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Conserved domains on  [gi|1879378069|ref|WP_180980710|]
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endonuclease/exonuclease/phosphatase family protein [Sinorhizobium sp. M4_45]

Protein Classification

endonuclease/exonuclease/phosphatase family protein( domain architecture ID 10007571)

endonuclease/exonuclease/phosphatase (EEP) family protein similar to PGAP2-interacting protein, which is involved in lipid remodeling during glycosylphosphatidylinositol (GPI)-anchor maturation

CATH:  3.60.10.10
Gene Ontology:  GO:0003824
PubMed:  10838565

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
14-256 5.99e-44

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


:

Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 146.59  E-value: 5.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  14 PKAMRQRIRFLTYNVHSCFGTDRRLDPARIAAVIAECQPDVIALQEVdvgrartggidqahmiathlnmeaefhpalhle 93
Cdd:COG3568     1 AAAAAATLRVMTYNIRYGLGTDGRADLERIARVIRALDPDVVALQEN--------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  94 dekygdAVLTALPMRLIKAAPLPSSG-EPRGALWVEIDVAEVKLQVIVTHLGLRGAE-RLRQATALLgpGWLGGMAqGDA 171
Cdd:COG3568    48 ------AILSRYPIVSSGTFDLPDPGgEPRGALWADVDVPGKPLRVVNTHLDLRSAAaRRRQARALA--ELLAELP-AGA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 172 HVVLAGDLNAtgrstayrllarqlsdaqlltgakprptfpsrlpllrIDHVLIGKGIEVASCRVHGSTLARSASDHLPLL 251
Cdd:COG3568   119 PVILAGDFND-------------------------------------IDYILVSPGLRVLSAEVLDSPLGRAASDHLPVV 161

                  ....*
gi 1879378069 252 AELDV 256
Cdd:COG3568   162 ADLEL 166
 
Name Accession Description Interval E-value
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
14-256 5.99e-44

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 146.59  E-value: 5.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  14 PKAMRQRIRFLTYNVHSCFGTDRRLDPARIAAVIAECQPDVIALQEVdvgrartggidqahmiathlnmeaefhpalhle 93
Cdd:COG3568     1 AAAAAATLRVMTYNIRYGLGTDGRADLERIARVIRALDPDVVALQEN--------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  94 dekygdAVLTALPMRLIKAAPLPSSG-EPRGALWVEIDVAEVKLQVIVTHLGLRGAE-RLRQATALLgpGWLGGMAqGDA 171
Cdd:COG3568    48 ------AILSRYPIVSSGTFDLPDPGgEPRGALWADVDVPGKPLRVVNTHLDLRSAAaRRRQARALA--ELLAELP-AGA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 172 HVVLAGDLNAtgrstayrllarqlsdaqlltgakprptfpsrlpllrIDHVLIGKGIEVASCRVHGSTLARSASDHLPLL 251
Cdd:COG3568   119 PVILAGDFND-------------------------------------IDYILVSPGLRVLSAEVLDSPLGRAASDHLPVV 161

                  ....*
gi 1879378069 252 AELDV 256
Cdd:COG3568   162 ADLEL 166
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
24-254 3.13e-30

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; 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: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 113.16  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  24 LTYNVHScFGTDR-RLDPARIAAVIAECQPDVIALQEVdVGRARTGGIDQAHMIATHLNMEaeFHPALhlEDEKYGDAVL 102
Cdd:cd09084     2 MSYNVRS-FNRYKwKDDPDKILDFIKKQDPDILCLQEY-YGSEGDKDDDLRLLLKGYPYYY--VVYKS--DSGGTGLAIF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 103 TALPmrLIKAAPLPSSGEPRGALWVEIDVAEVKLQVIVTHL---------------GLRGAERLRQATALLGPGWLGGMA 167
Cdd:cd09084    76 SKYP--ILNSGSIDFPNTNNNAIFADIRVGGDTIRVYNVHLesfritpsdkelykeEKKAKELSRNLLRKLAEAFKRRAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 168 QGDA----------HVVLAGDLNATGRSTAYRLLARQLSDAQLLTGAKPRPTFPSRLPLLRIDHVLIGKGIEVASCRVHG 237
Cdd:cd09084   154 QADLlaadiaaspyPVIVCGDFNDTPASYVYRTLKKGLTDAFVEAGSGFGYTFNGLFFPLRIDYILTSKGFKVLRYRVDP 233
                         250
                  ....*....|....*..
gi 1879378069 238 STLarsaSDHLPLLAEL 254
Cdd:cd09084   234 GKY----SDHYPIVATL 246
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
24-247 7.14e-14

