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Conserved domains on  [gi|502434158|ref|WP_012784587|]
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deoxyribonuclease IV [Catenulispora acidiphila]

Protein Classification

deoxyribonuclease IV( domain architecture ID 10011614)

deoxyribonuclease IV cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues

CATH:  3.20.20.150
EC:  3.1.21.2
PubMed:  10458614|21358045
SCOP:  4003294

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01060 PRK01060
endonuclease IV; Provisional
3-261 5.01e-109

endonuclease IV; Provisional


:

Pssm-ID: 179214  Cd Length: 281  Bit Score: 315.97  E-value: 5.01e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   3 MRIGSHV----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVaYPGGASALRAAAEQADVA---VYVHAAYIINVAATN 75
Cdd:PRK01060   2 KLIGAHVsaagGLEGAVAEAAEIGANAFMIFTGNPQQWKRKPL-EELNIEAFKAACEKYGISpedILVHAPYLINLGNPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  76 NRIRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADAPDAGFDNWRKAVDQL---EQHCPVFIENTAGGDHAMARRIDA 152
Cdd:PRK01060  81 KEILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEAldkTQGVTIVLENTAGQGSELGRRFEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 153 IAKLWDAVGH-SGIGLCLDTCHAFAGGIPL----ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIAPA 225
Cdd:PRK01060 161 LARIIDGVEDkSRVGVCLDTCHAFAAGYDLredfEGVLAEFDRIVGldRLKVMHLNDSKNEFGSRKDRHANLGEGTIGFD 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502434158 226 DL--IAQVIAEAGCPAICETPGGAEAQAADIKWLRERV 261
Cdd:PRK01060 241 ALryIVHDPRFDGIPKILETPYVGEIWKEEIAMLREQQ 278
 
Name Accession Description Interval E-value
PRK01060 PRK01060
endonuclease IV; Provisional
3-261 5.01e-109

endonuclease IV; Provisional


Pssm-ID: 179214  Cd Length: 281  Bit Score: 315.97  E-value: 5.01e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   3 MRIGSHV----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVaYPGGASALRAAAEQADVA---VYVHAAYIINVAATN 75
Cdd:PRK01060   2 KLIGAHVsaagGLEGAVAEAAEIGANAFMIFTGNPQQWKRKPL-EELNIEAFKAACEKYGISpedILVHAPYLINLGNPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  76 NRIRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADAPDAGFDNWRKAVDQL---EQHCPVFIENTAGGDHAMARRIDA 152
Cdd:PRK01060  81 KEILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEAldkTQGVTIVLENTAGQGSELGRRFEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 153 IAKLWDAVGH-SGIGLCLDTCHAFAGGIPL----ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIAPA 225
Cdd:PRK01060 161 LARIIDGVEDkSRVGVCLDTCHAFAAGYDLredfEGVLAEFDRIVGldRLKVMHLNDSKNEFGSRKDRHANLGEGTIGFD 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502434158 226 DL--IAQVIAEAGCPAICETPGGAEAQAADIKWLRERV 261
Cdd:PRK01060 241 ALryIVHDPRFDGIPKILETPYVGEIWKEEIAMLREQQ 278
Nfo COG0648
Endonuclease IV [Replication, recombination and repair];
3-262 3.23e-89

Endonuclease IV [Replication, recombination and repair];


Pssm-ID: 440413  Cd Length: 280  Bit Score: 265.83  E-value: 3.23e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   3 MRIGSHV----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVAYPGgASALRAAAEQADVA-VYVHAAYIINVAATNNR 77
Cdd:COG0648    2 MLIGAHVsiagGLLNAVERAAEIGANAFQIFTKNPRGWKAKPLDEED-IEAFREAMEEHGIGpVVVHAPYLINLASPKPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  78 IRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADaPDAGFDNWRKAVDQL----EQHCPVFIENTAGGDHAMARRIDAI 153
Cdd:COG0648   81 LREKSVAALRDELERCEALGAKYLVFHPGSHVGAG-EEAGIARIAEALNEVleetPGGVTILLENTAGQGTELGRTFEEL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 154 AKLWDAVGHSG-IGLCLDTCHAFAGGIPLESA------VADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIaP 224
Cdd:COG0648  160 AAIIDRVEDKErVGVCLDTCHAFAAGYDLRTPegydgvLDEFDRIIGldRLKVIHLNDSKNPLGSRKDRHAHIGEGEI-G 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 502434158 225 ADLIAQVIAE---AGCPAICETPGGAEAQAADIKWLRERVA 262
Cdd:COG0648  239 LEAFRRLVNDprlAGIPFILETPKEDPGYAEEIALLRELLG 279
AP2Ec smart00518
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
5-259 2.46e-64

