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Conserved domains on  [gi|490813988|ref|WP_004676097|]
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MULTISPECIES: WGR domain-containing protein [Rhizobium]

Protein Classification

WGR domain-containing protein( domain architecture ID 10526938)

WGR domain-containing protein similar to Sinorhizobium fredii protein Y4dW

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 6-79 1.27e-35

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


:

Pssm-ID: 398851  Cd Length: 79  Bit Score: 116.19  E-value: 1.27e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490813988    6 YQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRE 74
 
Name Accession Description Interval E-value
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 6-79 1.27e-35

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 116.19  E-value: 1.27e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490813988    6 YQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRE 74
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 1-82 1.71e-34

Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.


Pssm-ID: 214814  Cd Length: 84  Bit Score: 113.54  E-value: 1.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490813988     1 MLTQPYQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRPN 80
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDDFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEER 80


                   ..
gi 490813988    81 TN 82
Cdd:smart00773  81 GK 82
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
6-79 2.21e-30

WGR domain, predicted DNA-binding domain in MolR [Transcription];


Pssm-ID: 443043  Cd Length: 83  Bit Score: 103.14  E-value: 2.21e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490813988   6 YQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:COG3831    1 MRLYLERIDPAGNSARFYELEVEPDLFGGWSLTRRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLRKGYRE 74
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 7-79 1.36e-28

WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, as well as in various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain appears to occur in single-domain proteins and in a variety of domain architectures, together with ATP-dependent DNA ligase domains, WD40 repeats, leucine-rich repeats, and other domains. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153425  Cd Length: 74  Bit Score: 98.06  E-value: 1.36e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490813988   7 QLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:cd07996    1 MTRLERIDPERNSARFYEIELEGDLFGEWSLVRRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREKLKRGYRE 73
 
Name Accession Description Interval E-value
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 6-79 1.27e-35

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 116.19  E-value: 1.27e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490813988    6 YQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRE 74
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 1-82 1.71e-34

Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.


Pssm-ID: 214814  Cd Length: 84  Bit Score: 113.54  E-value: 1.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490813988     1 MLTQPYQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRPN 80
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDDFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEER 80


                   ..
gi 490813988    81 TN 82
Cdd:smart00773  81 GK 82
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
6-79 2.21e-30

WGR domain, predicted DNA-binding domain in MolR [Transcription];


Pssm-ID: 443043  Cd Length: 83  Bit Score: 103.14  E-value: 2.21e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490813988   6 YQLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:COG3831    1 MRLYLERIDPAGNSARFYELEVEPDLFGGWSLTRRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLRKGYRE 74
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 7-79 1.36e-28

WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, as well as in various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain appears to occur in single-domain proteins and in a variety of domain architectures, together with ATP-dependent DNA ligase domains, WD40 repeats, leucine-rich repeats, and other domains. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153425  Cd Length: 74  Bit Score: 98.06  E-value: 1.36e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490813988   7 QLYIERRDATKNMARFYALAIEPTLFGTPCLTRRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:cd07996    1 MTRLERIDPERNSARFYEIELEGDLFGEWSLVRRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREKLKRGYRE 73
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 1-72 2.36e-05

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.


Pssm-ID: 153426  Cd Length: 102  Bit Score: 39.60  E-value: 2.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490813988   1 MLTQPyqlyierrDATKNMARFYALAI----EPTLFGTPCltrRWGRIGTIGQAMVHHFDREEDAVRMFLELLRSK 72
Cdd:cd07997   13 TLNQT--------DISNNNNKFYKIQIleskGPNTYALFT---RWGRVGERGQSQLTPFGSLESAIKEFEKKFKDK 77
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 39-79 4.26e-05

WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs) as well as the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, a small family of bacterial DNA ligases, and various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain occurs in single-domain proteins and in a variety of domain architectures, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153424  Cd Length: 73  Bit Score: 38.41  E-value: 4.26e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 490813988  39 RRWGRIGT-IGQAMVHHFDREEDAVRMFLELLRSKRARGYRP 79
Cdd:cd07994   32 RSYGRVGTvIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 36-88 1.67e-04

WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging.


Pssm-ID: 153428 [Multi-domain]  Cd Length: 104  Bit Score: 37.57  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490813988  36 CLTRRWGRIGT-IGQAMVHHFDREEDAVRMFLELLRSKRARGYRPNTNVGREPM 88
Cdd:cd08001   42 WVFRSWGRVGTtIGGNKLEEFSSLEEAKMAFEELYEEKTGNDFENRKNFKKKPG 95
 
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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