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: 68.02  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  24 LTYNVHSCFGTDRRLDP--ARIAAVIAECQPDVIALQEVDVgrartggiDQAHMIATHLNMEAEFHPALHLEDEK--YGD 99
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRklDALAALIRAYDPDVVALQETDD--------DDASRLLLALLAYGGFLSYGGPGGGGggGGV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 100 AVLTALPMRLIKAAPLPSSGEPRGALWVEIDV-AEVKLQVIVTHLGLRGAERLRQATALLGPGWLGGMAQGDAHVVLAGD 178
Cdd:pfam03372  73 AILSRYPLSSVILVDLGEFGDPALRGAIAPFAgVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879378069 179 LNAtgrstayrllarqlsdaqlltgakprptfpsrlpllriDHVLIGKGIEVASCRVHGSTLARSASDH 247
Cdd:pfam03372 153 FNA--------------------------------------DYILVSGGLTVLSVGVLPDLGPRTGSDH 183
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
51-256 3.40e-06

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 47.24  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  51 QPDVIALQEVDVgrarTGGIDQahmIATHLNMEAEFHPALHLEDEKYGdaVLTALPMRLIKAAPLPSSgEP-----RGAL 125
Cdd:PRK05421   69 DADLVLLQEAQT----TPELVQ---FATANYLAADQAPAFVLPQHPSG--VMTLSKAHPVYCCPLRER-EPwlrlpKSAL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 126 WVEIDVAEVK-LQVIVTH-----LGLRGAER-LRQATALL----GPgwlggmaqgdahVVLAGDLNA--TGRSTAYRLLA 192
Cdd:PRK05421  139 ITEYPLPNGRtLLVVNIHainfsLGVDVYSKqLEPIGDQIahhsGP------------VILAGDFNTwsRKRMNALKRFA 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879378069 193 RQLSDAQLLTGAKPRPTFPSRlPLlriDHVLIgKGIEVASCRVHGStlarSASDHLPLLAELDV 256
Cdd:PRK05421  207 RELGLKEVRFTDDQRRRAFGR-PL---DFVFY-RGLNVSKASVLVT----RASDHNPLLVEFSL 261
 
Name Accession Description Interval E-value
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
14-256 5.99e-44

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 146.59  E-value: 5.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  14 PKAMRQRIRFLTYNVHSCFGTDRRLDPARIAAVIAECQPDVIALQEVdvgrartggidqahmiathlnmeaefhpalhle 93
Cdd:COG3568     1 AAAAAATLRVMTYNIRYGLGTDGRADLERIARVIRALDPDVVALQEN--------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  94 dekygdAVLTALPMRLIKAAPLPSSG-EPRGALWVEIDVAEVKLQVIVTHLGLRGAE-RLRQATALLgpGWLGGMAqGDA 171
Cdd:COG3568    48 ------AILSRYPIVSSGTFDLPDPGgEPRGALWADVDVPGKPLRVVNTHLDLRSAAaRRRQARALA--ELLAELP-AGA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 172 HVVLAGDLNAtgrstayrllarqlsdaqlltgakprptfpsrlpllrIDHVLIGKGIEVASCRVHGSTLARSASDHLPLL 251
Cdd:COG3568   119 PVILAGDFND-------------------------------------IDYILVSPGLRVLSAEVLDSPLGRAASDHLPVV 161

                  ....*
gi 1879378069 252 AELDV 256
Cdd:COG3568   162 ADLEL 166
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
12-256 6.36e-31

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 116.63  E-value: 6.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  12 RVPKAMRQRIRFLTYNVHScfgtdRRLDPARIAAVIAECQPDVIALQEVDVGRARtgGIDQahmiathlnMEAEF-HPAL 90
Cdd:COG3021    86 KSAPAGGPDLRVLTANVLF-----GNADAEALAALVREEDPDVLVLQETTPAWEE--ALAA---------LEADYpYRVL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  91 HLEDEKYGDAVLTALPmrLIKAAPLPSSGEPRGALWVEIDVAEVKLQVIVTHL---GLRGAERLRQATALlgPGWLggmA 167
Cdd:COG3021   150 CPLDNAYGMALLSRLP--LTEAEVVYLVGDDIPSIRATVELPGGPVRLVAVHPappVGGSAERDAELAAL--AKAV---A 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 168 QGDAHVVLAGDLNATGRSTAYRLLARQ--LSDAQllTGAKPRPTFPSRLPLLR--IDHVLIGKGIEVASCRVhgstLARS 243
Cdd:COG3021   223 ALDGPVIVAGDFNATPWSPTLRRLLRAsgLRDAR--AGRGLGPTWPANLPFLRlpIDHVLVSRGLTVVDVRV----LPVI 296
                         250
                  ....*....|...
gi 1879378069 244 ASDHLPLLAELDV 256
Cdd:COG3021   297 GSDHRPLLAELAL 309
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
24-254 3.13e-30