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites


Pssm-ID: 214707  Cd Length: 273  Bit Score: 202.15  E-value: 2.46e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158     5 IGSHVGNEDPIA----EAVARGADAVQIFLGDPQSWKAPTVAyPGGASALRAAAEQADVAVYVHAAYIINVAATNNRIRI 80
Cdd:smart00518   2 IGAHVSAAGGLYkafiEAVDIGARSFQLFLGNPRSWKGVRLS-EETAEKFKEALKENNIDVSVHAPYLINLASPDKEKVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158    81 PSRKLLQQTVALAAEAGARGVVVHGGhSTAADAPDAGFDNWRKAVDQL---EQHCPVFIENTAGGDHAMARRIDAIAKLW 157
Cdd:smart00518  81 KSIERLIDEIKRCEELGIKALVFHPG-SYLKQSKEEALNRIIESLNEVideTKGVVILLETTAGKGSQIGSTFEDLKEII 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   158 DAVG-HSGIGLCLDTCHAFAGGIPL------ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEI--APAD 226
Cdd:smart00518 160 DLIKeLDRIGVCIDTCHIFAAGYDIntvegfEKVLEEFENVLGleYLKAIHLNDSKIELGSGKDRHENLGEGYIgfEPFR 239
                          250       260       270
                   ....*....|....*....|....*....|...
gi 502434158   227 LIAQVIAEAGCPAICETPGGAEAQAADIKWLRE 259
Cdd:smart00518 240 LLMADKRFDGIPLILETPPGPEMYEKEIALLKE 272
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
5-260 4.65e-54

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 175.97  E-value: 4.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   5 IGSHV-----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVAyPGGASALRAAAEQ-ADVAVYVHAAYIINVAATNNRI 78
Cdd:cd00019    1 IGAHVsaagfGLENALKRAKEIGFDTVAMFLGNPRSWLSRPLK-KERAEKFKAIAEEgPSICLSVHAPYLINLASPDKEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  79 RIPSRKLLQQTVALAAEAGARGVVVHGGhSTAADAPDAGFDNWRKAVDQL-----EQHCPVFIENTAGGDHAMARRIDAI 153
Cdd:cd00019   80 REKSIERLKDEIERCEELGIRLLVFHPG-SYLGQSKEEGLKRVIEALNELidkaeTKGVVIALETMAGQGNEIGSSFEEL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 154 AKLWDAVGHS-GIGLCLDTCHAFAGG------IPLESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIAP 224
Cdd:cd00019  159 KEIIDLIKEKpRVGVCIDTCHIFAAGydistvEGFEKVLEEFDKVIGleYLKAIHLNDSKGELGSGKDRHEPIGEGDIDG 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 502434158 225 ADLIAQVIAEA--GCPAICETPGGAEAQAA---DIKWLRER 260
Cdd:cd00019  239 EELFKELKKDPyqNIPLILETPSENRDAAKikkEIKLLRKL 279
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
15-260 4.40e-36

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 128.64  E-value: 4.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   15 IAEAVARGADAVQIFLGDPQSWKAptvaYPGGASALRAAAEQADVAVYVHAAYII-NVAATNNRIRIPSRKLLQQTVALA 93
Cdd:pfam01261   1 LAAAAELGFDGVELFTRRWFRPPL----SDEEAEELKAALKEHGLEIVVHAPYLGdNLASPDEEEREKAIDRLKRAIELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   94 AEAGARGVVVHGGHSTAADaPDAGFDNWRKAVDQLEQHC-----PVFIENTAGGDHAMARRIDAIAKLWDAVGHSGIGLC 168
Cdd:pfam01261  77 AALGAKLVVFHPGSDLGDD-PEEALARLAESLRELADLAeregvRLALEPLAGKGTNVGNTFEEALEIIDEVDSPNVGVC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  169 LDTCHAF-AGGIPLESAVADIKavtgRVDLVHANDSQGGFDSGIDRHANFGSGEIaPADLIAQVIAEAG--CPAICETPG 245
Cdd:pfam01261 156 LDTGHLFaAGDGDLFELRLGDR----YIGHVHLKDSKNPLGSGPDRHVPIGEGVI-DFEALFRALKEIGydGPLSLETFN 230
                         250
                  ....*....|....*...
gi 502434158  246 ---GAEAQAADIKWLRER 260
Cdd:pfam01261 231 dgpPEEGAREGLEWLREL 248
nfo TIGR00587
apurinic endonuclease (APN1); All proteins in this family for which functions are known are 5' ...
3-257 1.15e-28

