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Conserved domains on  [gi|750186200|ref|WP_040490274|]
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endonuclease/exonuclease/phosphatase family protein [Indibacter alkaliphilus]

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 ...
27-265 1.24e-29

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


:

Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 109.61  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIYHGENPykPGSTNIEEVTSLISEVNPDFLALQEVdsmtqrtagfagkkldlaktwaektsmnghfakaidfs 106
Cdd:COG3568    8 LRVMTYNIRYGLGT--DGRADLERIARVIRALDPDVVALQEN-------------------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 107 eggygeAVLTKSK-AKFESISLPVPeGGEGRSMAVSYVDLDGGnRLAFAGTHLCHESPINRAAQVKAILEYFKDL--DHP 183
Cdd:COG3568   48 ------AILSRYPiVSSGTFDLPDP-GGEPRGALWADVDVPGK-PLRVVNTHLDLRSAAARRRQARALAELLAELpaGAP 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 184 VIITGDFNFeseeegyalmaehfqdaalvvdnpektyssddpkirIDYFWVPKNFeiEVVSVQTIP----VGYSDHLPLV 259
Cdd:COG3568  120 VILAGDFND------------------------------------IDYILVSPGL--RVLSAEVLDsplgRAASDHLPVV 161

                 ....*.
gi 750186200 260 MEIKMP 265
Cdd:COG3568  162 ADLELP 167
 
Name Accession Description Interval E-value
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
27-265 1.24e-29

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 109.61  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIYHGENPykPGSTNIEEVTSLISEVNPDFLALQEVdsmtqrtagfagkkldlaktwaektsmnghfakaidfs 106
Cdd:COG3568    8 LRVMTYNIRYGLGT--DGRADLERIARVIRALDPDVVALQEN-------------------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 107 eggygeAVLTKSK-AKFESISLPVPeGGEGRSMAVSYVDLDGGnRLAFAGTHLCHESPINRAAQVKAILEYFKDL--DHP 183
Cdd:COG3568   48 ------AILSRYPiVSSGTFDLPDP-GGEPRGALWADVDVPGK-PLRVVNTHLDLRSAAARRRQARALAELLAELpaGAP 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 184 VIITGDFNFeseeegyalmaehfqdaalvvdnpektyssddpkirIDYFWVPKNFeiEVVSVQTIP----VGYSDHLPLV 259
Cdd:COG3568  120 VILAGDFND------------------------------------IDYILVSPGL--RVLSAEVLDsplgRAASDHLPVV 161

                 ....*.
gi 750186200 260 MEIKMP 265
Cdd:COG3568  162 ADLELP 167
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
28-262 6.78e-22

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: 91.12  E-value: 6.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  28 KLMTYNI-----YHGENPY---KPGstnieeVTSLISEVNPDFLALQEV-DSMTQ---------------RTAGFAG--- 80
Cdd:cd09083    1 RVMTFNIrydnpSDGENSWenrKDL------VAELIKFYDPDIIGTQEAlPHQLAdleellpeydwigvgRDDGKEKgef 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  81 -------KKLDLAKtwaektsmNGHFAkaidFSE-----GGYG-EAVLTK--SKAKFEsislpvpeggegrsmavsyvDL 145
Cdd:cd09083   75 saifyrkDRFELLD--------SGTFW----LSEtpdvvGSKGwDAALPRicTWARFK--------------------DK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 146 DGGNRLAFAGTHLCHESPINRAAQVKAILEYFKDL--DHPVIITGDFNFESEEEGYALMAEH-FQDAALVVDNPEKT--- 219
Cdd:cd09083  123 KTGKEFYVFNTHLDHVGEEAREESAKLILERIKEIagDLPVILTGDFNAEPDSEPYKTLTSGgLKDARDTAATTDGGpeg 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 750186200 220 ----YSSDDPKIRIDYFWVPKnfEIEVVSVQTIPVGY-----SDHLPLVMEI 262
Cdd:cd09083  203 tfhgFKGPPGGSRIDYIFVSP--GVKVLSYEILTDRYdgrypSDHFPVVADL 252
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
30-255 2.08e-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: 69.56  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200   30 MTYNIYHGENPYKPGSTNIEEVTSLISEVNPDFLALQEVDSMTQRTAGFAGKKLDlaktwaektsmNGHFAKAIDFSEGG 109
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYG-----------GFLSYGGPGGGGGG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  110 YGEAVLTKSKAKFESISLPVPEGGEGRSMAVSYVDLDGGNRLAFAGTHLCHESPIN---RAAQVKAILEYFKDLDHPVII 186
Cdd:pfam03372  70 GGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARdeqRADLLLLLLALLAPRSEPVIL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 750186200  187 TGDFNfeseeegyalmaehfqdaalvvdnpektyssddpkirIDYFWVPKNFEIEVVSVQTIPVGY--SDH 255
Cdd:pfam03372 150 AGDFN-------------------------------------ADYILVSGGLTVLSVGVLPDLGPRtgSDH 183
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
21-261 4.78e-11

