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Conserved domains on  [gi|336032625|gb|AEH78557|]
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hypothetical protein SM11_chr1280 [Sinorhizobium meliloti SM11]

Protein Classification

endonuclease/exonuclease/phosphatase family protein( domain architecture ID 11457186)

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

CATH:  3.60.10.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0016787|GO:0003677
PubMed:  10838565
SCOP:  4002213

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
1-368 5.00e-56

Predicted extracellular nuclease [General function prediction only];


:

Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 187.15  E-value: 5.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625   1 MSLRLATFNIENLMSRFDFSgfrnqlkqDRVLRLFDvrSEAEYQRLeeartIAHTddtrqmsALAIADCDADILCLQEA- 79
Cdd:COG2374   67 GDLRVATFNVENLFDTDDDD--------DDFGRGAD--TPEEYERK-----LAKI-------AAAIAALDADIVGLQEVe 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  80 DNMAALQAFEYGylFRMAGNGYRQKYLVEGNDSRGIDVAVLMREEtrdgqKIECLEVKSHAALTYEDLDlfndelaltnr 159
Cdd:COG2374  125 NNGSALQDLVAA--LNLAGGTYAFVHPPDGPDGDGIRVALLYRPD-----RVTLVGSATIADLPDSPGN----------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 160 prDRIFKRDCLEVDVRI-GGRPLTLYVVHLKSMGPAREGlDGRQATMAVRIAEVKAVRHIIERRFGRGHTADKVfaICGD 238
Cdd:COG2374  187 --PDRFSRPPLAVTFELaNGEPFTVIVNHFKSKGSDDPG-DGQGASEAKRTAQAEALRAFVDSLLAADPDAPVI--VLGD 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 239 MNDYqekvkvlgdrrngyeflPHEETTSALdvLSHDGFVeNPNLRRPVLDRWTLFHsrgpeDRHLCQLDYIWLSPELARR 318
Cdd:COG2374  262 FNDY-----------------PFEDPLRAL--LGAGGLT-NLAEKLPAAERYSYVY-----DGNSGLLDHILVSPALAAR 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 336032625 319 NAARLPEIIRAGQpYRTIFpagqeVERYPRTGWDRPKASDHCPVVMTLDI 368
Cdd:COG2374  317 VTGADIWHINADI-YNDDF-----KPDFRTYADDPGRASDHDPVVVGLRL 360
 
Name Accession Description Interval E-value
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
1-368 5.00e-56

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 187.15  E-value: 5.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625   1 MSLRLATFNIENLMSRFDFSgfrnqlkqDRVLRLFDvrSEAEYQRLeeartIAHTddtrqmsALAIADCDADILCLQEA- 79
Cdd:COG2374   67 GDLRVATFNVENLFDTDDDD--------DDFGRGAD--TPEEYERK-----LAKI-------AAAIAALDADIVGLQEVe 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  80 DNMAALQAFEYGylFRMAGNGYRQKYLVEGNDSRGIDVAVLMREEtrdgqKIECLEVKSHAALTYEDLDlfndelaltnr 159
Cdd:COG2374  125 NNGSALQDLVAA--LNLAGGTYAFVHPPDGPDGDGIRVALLYRPD-----RVTLVGSATIADLPDSPGN----------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 160 prDRIFKRDCLEVDVRI-GGRPLTLYVVHLKSMGPAREGlDGRQATMAVRIAEVKAVRHIIERRFGRGHTADKVfaICGD 238
Cdd:COG2374  187 --PDRFSRPPLAVTFELaNGEPFTVIVNHFKSKGSDDPG-DGQGASEAKRTAQAEALRAFVDSLLAADPDAPVI--VLGD 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 239 MNDYqekvkvlgdrrngyeflPHEETTSALdvLSHDGFVeNPNLRRPVLDRWTLFHsrgpeDRHLCQLDYIWLSPELARR 318
Cdd:COG2374  262 FNDY-----------------PFEDPLRAL--LGAGGLT-NLAEKLPAAERYSYVY-----DGNSGLLDHILVSPALAAR 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 336032625 319 NAARLPEIIRAGQpYRTIFpagqeVERYPRTGWDRPKASDHCPVVMTLDI 368
Cdd:COG2374  317 VTGADIWHINADI-YNDDF-----KPDFRTYADDPGRASDHDPVVVGLRL 360
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
53-241 2.67e-08

