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Conserved domains on  [gi|15236238|ref|NP_192213|]
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uncharacterized protein AT4G03040 [Arabidopsis thaliana]

Protein Classification

ribonuclease H family protein( domain architecture ID 54171)

ribonuclease H (RNase H) family protein may function as an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNase_H_like super family cl14782
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
36-92 1.54e-05

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


The actual alignment was detected with superfamily member cd06222:

Pssm-ID: 449355 [Multi-domain]  Cd Length: 121  Bit Score: 39.99  E-value: 1.54e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15236238  36 QDSKAGICLILTDSHGKyILKGCSSIEPTNSALEAEAIALKEALLQVKCLQYQDVIL 92
Cdd:cd06222  10 NPGPAGIGGVLRDHEGG-WLGGFALKIGAPTALEAELLALLLALELALDLGYLKVII 65
 
Name Accession Description Interval E-value
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
36-92 1.54e-05

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


Pssm-ID: 259998 [Multi-domain]  Cd Length: 121  Bit Score: 39.99  E-value: 1.54e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15236238  36 QDSKAGICLILTDSHGKyILKGCSSIEPTNSALEAEAIALKEALLQVKCLQYQDVIL 92
Cdd:cd06222  10 NPGPAGIGGVLRDHEGG-WLGGFALKIGAPTALEAELLALLLALELALDLGYLKVII 65
RVT_3 pfam13456
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ...
27-79 3.61e-05

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.


Pssm-ID: 433223 [Multi-domain]  Cd Length: 123  Bit Score: 39.17  E-value: 3.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15236238    27 YDTTLSPLKQDSKAGIclILTDSHGKYILKGCSSIEPTNSALEAEAIALKEAL 79
Cdd:pfam13456   2 FDGAFKCDSGLAGAGV--VIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGL 52
PRK08719 PRK08719
ribonuclease H; Reviewed
21-91 1.56e-03

ribonuclease H; Reviewed


Pssm-ID: 236334 [Multi-domain]  Cd Length: 147  Bit Score: 35.22  E-value: 1.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236238   21 RHYKEVYDTTLSPLKQDS--KAGICLILTDSHGKYILKGCSSIEPTNSALEAEAIALkeallqVKCLQYQ---DVI 91
Cdd:PRK08719   2 RASYSIYIDGAAPNNQHGcvRGGIGLVVYDEAGEIVDEQSITVNRYTDNAELELLAL------IEALEYArdgDVI 71
 
Name Accession Description Interval E-value
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
36-92 1.54e-05

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


Pssm-ID: 259998 [Multi-domain]  Cd Length: 121  Bit Score: 39.99  E-value: 1.54e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15236238  36 QDSKAGICLILTDSHGKyILKGCSSIEPTNSALEAEAIALKEALLQVKCLQYQDVIL 92
Cdd:cd06222  10 NPGPAGIGGVLRDHEGG-WLGGFALKIGAPTALEAELLALLLALELALDLGYLKVII 65
RVT_3 pfam13456
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ...
27-79 3.61e-05

Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.


Pssm-ID: 433223 [Multi-domain]  Cd Length: 123  Bit Score: 39.17  E-value: 3.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15236238    27 YDTTLSPLKQDSKAGIclILTDSHGKYILKGCSSIEPTNSALEAEAIALKEAL 79
Cdd:pfam13456   2 FDGAFKCDSGLAGAGV--VIRDPNGNVLLAGQKKLGPGASVLEAEAQALIIGL 52
PRK08719 PRK08719
ribonuclease H; Reviewed
21-91 1.56e-03

ribonuclease H; Reviewed


Pssm-ID: 236334 [Multi-domain]  Cd Length: 147  Bit Score: 35.22  E-value: 1.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236238   21 RHYKEVYDTTLSPLKQDS--KAGICLILTDSHGKYILKGCSSIEPTNSALEAEAIALkeallqVKCLQYQ---DVI 91
Cdd:PRK08719   2 RASYSIYIDGAAPNNQHGcvRGGIGLVVYDEAGEIVDEQSITVNRYTDNAELELLAL------IEALEYArdgDVI 71
 
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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