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Conserved domains on  [gi|2103687831|ref|XP_043862801|]
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uncharacterized protein LOC122756649 [Drosophila santomea]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 10173339)

endonuclease/exonuclease/phosphatase (EEP) family protein is among a diverse set of enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins; similar to Bombyx mori non-LTR retrotransposon R1Bmks ORF2 protein

CATH:  3.60.10.10
PubMed:  10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 11-173 1.04e-49

Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons; This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


:

Pssm-ID: 197311 [Multi-domain]  Cd Length: 205  Bit Score: 165.93  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  11 MKIVQINLNHCEAAHHLLSQAMREVQADVALISEPYKKTSGAD-YILDGTRCAAILINGT-------------------- 69
Cdd:cd09077     1 LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVNNPnWVTDESGRAAIVVSDRlprkpiqrlslglgivaarv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  70 ------------RRPVPEFSAVIDELANDARGE-RNVVIAGDFNAWAEEWGSVHTNARGRTLQEAFASMDVALLNTGTEH 136
Cdd:cd09077    81 ggitvvscyappSESLEEFEEYLENLVRIVRGLsRPVIIGGDFNAWSPAWGSKRTDRRGRLLEDWIANLGLVLLNDGNSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2103687831 137 TFSRAGAGSVVDLTFCSGSLFQRAQL-SVSNVYTASDH 173
Cdd:cd09077   161 TFVRPRGTSIIDVTFCSPSLARRISNwRVLEDETLSDH 198
 
Name Accession Description Interval E-value
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 11-173 1.04e-49

Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons; This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197311 [Multi-domain]  Cd Length: 205  Bit Score: 165.93  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  11 MKIVQINLNHCEAAHHLLSQAMREVQADVALISEPYKKTSGAD-YILDGTRCAAILINGT-------------------- 69
Cdd:cd09077     1 LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVNNPnWVTDESGRAAIVVSDRlprkpiqrlslglgivaarv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  70 ------------RRPVPEFSAVIDELANDARGE-RNVVIAGDFNAWAEEWGSVHTNARGRTLQEAFASMDVALLNTGTEH 136
Cdd:cd09077    81 ggitvvscyappSESLEEFEEYLENLVRIVRGLsRPVIIGGDFNAWSPAWGSKRTDRRGRLLEDWIANLGLVLLNDGNSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2103687831 137 TFSRAGAGSVVDLTFCSGSLFQRAQL-SVSNVYTASDH 173
Cdd:cd09077   161 TFVRPRGTSIIDVTFCSPSLARRISNwRVLEDETLSDH 198
Exo_endo_phos_2 pfam14529
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of ...
 70-173 3.58e-15

Endonuclease-reverse transcriptase; This domain represents the endonuclease region of retrotransposons from a range of bacteria, archaea and eukaryotes. These are enzymes largely from class EC:2.7.7.49.


Pssm-ID: 434019 [Multi-domain]  Cd Length: 118  Bit Score: 71.24  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  70 RRPVPEFSAVIDELAN--DARGERNVVIAGDFNAWAEEWGSVHTN-ARGRTLQEAFASMDVALLNT-GTEHTFSRAGAGS 145
Cdd:pfam14529   8 CPPSDQLRNLLDTLEDilRSLDRPPIIIGGDFNAHHPLWGSNSTDvSRGEELIEFLNEHGLNLLNLpKSGPTFISSNGDS 87

                          90       100
                  ....*....|....*....|....*...
gi 2103687831 146 VVDLTFCSGSLFQRAqLSVSNVYTASDH 173
Cdd:pfam14529  88 TIDLTLTSDPLAVRV-LSDLGPDSGSDH 114
 
Name Accession Description Interval E-value
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 11-173 1.04e-49

Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons; This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197311 [Multi-domain]  Cd Length: 205  Bit Score: 165.93  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  11 MKIVQINLNHCEAAHHLLSQAMREVQADVALISEPYKKTSGAD-YILDGTRCAAILINGT-------------------- 69
Cdd:cd09077     1 LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVNNPnWVTDESGRAAIVVSDRlprkpiqrlslglgivaarv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  70 ------------RRPVPEFSAVIDELANDARGE-RNVVIAGDFNAWAEEWGSVHTNARGRTLQEAFASMDVALLNTGTEH 136
Cdd:cd09077    81 ggitvvscyappSESLEEFEEYLENLVRIVRGLsRPVIIGGDFNAWSPAWGSKRTDRRGRLLEDWIANLGLVLLNDGNSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2103687831 137 TFSRAGAGSVVDLTFCSGSLFQRAQL-SVSNVYTASDH 173
Cdd:cd09077   161 TFVRPRGTSIIDVTFCSPSLARRISNwRVLEDETLSDH 198
Exo_endo_phos_2 pfam14529
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of ...
 70-173 3.58e-15

Endonuclease-reverse transcriptase; This domain represents the endonuclease region of retrotransposons from a range of bacteria, archaea and eukaryotes. These are enzymes largely from class EC:2.7.7.49.


Pssm-ID: 434019 [Multi-domain]  Cd Length: 118  Bit Score: 71.24  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  70 RRPVPEFSAVIDELAN--DARGERNVVIAGDFNAWAEEWGSVHTN-ARGRTLQEAFASMDVALLNT-GTEHTFSRAGAGS 145
Cdd:pfam14529   8 CPPSDQLRNLLDTLEDilRSLDRPPIIIGGDFNAHHPLWGSNSTDvSRGEELIEFLNEHGLNLLNLpKSGPTFISSNGDS 87

                          90       100
                  ....*....|....*....|....*...
gi 2103687831 146 VVDLTFCSGSLFQRAqLSVSNVYTASDH 173
Cdd:pfam14529  88 TIDLTLTSDPLAVRV-LSDLGPDSGSDH 114
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 77-173 6.43e-03

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 37.97  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103687831  77 SAVIDELANDARGERNVVIAGDFNAWAEEwgSVHTNARGRTLQEAFASMD-VALLNTGTEHTFSRAGAGSVVDLTFCSGS 155
Cdd:cd09083   147 AKLILERIKEIAGDLPVILTGDFNAEPDS--EPYKTLTSGGLKDARDTAAtTDGGPEGTFHGFKGPPGGSRIDYIFVSPG 224

                          90       100
                  ....*....|....*....|..
gi 2103687831 156 L-FQRAQL---SVSNVYtASDH 173
Cdd:cd09083   225 VkVLSYEIltdRYDGRY-PSDH 245
 
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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