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  21 FAQNNLIKLMTYNIYHGENPykpgstNIEEVTSLISEvNPDFLALQEVdSMTQRTAGFAGKKldlaktwaektSMNGHFA 100
Cdd:PRK05421  38 LSTEERLRLLVWNIYKQQRA------GWLSVLKNLGK-DADLVLLQEA-QTTPELVQFATAN-----------YLAADQA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 101 KAIDFSEGGYGeaVLTKSKAKFESI-SLPVPEGGEG--RSMAVSYVDLDGGNRLAFAGTHLchespIN-------RAAQV 170
Cdd:PRK05421  99 PAFVLPQHPSG--VMTLSKAHPVYCcPLREREPWLRlpKSALITEYPLPNGRTLLVVNIHA-----INfslgvdvYSKQL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 171 KAILEYFKDLDHPVIITGDFNFESEEEgYALMAEHFQDAALVvdnpEKTYSSDDpkiRIDYFWVPKNF----EIEVVSVQ 246
Cdd:PRK05421 172 EPIGDQIAHHSGPVILAGDFNTWSRKR-MNALKRFARELGLK----EVRFTDDQ---RRRAFGRPLDFvfyrGLNVSKAS 243
                        250
                 ....*....|....*
gi 750186200 247 TIPVGYSDHLPLVME 261
Cdd:PRK05421 244 VLVTRASDHNPLLVE 258
 
Name Accession Description Interval E-value
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
27-265 1.24e-29

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 109.61  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIYHGENPykPGSTNIEEVTSLISEVNPDFLALQEVdsmtqrtagfagkkldlaktwaektsmnghfakaidfs 106
Cdd:COG3568    8 LRVMTYNIRYGLGT--DGRADLERIARVIRALDPDVVALQEN-------------------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 107 eggygeAVLTKSK-AKFESISLPVPeGGEGRSMAVSYVDLDGGnRLAFAGTHLCHESPINRAAQVKAILEYFKDL--DHP 183
Cdd:COG3568   48 ------AILSRYPiVSSGTFDLPDP-GGEPRGALWADVDVPGK-PLRVVNTHLDLRSAAARRRQARALAELLAELpaGAP 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 184 VIITGDFNFeseeegyalmaehfqdaalvvdnpektyssddpkirIDYFWVPKNFeiEVVSVQTIP----VGYSDHLPLV 259
Cdd:COG3568  120 VILAGDFND------------------------------------IDYILVSPGL--RVLSAEVLDsplgRAASDHLPVV 161

                 ....*.
gi 750186200 260 MEIKMP 265
Cdd:COG3568  162 ADLELP 167
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
3-265 1.13e-23

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


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 97.37  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200   3 ILAILTTLFFLTFASPMLF-------AQNNLIKLMTYNIYHGenpykpgSTNIEEVTSLISEVNPDFLALQEVDSMTQRt 75
Cdd:COG3021   64 AAALLLLLVQAALILPYTLpapksapAGGPDLRVLTANVLFG-------NADAEALAALVREEDPDVLVLQETTPAWEE- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  76 agfagkKLD-LAKTWAektsmngHFAKAIDfsEGGYGEAVLtkSKAKFESISlPVPEGGEGRSMAVSYVDLDGGnRLAFA 154
Cdd:COG3021  136 ------ALAaLEADYP-------YRVLCPL--DNAYGMALL--SRLPLTEAE-VVYLVGDDIPSIRATVELPGG-PVRLV 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 155 GTHLchESPI----NRAAQVKAILEYFKDLDHPVIITGDFNfeSEEEGYALmaEHFQDAALVVDnPEK------TYSSD- 223
Cdd:COG3021  197 AVHP--APPVggsaERDAELAALAKAVAALDGPVIVAGDFN--ATPWSPTL--RRLLRASGLRD-ARAgrglgpTWPANl 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 750186200 224 -DPKIRIDYFWVPKnfEIEVVSVQTIPVGYSDHLPLVMEIKMP 265
Cdd:COG3021  270 pFLRLPIDHVLVSR--GLTVVDVRVLPVIGSDHRPLLAELALP 310
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
28-262 6.78e-22