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: 54.22  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  53 AHTDDTRQMSALaIADCDADILCLQEadnmAALQAFEYGYLFRMAGNGYRQKYLVEGNDSRGIDVAVLMReetrdgqkie 132
Cdd:cd09084   13 KWKDDPDKILDF-IKKQDPDILCLQE----YYGSEGDKDDDLRLLLKGYPYYYVVYKSDSGGTGLAIFSK---------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 133 cLEVKSHAALTYEdldlfndelaltNRPRDRIFkrdcleVDVRIGGRPLTLYVVHLKSMG-------PAREGLDGRQA-- 203
Cdd:cd09084   78 -YPILNSGSIDFP------------NTNNNAIF------ADIRVGGDTIRVYNVHLESFRitpsdkeLYKEEKKAKELsr 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 336032625 204 --------TMAVRIAEVKAVRHIIERRFGrghtadKVFaICGDMND 241
Cdd:cd09084  139 nllrklaeAFKRRAAQADLLAADIAASPY------PVI-VCGDFND 177
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
230-366 5.28e-05

exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model also contains eukaryotic apurinic/apyrimidinic endonucleases which group in the same family [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272954 [Multi-domain]  Cd Length: 254  Bit Score: 44.30  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  230 DKVFAICGDMNDYQEKVKV-LGD-RRNGYEFLPHEetTSALDVLSHDGFVE-----NPNLRRPVldrWTLFHSRGPEDRH 302
Cdd:TIGR00195 138 DKPVLICGDMNIAPTEIDLhIPDeNRNHTGFLPEE--REWLDRLLEAGLVDtfrkfNPDEGAYS---WWDYRTKARDRNR 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336032625  303 LCQLDYIWLSPELARRnaarlpeIIRAGqpyrtifpagqeVERYPRtGWDRPkaSDHCPVVMTL 366
Cdd:TIGR00195 213 GWRIDYFLVSEPLKER-------CVDCG------------IDYDIR-GSEKP--SDHCPVVLEF 254
 
Name Accession Description Interval E-value
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
1-368 5.00e-56

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 187.15  E-value: 5.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625   1 MSLRLATFNIENLMSRFDFSgfrnqlkqDRVLRLFDvrSEAEYQRLeeartIAHTddtrqmsALAIADCDADILCLQEA- 79
Cdd:COG2374   67 GDLRVATFNVENLFDTDDDD--------DDFGRGAD--TPEEYERK-----LAKI-------AAAIAALDADIVGLQEVe 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  80 DNMAALQAFEYGylFRMAGNGYRQKYLVEGNDSRGIDVAVLMREEtrdgqKIECLEVKSHAALTYEDLDlfndelaltnr 159
Cdd:COG2374  125 NNGSALQDLVAA--LNLAGGTYAFVHPPDGPDGDGIRVALLYRPD-----RVTLVGSATIADLPDSPGN----------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 160 prDRIFKRDCLEVDVRI-GGRPLTLYVVHLKSMGPAREGlDGRQATMAVRIAEVKAVRHIIERRFGRGHTADKVfaICGD 238
Cdd:COG2374  187 --PDRFSRPPLAVTFELaNGEPFTVIVNHFKSKGSDDPG-DGQGASEAKRTAQAEALRAFVDSLLAADPDAPVI--VLGD 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 239 MNDYqekvkvlgdrrngyeflPHEETTSALdvLSHDGFVeNPNLRRPVLDRWTLFHsrgpeDRHLCQLDYIWLSPELARR 318
Cdd:COG2374  262 FNDY-----------------PFEDPLRAL--LGAGGLT-NLAEKLPAAERYSYVY-----DGNSGLLDHILVSPALAAR 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 336032625 319 NAARLPEIIRAGQpYRTIFpagqeVERYPRTGWDRPKASDHCPVVMTLDI 368
Cdd:COG2374  317 VTGADIWHINADI-YNDDF-----KPDFRTYADDPGRASDHDPVVVGLRL 360
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
160-368 9.84e-09

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 54.14  E-value: 9.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 160 PRDRIFKRDCLEVDVRIGGRPLTLYVVHLKSMGParegldgrqatmAVRIAEVKAVRHIIERRFGRGHTadkvfAICGDM 239
Cdd:COG3568   64 PDPGGEPRGALWADVDVPGKPLRVVNTHLDLRSA------------AARRRQARALAELLAELPAGAPV-----ILAGDF 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 240 NDyqekvkvlgdrrngyeflpheettsaldvlshdgfvenpnlrrpvldrwtlfhsrgpedrhlcqLDYIWLSPELARRN 319
Cdd:COG3568  127 ND----------------------------------------------------------------IDYILVSPGLRVLS 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 336032625 320 AARLpeiiragqpyrtifpagqeveryprTGWDRPKASDHCPVVMTLDI 368
Cdd:COG3568  143 AEVL-------------------------DSPLGRAASDHLPVVADLEL 166
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
53-241 2.67e-08

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: 54.22  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  53 AHTDDTRQMSALaIADCDADILCLQEadnmAALQAFEYGYLFRMAGNGYRQKYLVEGNDSRGIDVAVLMReetrdgqkie 132
Cdd:cd09084   13 KWKDDPDKILDF-IKKQDPDILCLQE----YYGSEGDKDDDLRLLLKGYPYYYVVYKSDSGGTGLAIFSK---------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 133 cLEVKSHAALTYEdldlfndelaltNRPRDRIFkrdcleVDVRIGGRPLTLYVVHLKSMG-------PAREGLDGRQA-- 203
Cdd:cd09084   78 -YPILNSGSIDFP------------NTNNNAIF------ADIRVGGDTIRVYNVHLESFRitpsdkeLYKEEKKAKELsr 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 336032625 204 --------TMAVRIAEVKAVRHIIERRFGrghtadKVFaICGDMND 241
Cdd:cd09084  139 nllrklaeAFKRRAAQADLLAADIAASPY------PVI-VCGDFND 177
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
66-366 3.77e-08

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: 53.64  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  66 IADCDADILCLQEADNMAALQAFEYGYLFrmagNGYRQkYLVEGNDSRGID-VAVLMREEtrdgqKIECLEVKshaalty 144
Cdd:cd08372   22 VRELDPDIVCLQEVKDSQYSAVALNQLLP----EGYHQ-YQSGPSRKEGYEgVAILSKTP-----KFKIVEKH------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 145 edlDLFNDELALTNRPrdrifkrdCLEVDVRIGGRPLTLYVVHLKSMGPAREgldgrqatmaVRIAEVKAVRHIIERRfg 224
Cdd:cd08372   85 ---QYKFGEGDSGERR--------AVVVKFDVHDKELCVVNAHLQAGGTRAD----------VRDAQLKEVLEFLKRL-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 225 RGHTADKVFaICGDMNDYQEKVkvlgdrrngyeflpHEETTSALDVLSHDGFVENPNLRRPVLDRWTLFHSRGPedrhlC 304
Cdd:cd08372  142 RQPNSAPVV-ICGDFNVRPSEV--------------DSENPSSMLRLFVALNLVDSFETLPHAYTFDTYMHNVK-----S 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336032625 305 QLDYIWLSPELarrnaarLPEIIRAGqpyrtIFPAGQEVERYprtgwdrpkaSDHCPVVMTL 366
Cdd:cd08372  202 RLDYIFVSKSL-------LPSVKSSK-----ILSDAARARIP----------SDHYPIEVTL 241
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
3-366 1.41e-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: 52.02  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625   3 LRLATFNIENLmsrfdfsgfrnqlkqdrvlrlFDVRSEAEYQRLeeARTIAHTDdtrqmsalaiadcdADILCLQE-ADN 81
Cdd:cd10283    1 LRIASWNILNF---------------------GNSKGKEKNPAI--AEIISAFD--------------LDLIALQEvMDN 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  82 MAALQAFEYgylFRMAGNGYRQ--KYLV----EGNDSRGIDVAVLMREETRDGQKieclevkshaaLTYEDLDLfndela 155
Cdd:cd10283   44 GGGLDALAK---LVNELNKPGGtwKYIVsdktGGSSGDKERYAFLYKSSKVRKVG-----------KAVLEKDS------ 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 156 lTNRPRDRI-----FKrdclevdVRIGGRPLTLYVVHLKSmGPAREGLDGRQatmavRIAEVKAVRHIIERRFGRGHTAD 230
Cdd:cd10283  104 -NTDGFARPpyaakFK-------SGGTGFDFTLVNVHLKS-GGSSKSGQGAK-----RVAEAQALAEYLKELADEDPDDD 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625 231 kVFaICGDMNDYqekvkvlgdrrngyeflPHEEttsALDVLSHDGFVenpnlrrPVLDRWTLfHSR--GPEDRHLcqlDY 308
Cdd:cd10283  170 -VI-LLGDFNIP-----------------ADED---AFKALTKAGFK-------SLLPDSTN-LSTsfKGYANSY---DN 216
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 336032625 309 IWLSPELArrnaarlpEIIRAGQPYRTIFPAGQEVERYPRTGWDRPKASDHCPVVMTL 366
Cdd:cd10283  217 IFVSGNLK--------EKFSNSGVFDFNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
XthA COG0708
Exonuclease III [Replication, recombination and repair];
306-367 1.29e-05

