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Conserved domains on  [gi|1912013734|ref|XP_036218807|]
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uncharacterized protein LOC118680905 [Bactrocera oleae]

Protein Classification

exonuclease/endonuclease/phosphatase family protein( domain architecture ID 662)

exonuclease/endonuclease/phosphatase (EEP) family protein may cleave phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 14-218 1.52e-35

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or 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.


The actual alignment was detected with superfamily member cd09077:

Pssm-ID: 469791 [Multi-domain]  Cd Length: 205  Bit Score: 124.71  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  14 MRILQINLQHSTAASADLVLRLGRDEADVVLIQEPWLSRNGisglrtkshkLLAANSTGRTRACLLIRNELTVFLLLNFR 93
Cdd:cd09077     1 LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVN----------NPNWVTDESGRAAIVVSDRLPRKPIQRLS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  94 N-EDVVAARLEDsaeeLWLVSAYMPHDDEVEPPPYLLRRVLAEARRKGTGVLIGLDANSRHTVWGSSDINARGESLFDFI 172
Cdd:cd09077    71 LgLGIVAARVGG----ITVVSCYAPPSESLEEFEEYLENLVRIVRGLSRPVIIGGDFNAWSPAWGSKRTDRRGRLLEDWI 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1912013734 173 CSVDLSICNRGNSPTFVTASRFTIYMLLYATSSTIKRIKsqddGWR 218
Cdd:cd09077   147 ANLGLVLLNDGNSPTFVRPRGTSIIDVTFCSPSLARRIS----NWR 188
 
Name Accession Description Interval E-value
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 14-218 1.52e-35

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: 124.71  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  14 MRILQINLQHSTAASADLVLRLGRDEADVVLIQEPWLSRNGisglrtkshkLLAANSTGRTRACLLIRNELTVFLLLNFR 93
Cdd:cd09077     1 LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVN----------NPNWVTDESGRAAIVVSDRLPRKPIQRLS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  94 N-EDVVAARLEDsaeeLWLVSAYMPHDDEVEPPPYLLRRVLAEARRKGTGVLIGLDANSRHTVWGSSDINARGESLFDFI 172
Cdd:cd09077    71 LgLGIVAARVGG----ITVVSCYAPPSESLEEFEEYLENLVRIVRGLSRPVIIGGDFNAWSPAWGSKRTDRRGRLLEDWI 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1912013734 173 CSVDLSICNRGNSPTFVTASRFTIYMLLYATSSTIKRIKsqddGWR 218
Cdd:cd09077   147 ANLGLVLLNDGNSPTFVRPRGTSIIDVTFCSPSLARRIS----NWR 188
Exo_endo_phos_2 pfam14529
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of ...
 111-196 1.58e-07

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: 48.51  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734 111 LVSAYMPHDDEVEPPPYLLRRVLAEARRkgTGVLIGLDANSRHTVWGSSDIN-ARGESLFDFICSVDLSICNRGNS-PTF 188
Cdd:pfam14529   3 IISVYCPPSDQLRNLLDTLEDILRSLDR--PPIIIGGDFNAHHPLWGSNSTDvSRGEELIEFLNEHGLNLLNLPKSgPTF 80


                  ....*...
gi 1912013734 189 VTASRFTI 196
Cdd:pfam14529  81 ISSNGDST 88
 
Name Accession Description Interval E-value
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 14-218 1.52e-35

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: 124.71  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  14 MRILQINLQHSTAASADLVLRLGRDEADVVLIQEPWLSRNGisglrtkshkLLAANSTGRTRACLLIRNELTVFLLLNFR 93
Cdd:cd09077     1 LRILQINLNRCKAAQDLLLQTAREEGADIALIQEPYLVPVN----------NPNWVTDESGRAAIVVSDRLPRKPIQRLS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  94 N-EDVVAARLEDsaeeLWLVSAYMPHDDEVEPPPYLLRRVLAEARRKGTGVLIGLDANSRHTVWGSSDINARGESLFDFI 172
Cdd:cd09077    71 LgLGIVAARVGG----ITVVSCYAPPSESLEEFEEYLENLVRIVRGLSRPVIIGGDFNAWSPAWGSKRTDRRGRLLEDWI 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1912013734 173 CSVDLSICNRGNSPTFVTASRFTIYMLLYATSSTIKRIKsqddGWR 218
Cdd:cd09077   147 ANLGLVLLNDGNSPTFVRPRGTSIIDVTFCSPSLARRIS----NWR 188
Exo_endo_phos_2 pfam14529
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of ...
 111-196 1.58e-07

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: 48.51  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734 111 LVSAYMPHDDEVEPPPYLLRRVLAEARRkgTGVLIGLDANSRHTVWGSSDIN-ARGESLFDFICSVDLSICNRGNS-PTF 188
Cdd:pfam14529   3 IISVYCPPSDQLRNLLDTLEDILRSLDR--PPIIIGGDFNAHHPLWGSNSTDvSRGEELIEFLNEHGLNLLNLPKSgPTF 80


                  ....*...
gi 1912013734 189 VTASRFTI 196
Cdd:pfam14529  81 ISSNGDST 88
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 17-178 6.65e-03

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 36.43  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  17 LQINLQHSTAASADLVLR-------LGRDEADVVLIQEPWLS-----RNGISGLRTKSHKLLAANSTGRTRACLLIRNEL 84
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKldalaalIRAYDPDVVALQETDDDdasrlLLALLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912013734  85 TVFLLLNFRNEDVVAARLEDSAEELWLVSAYMPHDDEVEPPPY--------LLRRVLAEARRKGTGVLIGLDANSRHtVW 156
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLardeqradLLLLLLALLAPRSEPVILAGDFNADY-IL 159

                         170       180
                  ....*....|....*....|..
gi 1912013734 157 GSSDINARGESLFDFICSVDLS 178
Cdd:pfam03372 160 VSGGLTVLSVGVLPDLGPRTGS 181
 
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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