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: 91.12  E-value: 6.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  28 KLMTYNI-----YHGENPY---KPGstnieeVTSLISEVNPDFLALQEV-DSMTQ---------------RTAGFAG--- 80
Cdd:cd09083    1 RVMTFNIrydnpSDGENSWenrKDL------VAELIKFYDPDIIGTQEAlPHQLAdleellpeydwigvgRDDGKEKgef 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  81 -------KKLDLAKtwaektsmNGHFAkaidFSE-----GGYG-EAVLTK--SKAKFEsislpvpeggegrsmavsyvDL 145
Cdd:cd09083   75 saifyrkDRFELLD--------SGTFW----LSEtpdvvGSKGwDAALPRicTWARFK--------------------DK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 146 DGGNRLAFAGTHLCHESPINRAAQVKAILEYFKDL--DHPVIITGDFNFESEEEGYALMAEH-FQDAALVVDNPEKT--- 219
Cdd:cd09083  123 KTGKEFYVFNTHLDHVGEEAREESAKLILERIKEIagDLPVILTGDFNAEPDSEPYKTLTSGgLKDARDTAATTDGGpeg 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 750186200 220 ----YSSDDPKIRIDYFWVPKnfEIEVVSVQTIPVGY-----SDHLPLVMEI 262
Cdd:cd09083  203 tfhgFKGPPGGSRIDYIFVSP--GVKVLSYEILTDRYdgrypSDHFPVVADL 252
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
27-255 6.46e-18

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: 80.47  E-value: 6.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIYHGENPYKpgSTNIEEVTSLISEVNPDFLALQEVdsmTQRTAGFagkkLDLAKTWAEK-TSMNGHFAKAIDf 105
Cdd:cd09080    1 LKVLTWNVDFLDDVNL--AERMRAILKLLEELDPDVIFLQEV---TPPFLAY----LLSQPWVRKNyYFSEGPPSPAVD- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 106 segGYGEAVLtkSKAKFESISLPVPEGGEGRSMAVSYVDLDGGNRLAFAGTHLchESPIN----RAAQVKAILEYFKDLD 181
Cdd:cd09080   71 ---PYGVLIL--SKKSLVVRRVPFTSTRMGRNLLAAEINLGSGEPLRLATTHL--ESLKShsseRTAQLEEIAKKLKKPP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 182 --HPVIITGDFNFESEEEGYALMAEHFQDAALVV-------------DNPEKTYSSDDPKIRID--YF----WVPKNFEI 240
Cdd:cd09080  144 gaANVILGGDFNLRDKEDDTGGLPNGFVDAWEELgppgepgytwdtqKNPMLRKGEAGPRKRFDrvLLrgsdLKPKSIEL 223
                        250
                 ....*....|....*...
gi 750186200 241 ---EVVSVQTIPVGYSDH 255
Cdd:cd09080  224 igtEPIPGDEEGLFPSDH 241
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
29-262 1.47e-15

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: 73.67  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  29 LMTYNIyHGENpykpGSTNIEEVTSLISEVNPDFLALQEVDSMTQRTAGFAGKKLDLAKtwaektsmngHFAKAIDFSEG 108
Cdd:cd08372    1 VASYNV-NGLN----AATRASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYH----------QYQSGPSRKEG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 109 GYGEAVLTKSKaKFESISLPVPEGGEGRSMA--VSYVDLDGGNR-LAFAGTHLCHESPIN--RAAQVKAILEYFKDL--- 180
Cdd:cd08372   66 YEGVAILSKTP-KFKIVEKHQYKFGEGDSGErrAVVVKFDVHDKeLCVVNAHLQAGGTRAdvRDAQLKEVLEFLKRLrqp 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 181 -DHPVIITGDFN---FESEEEGYALMAEHFQDAALVVDNPEK----TYSS--DDPKIRIDYFWVPKNFEIEVVSVQTIPV 250
Cdd:cd08372  145 nSAPVVICGDFNvrpSEVDSENPSSMLRLFVALNLVDSFETLphayTFDTymHNVKSRLDYIFVSKSLLPSVKSSKILSD 224
                        250
                 ....*....|....*..
gi 750186200 251 G-----YSDHLPLVMEI 262
Cdd:cd08372  225 AarariPSDHYPIEVTL 241
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
29-262 4.12e-15