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; 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: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 113.16  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  24 LTYNVHScFGTDR-RLDPARIAAVIAECQPDVIALQEVdVGRARTGGIDQAHMIATHLNMEaeFHPALhlEDEKYGDAVL 102
Cdd:cd09084     2 MSYNVRS-FNRYKwKDDPDKILDFIKKQDPDILCLQEY-YGSEGDKDDDLRLLLKGYPYYY--VVYKS--DSGGTGLAIF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 103 TALPmrLIKAAPLPSSGEPRGALWVEIDVAEVKLQVIVTHL---------------GLRGAERLRQATALLGPGWLGGMA 167
Cdd:cd09084    76 SKYP--ILNSGSIDFPNTNNNAIFADIRVGGDTIRVYNVHLesfritpsdkelykeEKKAKELSRNLLRKLAEAFKRRAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 168 QGDA----------HVVLAGDLNATGRSTAYRLLARQLSDAQLLTGAKPRPTFPSRLPLLRIDHVLIGKGIEVASCRVHG 237
Cdd:cd09084   154 QADLlaadiaaspyPVIVCGDFNDTPASYVYRTLKKGLTDAFVEAGSGFGYTFNGLFFPLRIDYILTSKGFKVLRYRVDP 233
                         250
                  ....*....|....*..
gi 1879378069 238 STLarsaSDHLPLLAEL 254
Cdd:cd09084   234 GKY----SDHYPIVATL 246
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
25-254 6.36e-15

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: 72.25  E-value: 6.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  25 TYNVHscFGTD---------RRldpARIAAVIAECQPDVIALQEVD----------------VGRARTGGIDqahmiath 79
Cdd:cd09083     4 TFNIR--YDNPsdgenswenRK---DLVAELIKFYDPDIIGTQEALphqladleellpeydwIGVGRDDGKE-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  80 lnmEAEFHPALHLEDE----KYGDAVLTALPmrlikaAPLPSSGE----PRGALWVEI-DVAEVK-LQVIVTHLGLRGAE 149
Cdd:cd09083    71 ---KGEFSAIFYRKDRfellDSGTFWLSETP------DVVGSKGWdaalPRICTWARFkDKKTGKeFYVFNTHLDHVGEE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 150 -RLRQATALLGpgWLGGMAqGDAHVVLAGDLNATGRSTAYRLLAR-QLSDAQLLTGAK---PRPTFPS---RLPLLRIDH 221
Cdd:cd09083   142 aREESAKLILE--RIKEIA-GDLPVILTGDFNAEPDSEPYKTLTSgGLKDARDTAATTdggPEGTFHGfkgPPGGSRIDY 218
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1879378069 222 VLIGKGIEVASCRV-HGSTLARSASDHLPLLAEL 254
Cdd:cd09083   219 IFVSPGVKVLSYEIlTDRYDGRYPSDHFPVVADL 252
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
24-247 7.14e-14

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: 68.02  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  24 LTYNVHSCFGTDRRLDP--ARIAAVIAECQPDVIALQEVDVgrartggiDQAHMIATHLNMEAEFHPALHLEDEK--YGD 99
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRklDALAALIRAYDPDVVALQETDD--------DDASRLLLALLAYGGFLSYGGPGGGGggGGV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 100 AVLTALPMRLIKAAPLPSSGEPRGALWVEIDV-AEVKLQVIVTHLGLRGAERLRQATALLGPGWLGGMAQGDAHVVLAGD 178
Cdd:pfam03372  73 AILSRYPLSSVILVDLGEFGDPALRGAIAPFAgVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1879378069 179 LNAtgrstayrllarqlsdaqlltgakprptfpsrlpllriDHVLIGKGIEVASCRVHGSTLARSASDH 247
Cdd:pfam03372 153 FNA--------------------------------------DYILVSGGLTVLSVGVLPDLGPRTGSDH 183
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
9-255 2.29e-13