apurinic endonuclease (APN1); All proteins in this family for which functions are known are 5' AP endonculeases that are used in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273156  Cd Length: 274  Bit Score: 109.75  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158    3 MRIGSHVGNEDPIA----EAVARGADAVQIFLGDPQSWKAPTVAyPGGASALRAAAEQ---ADVAVYVHAAYIINVAATN 75
Cdd:TIGR00587   1 KLLGAHVSAAGGLQaaynRAAEIGATAFMFFLKSPRWWRRPMLE-EEVIDWFKAALETnknLSQIVLVHAPYLINLASPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   76 NRIRIPSRKLLQQTVALAAEAGARGVVVHGGhSTAADAPDAGFDNWRKAVDQ---LEQHCPVFIENTAGGDHAMARRIDA 152
Cdd:TIGR00587  80 EEKEEKSLDVLDEELKRCELLGIMLYNFHPG-SALKCSEEEGLDNLIESLNVvikETKIVTILLENMAGQGSELGRSFEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  153 IAKLWDA-VGHSGIGLCLDTCHAFAGGIPL------ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEI- 222
Cdd:TIGR00587 159 LAYIIKViVDKRRIGVCLDTCHFFAAGYDIttkayfEVVKNEFDVVVGfkYLKAIHLNDSKNVLGSRKDRHENIGEGIIg 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 502434158  223 -APADLIAQVIAEAGCPAICETPGGAEAQAADIKWL 257
Cdd:TIGR00587 239 fDAFRLIMDDERFKGIPIILETPENPKYYEEEIEML 274
 
Name Accession Description Interval E-value
PRK01060 PRK01060
endonuclease IV; Provisional
3-261 5.01e-109

endonuclease IV; Provisional


Pssm-ID: 179214  Cd Length: 281  Bit Score: 315.97  E-value: 5.01e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   3 MRIGSHV----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVaYPGGASALRAAAEQADVA---VYVHAAYIINVAATN 75
Cdd:PRK01060   2 KLIGAHVsaagGLEGAVAEAAEIGANAFMIFTGNPQQWKRKPL-EELNIEAFKAACEKYGISpedILVHAPYLINLGNPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  76 NRIRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADAPDAGFDNWRKAVDQL---EQHCPVFIENTAGGDHAMARRIDA 152
Cdd:PRK01060  81 KEILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEAldkTQGVTIVLENTAGQGSELGRRFEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 153 IAKLWDAVGH-SGIGLCLDTCHAFAGGIPL----ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIAPA 225
Cdd:PRK01060 161 LARIIDGVEDkSRVGVCLDTCHAFAAGYDLredfEGVLAEFDRIVGldRLKVMHLNDSKNEFGSRKDRHANLGEGTIGFD 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502434158 226 DL--IAQVIAEAGCPAICETPGGAEAQAADIKWLRERV 261
Cdd:PRK01060 241 ALryIVHDPRFDGIPKILETPYVGEIWKEEIAMLREQQ 278
Nfo COG0648
Endonuclease IV [Replication, recombination and repair];
3-262 3.23e-89

Endonuclease IV [Replication, recombination and repair];


Pssm-ID: 440413  Cd Length: 280  Bit Score: 265.83  E-value: 3.23e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   3 MRIGSHV----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVAYPGgASALRAAAEQADVA-VYVHAAYIINVAATNNR 77
Cdd:COG0648    2 MLIGAHVsiagGLLNAVERAAEIGANAFQIFTKNPRGWKAKPLDEED-IEAFREAMEEHGIGpVVVHAPYLINLASPKPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  78 IRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADaPDAGFDNWRKAVDQL----EQHCPVFIENTAGGDHAMARRIDAI 153
Cdd:COG0648   81 LREKSVAALRDELERCEALGAKYLVFHPGSHVGAG-EEAGIARIAEALNEVleetPGGVTILLENTAGQGTELGRTFEEL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 154 AKLWDAVGHSG-IGLCLDTCHAFAGGIPLESA------VADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIaP 224
Cdd:COG0648  160 AAIIDRVEDKErVGVCLDTCHAFAAGYDLRTPegydgvLDEFDRIIGldRLKVIHLNDSKNPLGSRKDRHAHIGEGEI-G 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 502434158 225 ADLIAQVIAE---AGCPAICETPGGAEAQAADIKWLRERVA 262
Cdd:COG0648  239 LEAFRRLVNDprlAGIPFILETPKEDPGYAEEIALLRELLG 279
AP2Ec smart00518
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
5-259 2.46e-64