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 46.22  E-value: 1.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336032625 306 LDYIWLSPELARRnaarlpeIIRAGqpyrtifpagqeVERYPRtGWDRPkaSDHCPVVMTLD 367
Cdd:COG0708  217 IDYILASPALADR-------LKDAG------------IDREPR-GDERP--SDHAPVVVELD 256
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
230-366 5.28e-05

exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model also contains eukaryotic apurinic/apyrimidinic endonucleases which group in the same family [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272954 [Multi-domain]  Cd Length: 254  Bit Score: 44.30  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336032625  230 DKVFAICGDMNDYQEKVKV-LGD-RRNGYEFLPHEetTSALDVLSHDGFVE-----NPNLRRPVldrWTLFHSRGPEDRH 302
Cdd:TIGR00195 138 DKPVLICGDMNIAPTEIDLhIPDeNRNHTGFLPEE--REWLDRLLEAGLVDtfrkfNPDEGAYS---WWDYRTKARDRNR 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336032625  303 LCQLDYIWLSPELARRnaarlpeIIRAGqpyrtifpagqeVERYPRtGWDRPkaSDHCPVVMTL 366
Cdd:TIGR00195 213 GWRIDYFLVSEPLKER-------CVDCG------------IDYDIR-GSEKP--SDHCPVVLEF 254
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
306-366 3.53e-03

Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Escherichia coli ExoIII, Neisseria meningitides NExo,and related proteins. These are ExoIII family AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiencies. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For example, Neisseria meningitides Nape and NExo, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. NExo and ExoIII are found in this subfamily. NExo is the non-dominant AP endonuclease. It exhibits strong 3'-5' exonuclease and 3'-deoxyribose phosphodiesterase activities. Escherichia coli ExoIII is an active AP endonuclease, and in addition, it exhibits double strand (ds)-specific 3'-5' exonuclease, exonucleolytic RNase H, 3'-phosphomonoesterase and 3'-phosphodiesterase activities, all catalyzed by a single active site. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes ExoIII and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197320 [Multi-domain]  Cd Length: 254  Bit Score: 38.65  E-value: 3.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336032625 306 LDYIWLSPELARRnaarlpeIIRAGqpyrtifpagqeVERYPRtGWDRPkaSDHCPVVMTL 366
Cdd:cd09086  216 IDHILASPALADR-------LKDVG------------IDREPR-GWEKP--SDHAPVVAEL 254
 
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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