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 68.89  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069   9 QMLRVPKAMRQRIRFLTYNVHSCFGTDRRLDP---------------ARIAAVIAECQPDVIALQEVDvgrartggiDQA 73
Cdd:COG2374    57 VNPRPEAPVGGDLRVATFNVENLFDTDDDDDDfgrgadtpeeyerklAKIAAAIAALDADIVGLQEVE---------NNG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  74 HMIAT---HLNMEAEFHPALHLEDEKYGDAVLTALPMR-----LIKAAPLP----SSGEP----RGALWVEIDVAEVK-L 136
Cdd:COG2374   128 SALQDlvaALNLAGGTYAFVHPPDGPDGDGIRVALLYRpdrvtLVGSATIAdlpdSPGNPdrfsRPPLAVTFELANGEpF 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 137 QVIVTHL----------GLRGAE--RLRQATALLgpGWLGGM--AQGDAHVVLAGDLNATGRSTAYRLL--ARQLSDAQL 200
Cdd:COG2374   208 TVIVNHFkskgsddpgdGQGASEakRTAQAEALR--AFVDSLlaADPDAPVIVLGDFNDYPFEDPLRALlgAGGLTNLAE 285
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1879378069 201 LTGAKPRPT--FPSRLPLLriDHVLI-------GKGIEVASCRVH------------GSTLARSASDHLPLLAELD 255
Cdd:COG2374   286 KLPAAERYSyvYDGNSGLL--DHILVspalaarVTGADIWHINADiynddfkpdfrtYADDPGRASDHDPVVVGLR 359
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
24-254 7.19e-13

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.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 66.35  E-value: 7.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  24 LTYNVHSCFGTDRRldpARIAAVIAECQPDVIALQEVDVGRARTGGIDQAHMIATHLnmeaeFHPALHLEDEKYGDAVLT 103
Cdd:cd08372     2 ASYNVNGLNAATRA---SGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQ-----YQSGPSRKEGYEGVAILS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 104 ALPMRLIKAAPLPSSGE----PRGALWVEIDVAEVKLQVIVTHL---GLRGAERLRQATALLG-----PGWLGgmaqgdA 171
Cdd:cd08372    74 KTPKFKIVEKHQYKFGEgdsgERRAVVVKFDVHDKELCVVNAHLqagGTRADVRDAQLKEVLEflkrlRQPNS------A 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 172 HVVLAGDLNA--------TGRSTAYRLLARQLSDA-QLLTGAKPRPTFPSRLPlLRIDHVLIGKGIEVASCRVHGSTLAR 242
Cdd:cd08372   148 PVVICGDFNVrpsevdseNPSSMLRLFVALNLVDSfETLPHAYTFDTYMHNVK-SRLDYIFVSKSLLPSVKSSKILSDAA 226
                         250
                  ....*....|....*
gi 1879378069 243 SA---SDHLPLLAEL 254
Cdd:cd08372   227 RAripSDHYPIEVTL 241
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
21-254 1.18e-11

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. 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: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 63.13  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  21 IRFLTYNVHscFGTDRRLDpAR---IAAVIAECQPDVIALQEVdvgrartggIDQA-HMIATHLNMEAEFH----PALHL 92
Cdd:cd09080     1 LKVLTWNVD--FLDDVNLA-ERmraILKLLEELDPDVIFLQEV---------TPPFlAYLLSQPWVRKNYYfsegPPSPA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  93 EDEkYGDAVLTALPMRlIKAAPLPSSGEPRGALWVEIDV-AEVKLQVIVTHL---GLRGAERLRQATALLgpGWLGGmAQ 168
Cdd:cd09080    69 VDP-YGVLILSKKSLV-VRRVPFTSTRMGRNLLAAEINLgSGEPLRLATTHLeslKSHSSERTAQLEEIA--KKLKK-PP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 169 GDAHVVLAGDLNATGRSTAYRLLARQLSDAQLLTGAKPRPTF-----------------PSRL-------PLLRIDHV-L 223
Cdd:cd09080   144 GAANVILGGDFNLRDKEDDTGGLPNGFVDAWEELGPPGEPGYtwdtqknpmlrkgeagpRKRFdrvllrgSDLKPKSIeL 223
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1879378069 224 IGKGievascRVHGSTLARSASDHLPLLAEL 254
Cdd:cd09080   224 IGTE------PIPGDEEGLFPSDHFGLLAEL 248
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
23-254 1.55e-11

Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. 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: 197313 [Multi-domain]  Cd Length: 259  Bit Score: 62.67  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  23 FLTYNVHSC--FGTDRRLDpaRIAAVIAECQPDVIALQEVDV---GRARTGGIDQ---AHMIATHLNMEAEFHPAL---- 90
Cdd:cd09079     1 LLTLNTHSWleENQKEKLE--RLAKIIAEEDYDVIALQEVNQsidAPVSQVPIKEdnfALLLYEKLRELGATYYWTwils 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  91 HLEDEKY--GDAVLTALPMR-----LIKAAPLPSSGEPRGALWVEIDVAEVKLQVIVTHLGLRGAERLRQA-------TA 156
Cdd:cd09079    79 HIGYDKYdeGLAILSKRPIAevedfYVSKSQDYTDYKSRKILGATIEINGQPIDVYSCHLGWWYDEEEPFAyewskleKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 157 LlgpgwlggmAQGDAHVVLAGDLNATGRSTAY---RLLARQLSDAQLLTGAKP-RPTFPSRLP-------LLRIDHVLIG 225
Cdd:cd09079   159 L---------AEAGRPVLLMGDFNNPAGSRGEgydLISSLGLQDTYDLAEEKDgGVTVEKAIDgwrgnkeAKRIDYIFVN 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1879378069 226 KGIEVASCRV--HGsTLARSASDHLPLLAEL 254
Cdd:cd09079   230 RKVKVKSSRVifNG-KNPPIVSDHFGVEVEL 259
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
21-254 5.45e-07

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily 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: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 49.70  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  21 IRFLTYNVHSCFGTDRRLDPARIAAVIAECQPDVIALQEVdvgRARTGGIDQAHMIATHLNMEAE------FHPALH--L 92
Cdd:cd10283     1 LRIASWNILNFGNSKGKEKNPAIAEIISAFDLDLIALQEV---MDNGGGLDALAKLVNELNKPGGtwkyivSDKTGGssG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  93 EDEKYG-----DAVLTALPMRLIK-AAPLPSSGEPRGAL--WVEIDvaeVKLQVIVTHL-------GLRGAERLRQATAL 157
Cdd:cd10283    78 DKERYAflyksSKVRKVGKAVLEKdSNTDGFARPPYAAKfkSGGTG---FDFTLVNVHLksggsskSGQGAKRVAEAQAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 158 LgpGWLGGMAQ--GDAHVVLAGDLNATGRSTAYR-LLARQLSDaqlLTGAKPRPTFPSRLPLLRIDHVLIgKGIEVASCR 234
Cdd:cd10283   155 A--EYLKELADedPDDDVILLGDFNIPADEDAFKaLTKAGFKS---LLPDSTNLSTSFKGYANSYDNIFV-SGNLKEKFS 228
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1879378069 235 VHG------------------STLARSASDHLPLLAEL 254
Cdd:cd10283   229 NSGvfdfnilvdeageedldySKWRKQISDHDPVWVEF 266
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
51-256 3.40e-06

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 47.24  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069  51 QPDVIALQEVDVgrarTGGIDQahmIATHLNMEAEFHPALHLEDEKYGdaVLTALPMRLIKAAPLPSSgEP-----RGAL 125
Cdd:PRK05421   69 DADLVLLQEAQT----TPELVQ---FATANYLAADQAPAFVLPQHPSG--VMTLSKAHPVYCCPLRER-EPwlrlpKSAL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879378069 126 WVEIDVAEVK-LQVIVTH-----LGLRGAER-LRQATALL----GPgwlggmaqgdahVVLAGDLNA--TGRSTAYRLLA 192
Cdd:PRK05421  139 ITEYPLPNGRtLLVVNIHainfsLGVDVYSKqLEPIGDQIahhsGP------------VILAGDFNTwsRKRMNALKRFA 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879378069 193 RQLSDAQLLTGAKPRPTFPSRlPLlriDHVLIgKGIEVASCRVHGStlarSASDHLPLLAELDV 256
Cdd:PRK05421  207 RELGLKEVRFTDDQRRRAFGR-PL---DFVFY-RGLNVSKASVLVT----RASDHNPLLVEFSL 261
 
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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