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites


Pssm-ID: 214707  Cd Length: 273  Bit Score: 202.15  E-value: 2.46e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158     5 IGSHVGNEDPIA----EAVARGADAVQIFLGDPQSWKAPTVAyPGGASALRAAAEQADVAVYVHAAYIINVAATNNRIRI 80
Cdd:smart00518   2 IGAHVSAAGGLYkafiEAVDIGARSFQLFLGNPRSWKGVRLS-EETAEKFKEALKENNIDVSVHAPYLINLASPDKEKVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158    81 PSRKLLQQTVALAAEAGARGVVVHGGhSTAADAPDAGFDNWRKAVDQL---EQHCPVFIENTAGGDHAMARRIDAIAKLW 157
Cdd:smart00518  81 KSIERLIDEIKRCEELGIKALVFHPG-SYLKQSKEEALNRIIESLNEVideTKGVVILLETTAGKGSQIGSTFEDLKEII 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   158 DAVG-HSGIGLCLDTCHAFAGGIPL------ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEI--APAD 226
Cdd:smart00518 160 DLIKeLDRIGVCIDTCHIFAAGYDIntvegfEKVLEEFENVLGleYLKAIHLNDSKIELGSGKDRHENLGEGYIgfEPFR 239
                          250       260       270
                   ....*....|....*....|....*....|...
gi 502434158   227 LIAQVIAEAGCPAICETPGGAEAQAADIKWLRE 259
Cdd:smart00518 240 LLMADKRFDGIPLILETPPGPEMYEKEIALLKE 272
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
5-260 4.65e-54

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 175.97  E-value: 4.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   5 IGSHV-----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVAyPGGASALRAAAEQ-ADVAVYVHAAYIINVAATNNRI 78
Cdd:cd00019    1 IGAHVsaagfGLENALKRAKEIGFDTVAMFLGNPRSWLSRPLK-KERAEKFKAIAEEgPSICLSVHAPYLINLASPDKEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  79 RIPSRKLLQQTVALAAEAGARGVVVHGGhSTAADAPDAGFDNWRKAVDQL-----EQHCPVFIENTAGGDHAMARRIDAI 153
Cdd:cd00019   80 REKSIERLKDEIERCEELGIRLLVFHPG-SYLGQSKEEGLKRVIEALNELidkaeTKGVVIALETMAGQGNEIGSSFEEL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 154 AKLWDAVGHS-GIGLCLDTCHAFAGG------IPLESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEIAP 224
Cdd:cd00019  159 KEIIDLIKEKpRVGVCIDTCHIFAAGydistvEGFEKVLEEFDKVIGleYLKAIHLNDSKGELGSGKDRHEPIGEGDIDG 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 502434158 225 ADLIAQVIAEA--GCPAICETPGGAEAQAA---DIKWLRER 260
Cdd:cd00019  239 EELFKELKKDPyqNIPLILETPSENRDAAKikkEIKLLRKL 279
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
15-260 4.40e-36

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 128.64  E-value: 4.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   15 IAEAVARGADAVQIFLGDPQSWKAptvaYPGGASALRAAAEQADVAVYVHAAYII-NVAATNNRIRIPSRKLLQQTVALA 93
Cdd:pfam01261   1 LAAAAELGFDGVELFTRRWFRPPL----SDEEAEELKAALKEHGLEIVVHAPYLGdNLASPDEEEREKAIDRLKRAIELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   94 AEAGARGVVVHGGHSTAADaPDAGFDNWRKAVDQLEQHC-----PVFIENTAGGDHAMARRIDAIAKLWDAVGHSGIGLC 168
Cdd:pfam01261  77 AALGAKLVVFHPGSDLGDD-PEEALARLAESLRELADLAeregvRLALEPLAGKGTNVGNTFEEALEIIDEVDSPNVGVC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  169 LDTCHAF-AGGIPLESAVADIKavtgRVDLVHANDSQGGFDSGIDRHANFGSGEIaPADLIAQVIAEAG--CPAICETPG 245
Cdd:pfam01261 156 LDTGHLFaAGDGDLFELRLGDR----YIGHVHLKDSKNPLGSGPDRHVPIGEGVI-DFEALFRALKEIGydGPLSLETFN 230
                         250
                  ....*....|....*...
gi 502434158  246 ---GAEAQAADIKWLRER 260
Cdd:pfam01261 231 dgpPEEGAREGLEWLREL 248
nfo TIGR00587
apurinic endonuclease (APN1); All proteins in this family for which functions are known are 5' ...
3-257 1.15e-28

