiIDFLNTTGIAISDTA 90
Cdd:COG3663     1 LPPVLAPGLRVLILGSNPGLAS-LAAGFYYAHPRNRFWPILGAAGGTDPR--LDYPER-------KAFLLEHGIGLWDVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  91 QQVIRLKGnASDKFLQIEKPMDIAALLSKIPLCQSIMTTGDKATDTLmlsmpESAEKPQIGQAthcyfakRELHLYRMPS 170
Cdd:COG3663    71 ARCTRRAG-SLDSAIRNAGPNDLAALLRYRPRIKTVAFNGKTAYRLF-----FKLVAPQPETI-------GGIELWVLPS 137
                         170
                  ....*....|....*..
gi 1352907378 171 SSRAYP-LALEKKAEAY 186
Cdd:COG3663   138 PSPANArFSLEEKLAAW 154
UDG-F6_HDG cd10032
Uracil DNA glycosylase family 6, includes hypoxanthine-DNA glycosylase and similar proteins; ...
9-176 6.22e-38

Uracil DNA glycosylase family 6, includes hypoxanthine-DNA glycosylase and similar proteins; Uracil DNA glycosylase family 6 hypoxanthine-DNA glycosylase (HDG) lacks any detectable UDG activity; it excises hypoxanthine, a deamination product of adenine, from double-stranded DNA. Uracil-DNA glycosylase (UDGs) initiates repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.


Pssm-ID: 381682  Cd Length: 141  Bit Score: 127.70  E-value: 6.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378   9 HPLEPFLPANAKLLMLGSFPPPKSRWKMdFYYPNYQNDMWRILGLCFFQDKNYFlDLEAKnfhlhkiIDFLNTTGIAISD 88
Cdd:cd10032     1 HGFPPVVDENSRVLILGSFPSVKSLEAQ-FYYGHPRNRFWRILGALFGEDLKAL-DYEER-------KAFLLEHGIALWD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  89 TAQQVIRlkGNASDKFLQIEKPMDIAALLSKIPLCQSIMTTGDKATdtlmlsmpESAEKPqigqathcYFAKRELHLYRM 168
Cdd:cd10032    72 VLASCRR--KGSLDSAIRNVEPNDIAGLLAKAPNIKAIIFNGKKAA--------RLFKKY--------VAPLRGIETLRL 133

                  ....*...
gi 1352907378 169 PSSSRAYP 176
Cdd:cd10032   134 PSTSPANA 141
 
Name Accession Description Interval E-value
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
11-186 1.13e-40

G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 442880  Cd Length: 157  Bit Score: 135.29  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  11 LEPFLPANAKLLMLGSFPPPKSrWKMDFYYPNYQNDMWRILGLCFFQDKNyfLDLEAKnfhlhkiIDFLNTTGIAISDTA 90
Cdd:COG3663     1 LPPVLAPGLRVLILGSNPGLAS-LAAGFYYAHPRNRFWPILGAAGGTDPR--LDYPER-------KAFLLEHGIGLWDVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  91 QQVIRLKGnASDKFLQIEKPMDIAALLSKIPLCQSIMTTGDKATDTLmlsmpESAEKPQIGQAthcyfakRELHLYRMPS 170
Cdd:COG3663    71 ARCTRRAG-SLDSAIRNAGPNDLAALLRYRPRIKTVAFNGKTAYRLF-----FKLVAPQPETI-------GGIELWVLPS 137
                         170
                  ....*....|....*..
gi 1352907378 171 SSRAYP-LALEKKAEAY 186
Cdd:COG3663   138 PSPANArFSLEEKLAAW 154
UDG-F6_HDG cd10032
Uracil DNA glycosylase family 6, includes hypoxanthine-DNA glycosylase and similar proteins; ...
9-176 6.22e-38

Uracil DNA glycosylase family 6, includes hypoxanthine-DNA glycosylase and similar proteins; Uracil DNA glycosylase family 6 hypoxanthine-DNA glycosylase (HDG) lacks any detectable UDG activity; it excises hypoxanthine, a deamination product of adenine, from double-stranded DNA. Uracil-DNA glycosylase (UDGs) initiates repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.


Pssm-ID: 381682  Cd Length: 141  Bit Score: 127.70  E-value: 6.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378   9 HPLEPFLPANAKLLMLGSFPPPKSRWKMdFYYPNYQNDMWRILGLCFFQDKNYFlDLEAKnfhlhkiIDFLNTTGIAISD 88
Cdd:cd10032     1 HGFPPVVDENSRVLILGSFPSVKSLEAQ-FYYGHPRNRFWRILGALFGEDLKAL-DYEER-------KAFLLEHGIALWD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352907378  89 TAQQVIRlkGNASDKFLQIEKPMDIAALLSKIPLCQSIMTTGDKATdtlmlsmpESAEKPqigqathcYFAKRELHLYRM 168
Cdd:cd10032    72 VLASCRR--KGSLDSAIRNVEPNDIAGLLAKAPNIKAIIFNGKKAA--------RLFKKY--------VAPLRGIETLRL 133

                  ....*...
gi 1352907378 169 PSSSRAYP 176
Cdd:cd10032   134 PSTSPANA 141
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH