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Conserved domains on  [gi|343398698|gb|EGV11227|]
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hypothetical protein HMPREF9127_0010 [Parvimonas sp. oral taxon 393 str. F0440]

Protein Classification

macro domain-containing protein( domain architecture ID 1211)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling

CATH:  3.40.220.10
Gene Ontology:  GO:0072570
PubMed:  26844395|15902274
SCOP:  4000521

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
3-86 8.39e-11

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


The actual alignment was detected with superfamily member PRK04143:

Pssm-ID: 469581  Cd Length: 264  Bit Score: 56.14  E-value: 8.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398698   3 RNKEQMLDFLVKAFIADSDNYKNMEIPEDETQKKVVLRSLMNIRIPRKMDDKVLEVQDEYLKLCAEEKRIVEIKDIPVVK 82
Cdd:PRK04143   2 PSQKARLEYLINYLQKEQLTSDVLPLPNDLEEQQDLLRALANVRPALPLSDEYLNLQDAYLQDENAERGVVDLKDLQPIK 81

                 ....*.
gi 343398698  83 D--IFL 86
Cdd:PRK04143  82 YdnIFL 87
 
Name Accession Description Interval E-value
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
3-86 8.39e-11

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 56.14  E-value: 8.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398698   3 RNKEQMLDFLVKAFIADSDNYKNMEIPEDETQKKVVLRSLMNIRIPRKMDDKVLEVQDEYLKLCAEEKRIVEIKDIPVVK 82
Cdd:PRK04143   2 PSQKARLEYLINYLQKEQLTSDVLPLPNDLEEQQDLLRALANVRPALPLSDEYLNLQDAYLQDENAERGVVDLKDLQPIK 81

                 ....*.
gi 343398698  83 D--IFL 86
Cdd:PRK04143  82 YdnIFL 87
 
Name Accession Description Interval E-value
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
3-86 8.39e-11

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 56.14  E-value: 8.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398698   3 RNKEQMLDFLVKAFIADSDNYKNMEIPEDETQKKVVLRSLMNIRIPRKMDDKVLEVQDEYLKLCAEEKRIVEIKDIPVVK 82
Cdd:PRK04143   2 PSQKARLEYLINYLQKEQLTSDVLPLPNDLEEQQDLLRALANVRPALPLSDEYLNLQDAYLQDENAERGVVDLKDLQPIK 81

                 ....*.
gi 343398698  83 D--IFL 86
Cdd:PRK04143  82 YdnIFL 87
 
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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