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: 72.71  E-value: 4.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  29 LMTYNIyHGENPYKpGSTNIEEVTSLISEVNPDFLALQEvdsmtqrTAGFAGKKLDLAKTWAEKTSmngHFAKAIDFSEG 108
Cdd:cd09084    1 VMSYNV-RSFNRYK-WKDDPDKILDFIKKQDPDILCLQE-------YYGSEGDKDDDLRLLLKGYP---YYYVVYKSDSG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 109 GYGEAVLTK---SKAKfesiSLPVPEGGEGrsmaVSYVDLD-GGNRLAFAGTHLchESP--------------------- 163
Cdd:cd09084   69 GTGLAIFSKypiLNSG----SIDFPNTNNN----AIFADIRvGGDTIRVYNVHL--ESFritpsdkelykeekkakelsr 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 164 ----------INRAAQVKAILEYFKDLDHPVIITGDFNFESEEEGYALMAEHFQDAALVVDN-PEKTYSSDDPKIRIDYF 232
Cdd:cd09084  139 nllrklaeafKRRAAQADLLAADIAASPYPVIVCGDFNDTPASYVYRTLKKGLTDAFVEAGSgFGYTFNGLFFPLRIDYI 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 750186200 233 WVPKNFeiEVVSVQTIPVGYSDHLPLVMEI 262
Cdd:cd09084  219 LTSKGF--KVLRYRVDPGKYSDHYPIVATL 246
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
30-255 2.08e-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: 69.56  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200   30 MTYNIYHGENPYKPGSTNIEEVTSLISEVNPDFLALQEVDSMTQRTAGFAGKKLDlaktwaektsmNGHFAKAIDFSEGG 109
Cdd:pfam03372   1 LTWNVNGGNADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYG-----------GFLSYGGPGGGGGG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  110 YGEAVLTKSKAKFESISLPVPEGGEGRSMAVSYVDLDGGNRLAFAGTHLCHESPIN---RAAQVKAILEYFKDLDHPVII 186
Cdd:pfam03372  70 GGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARdeqRADLLLLLLALLAPRSEPVIL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 750186200  187 TGDFNfeseeegyalmaehfqdaalvvdnpektyssddpkirIDYFWVPKNFEIEVVSVQTIPVGY--SDH 255
Cdd:pfam03372 150 AGDFN-------------------------------------ADYILVSGGLTVLSVGVLPDLGPRtgSDH 183
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
27-262 2.68e-11

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: 62.03  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIYHGENpyKPGSTNIEEVTSLISEVNPDFLALQEVDSMTQRTAG---FAGKKLDLAKTWAEKTSMNGHfakai 103
Cdd:cd10283    1 LRIASWNILNFGN--SKGKEKNPAIAEIISAFDLDLIALQEVMDNGGGLDAlakLVNELNKPGGTWKYIVSDKTG----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 104 dfSEGGYGE--AVLTKSkAKFESISLPVPEGGEGRS------MAVSYVDLDGGNRLAFAGTHL------CHESPINRAAQ 169
Cdd:cd10283   74 --GSSGDKEryAFLYKS-SKVRKVGKAVLEKDSNTDgfarppYAAKFKSGGTGFDFTLVNVHLksggssKSGQGAKRVAE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 170 VKAILEYFK-----DLDHPVIITGDFNFESEEEGY-ALMAEHFQDaaLVVDNPEKTYSSDDPKIRIDYFWVPKN------ 237
Cdd:cd10283  151 AQALAEYLKeladeDPDDDVILLGDFNIPADEDAFkALTKAGFKS--LLPDSTNLSTSFKGYANSYDNIFVSGNlkekfs 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 750186200 238 -----------FEIEVVSVQTIPVGY--SDHLPLVMEI 262
Cdd:cd10283  229 nsgvfdfnilvDEAGEEDLDYSKWRKqiSDHDPVWVEF 266
PRK05421 PRK05421
endonuclease/exonuclease/phosphatase family protein;
21-261 4.78e-11

endonuclease/exonuclease/phosphatase family protein;