apurinic endonuclease (APN1); All proteins in this family for which functions are known are 5' AP endonculeases that are used in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273156  Cd Length: 274  Bit Score: 109.75  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158    3 MRIGSHVGNEDPIA----EAVARGADAVQIFLGDPQSWKAPTVAyPGGASALRAAAEQ---ADVAVYVHAAYIINVAATN 75
Cdd:TIGR00587   1 KLLGAHVSAAGGLQaaynRAAEIGATAFMFFLKSPRWWRRPMLE-EEVIDWFKAALETnknLSQIVLVHAPYLINLASPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   76 NRIRIPSRKLLQQTVALAAEAGARGVVVHGGhSTAADAPDAGFDNWRKAVDQ---LEQHCPVFIENTAGGDHAMARRIDA 152
Cdd:TIGR00587  80 EEKEEKSLDVLDEELKRCELLGIMLYNFHPG-SALKCSEEEGLDNLIESLNVvikETKIVTILLENMAGQGSELGRSFEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  153 IAKLWDA-VGHSGIGLCLDTCHAFAGGIPL------ESAVADIKAVTG--RVDLVHANDSQGGFDSGIDRHANFGSGEI- 222
Cdd:TIGR00587 159 LAYIIKViVDKRRIGVCLDTCHFFAAGYDIttkayfEVVKNEFDVVVGfkYLKAIHLNDSKNVLGSRKDRHENIGEGIIg 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 502434158  223 -APADLIAQVIAEAGCPAICETPGGAEAQAADIKWL 257
Cdd:TIGR00587 239 fDAFRLIMDDERFKGIPIILETPENPKYYEEEIEML 274
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
3-259 5.28e-20

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 86.22  E-value: 5.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   3 MRIG--SHVGNEDPIAEAVAR----GADAVQIFLGDPQswkaptvayPGGASALRAAAEQADVAVYVHAAYIINVAAtNN 76
Cdd:COG1082    1 MKLGlsTYSLPDLDLEEALRAaaelGYDGVELAGGDLD---------EADLAELRAALADHGLEISSLHAPGLNLAP-DP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  77 RIRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADAPDAGF-----DNWRKAVDQLEQH-CPVFIENTAGGdhaMARRI 150
Cdd:COG1082   71 EVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAwdrlaERLRELAELAEEAgVTLALENHEGT---FVNTP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 151 DAIAKLWDAVGHSGIGLCLDTCHAFAGGiplESAVADIKAVTGRVDLVHANDSQGgfdsgiDRHANFGSGEIAPADLIAQ 230
Cdd:COG1082  148 EEALRLLEAVDSPNVGLLLDTGHALLAG---EDPVELLRKLGDRIKHVHLKDADG------DQHLPPGEGDIDFAAILRA 218
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 502434158 231 ViAEAG--CPAICE----TPGGAEAQAADIKWLRE 259
Cdd:COG1082  219 L-KEAGydGWLSLEvesdPDDPEEAARESLEYLRK 252
PTZ00372 PTZ00372
endonuclease 4-like protein; Provisional
5-244 5.68e-17

endonuclease 4-like protein; Provisional


Pssm-ID: 240388  Cd Length: 413  Bit Score: 79.76  E-value: 5.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158   5 IGSHV----GNEDPIAEAVARGADAVQIFLGDPQSWKAPTVAypggasalRAAAEQ--ADVAVY--------VHAAYIIN 70
Cdd:PTZ00372 133 IGAHVsasgGVDNSPINAYNIAGQAFALFLKNQRTWNSPPLS--------DETIDKfkENCKKYnydpkfilPHGSYLIN 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158  71 VAATNNRIRIPSRKLLQQTVALAAEAGARGVVVHGGHSTAADAPDAGFDNWRKAVDQ-LEQHCPVFI--ENTAGGDHAMA 147
Cdd:PTZ00372 205 LANPDKEKREKSYDAFLDDLQRCEQLGIKLYNFHPGSTVGQCSKEEGIKNIADCINKaHEETKSVIIvlENTAGQKNSVG 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502434158 148 RRI----DAIAKLWDAvghSGIGLCLDTCHAFAGGIPL------ESAVADIKAVTGRVDL--VHANDSQGGFDSGIDRHA 215
Cdd:PTZ00372 285 SKFedlrDIIALVEDK---SRVGVCLDTCHLFAAGYDIrtkesfDKVMKEFDEIVGLKYLkaVHLNDSKSDLGSGLDRHE 361
                        250       260       270
                 ....*....|....*....|....*....|.
gi 502434158 216 NFGSGEI--APADLIAQVIAEAGCPAICETP 244
Cdd:PTZ00372 362 NIGKGKLgmETFKFIMNSKYFKNIPIILETP 392
 
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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