Pssm-ID: 235454 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  21 FAQNNLIKLMTYNIYHGENPykpgstNIEEVTSLISEvNPDFLALQEVdSMTQRTAGFAGKKldlaktwaektSMNGHFA 100
Cdd:PRK05421  38 LSTEERLRLLVWNIYKQQRA------GWLSVLKNLGK-DADLVLLQEA-QTTPELVQFATAN-----------YLAADQA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 101 KAIDFSEGGYGeaVLTKSKAKFESI-SLPVPEGGEG--RSMAVSYVDLDGGNRLAFAGTHLchespIN-------RAAQV 170
Cdd:PRK05421  99 PAFVLPQHPSG--VMTLSKAHPVYCcPLREREPWLRlpKSALITEYPLPNGRTLLVVNIHA-----INfslgvdvYSKQL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 171 KAILEYFKDLDHPVIITGDFNFESEEEgYALMAEHFQDAALVvdnpEKTYSSDDpkiRIDYFWVPKNF----EIEVVSVQ 246
Cdd:PRK05421 172 EPIGDQIAHHSGPVILAGDFNTWSRKR-MNALKRFARELGLK----EVRFTDDQ---RRRAFGRPLDFvfyrGLNVSKAS 243
                        250
                 ....*....|....*
gi 750186200 247 TIPVGYSDHLPLVME 261
Cdd:PRK05421 244 VLVTRASDHNPLLVE 258
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
49-262 9.88e-09

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-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. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-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: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 54.28  E-value: 9.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  49 EEVTSLISEVNPDFLALQEvdsmTQRTagfaGKKLDLAKTWAEKTSMNGHFAKAIDfseggyGEAVLTKSKAKFESISLP 128
Cdd:cd09076   16 AQLLEELKRKKLDILGLQE----THWT----GEGELKKKREGGTILYSGSDSGKSR------GVAILLSKTAANKLLEYT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 129 VPEggEGRSMAVSyvdLDGGN-RLAFAGTHlcheSPINRAAQVKAilEYFKDLD---------HPVIITGDFNF--ESEE 196
Cdd:cd09076   82 KVV--SGRIIMVR---FKIKGkRLTIINVY----APTARDEEEKE--EFYDQLQdvldkvprhDTLIIGGDFNAvlGPKD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 197 EGYALM------AEHFQDAAL----VVD-----NPEK---TYSSDDPKI--RIDYFWVPKNFEIEVVSVQTIPVGYSDHL 256
Cdd:cd09076  151 DGRKGLdkrnenGERALSALIeehdLVDvwrenNPKTreyTWRSPDHGSrsRIDRILVSKRLRVKVKKTKITPGAGSDHR 230

                 ....*.
gi 750186200 257 PLVMEI 262
Cdd:cd09076  231 LVTLKL 236
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
27-262 2.15e-08

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. 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: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 53.89  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIY-HGENPYKPGSTNIEEVTSLI--SEVNPDFLALQEV------DSMTQRTAGFAGKKLDLaktwaekTSMNG 97
Cdd:cd09078    1 LKVLTYNVFlLPPLLYNNGDDGQDERLDLIpkALLQYDVVVLQEVfdararKRLLNGLKKEYPYQTDV-------VGRSP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  98 HFA--KAIDfseGGygeaVLTKSKakF---ESISLPVPEGGEGRSMA---VSYV--DLDGGNRLAFAGTHL------CHE 161
Cdd:cd09078   74 SGWssKLVD---GG----VVILSR--YpivEKDQYIFPNGCGADCLAakgVLYAkiNKGGTKVYHVFGTHLqasdgsCLD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 162 SPInRAAQVKAILEYFKD----LDHPVIITGDFNFE---SEEEGYALMAEHFQDAALVVDNPEKTYSSDDPKI------- 227
Cdd:cd09078  145 RAV-RQKQLDELRAFIEEknipDNEPVIIAGDFNVDkrsSRDEYDDMLEQLHDYNAPEPITAGETPLTWDPGTnllakyn 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 750186200 228 -------RIDY-FWVPKNF-------EIEVVSVQTIPV-------GYSDHLPLVMEI 262
Cdd:cd09078  224 ypggggeRLDYiLYSNDHLqpsswsnEVEVPKSPTWSVtngytfaDLSDHYPVSATF 280
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
29-262 1.23e-07

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: 51.50  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  29 LMTYNIyHG---ENP-YKpgstnIEEVTSLISEVNPDFLALQEVDSMTQRTAGFAGKKLD-LAKTWAEKTSMNGHFAKAI 103
Cdd:cd09079    1 LLTLNT-HSwleENQkEK-----LERLAKIIAEEDYDVIALQEVNQSIDAPVSQVPIKEDnFALLLYEKLRELGATYYWT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 104 -DFSEGGYGE-----AVLTKSK-AKFESISLpvpegGEGRSM-------AVSYVDLDGGNRLAFAGTHL----CHESPIn 165
Cdd:cd09079   75 wILSHIGYDKydeglAILSKRPiAEVEDFYV-----SKSQDYtdyksrkILGATIEINGQPIDVYSCHLgwwyDEEEPF- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 166 rAAQVKAILEYFKDLDHPVIITGDFNFE--SEEEGY-ALMAEHFQDAALVVDNPEK---------TYSSDDPKIRIDYFW 233
Cdd:cd09079  149 -AYEWSKLEKALAEAGRPVLLMGDFNNPagSRGEGYdLISSLGLQDTYDLAEEKDGgvtvekaidGWRGNKEAKRIDYIF 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 750186200 234 VPKNFeiEVVSVQTI-----PVGYSDHLPLVMEI 262
Cdd:cd09079  228 VNRKV--KVKSSRVIfngknPPIVSDHFGVEVEL 259
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
27-265 2.62e-07

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 50.79  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  27 IKLMTYNIyhgEN---------PYKPGSTNIEE-------VTSLISEVNPDFLALQEVDSMTQRTAGFAGKKLDLAKTWA 90
Cdd:COG2374   69 LRVATFNV---ENlfdtdddddDFGRGADTPEEyerklakIAAAIAALDADIVGLQEVENNGSALQDLVAALNLAGGTYA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  91 EKTSMNGHFAKAIDFseggygeAVLTKsKAKFE-----SISLPVPEGGEGRS-----MAVSyVDLDGGNRLAFAGTHL-- 158
Cdd:COG2374  146 FVHPPDGPDGDGIRV-------ALLYR-PDRVTlvgsaTIADLPDSPGNPDRfsrppLAVT-FELANGEPFTVIVNHFks 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 159 ---------CHESPINRAAQVKAILEYFKDL-----DHPVIITGDFNFESEEEGYALMAEH--FQDAALVVDNPEK-TYS 221
Cdd:COG2374  217 kgsddpgdgQGASEAKRTAQAEALRAFVDSLlaadpDAPVIVLGDFNDYPFEDPLRALLGAggLTNLAEKLPAAERySYV 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 750186200 222 SDDPKIRIDYFWVPKNFEIEVVSVQTI---------------------PVGYSDHLPLVMEIKMP 265
Cdd:COG2374  297 YDGNSGLLDHILVSPALAARVTGADIWhinadiynddfkpdfrtyaddPGRASDHDPVVVGLRLP 361
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
60-259 8.71e-04

C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the C-terminal catalytic domain of the deadenylase, nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. In mouse, the nocturnin gene, mNoc, is expressed in a circadian pattern in a range of tissues including retina, spleen, heart, kidney, and liver. It is highly expressed in bone-marrow stromal cells, adipocytes and hepatocytes. In mammals, nocturnin plays a role in regulating mesenchymal stem-cell lineage allocation, perhaps through regulating PPAR-gamma (peroxisome proliferator-activated receptor-gamma) nuclear translocation. 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: 197330 [Multi-domain]  Cd Length: 280  Bit Score: 40.10  E-value: 8.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200  60 PDFLALQEVD--------SMTQRtaGFAGkkLDLAKTWAEKTSMNGhfakaidfSEGGYGEAVLTKsKAKF-----ESIS 126
Cdd:cd09096   45 PDILCLQEVDhykdtlqpLLSRL--GYQG--TFFPKPDSPCLYIEN--------NNGPDGCALFFR-KDRFelvntEKIR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 127 LPVPEGGEGR-SMAVSYVDLDGGNRLAFAGTHLCHESPIN--RAAQVKAILEYFKDLDH----PVIITGDFNFESEEEGY 199
Cdd:cd09096  112 LSAMTLKTNQvAIACTLRCKETGREICLAVTHLKARTGWErlRSEQGKDLLQNLQSFIEgakiPLIICGDFNAEPTEPVY 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750186200 200 almaEHFQDAALVVDNPEKTYSSD---DP-----KIR--------IDYFWVPKNfEIEVVSVQTIPVGY----------- 252
Cdd:cd09096  192 ----KTFSNSSLNLNSAYKLLSADgqsEPpyttwKIRtsgecrhtLDYIFYSKD-ALSVEQLLDLPTEEqigpnrlpsfn 266

                 ....*....
gi 750186200 253 --SDHLPLV 259
Cdd:cd09096  267 ypSDHLSLV 275
 
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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