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Conserved domains on  [gi|518694670|ref|WP_019856363|]
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deoxyribonuclease IV [Actinopolyspora mortivallis]

Protein Classification

apurinic/apyrimidinic endonuclease family protein( domain architecture ID 581065)

apurinic/apyrimidinic (AP) endonuclease family protein may function as an endonuclease, isomerase, epimerase or dehydratase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01060 PRK01060
endonuclease IV; Provisional
1-251 1.52e-92

endonuclease IV; Provisional


:

Pssm-ID: 179214  Cd Length: 281  Bit Score: 273.60  E-value: 1.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   1 MQIGAHVR----DDDPLAAAAELDAEVVQFFLSDPQGWKAP--------QPHPRAAELKDSEVRVFVHSPYVINVASLNN 68
Cdd:PRK01060   2 KLIGAHVSaaggLEGAVAEAAEIGANAFMIFTGNPQQWKRKpleelnieAFKAACEKYGISPEDILVHAPYLINLGNPNK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  69 RIRIPSRKAVLQQVAAAAEVGAEGVVVHGGHVTKNDDPAEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDD 148
Cdd:PRK01060  82 EILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEALDKTQG-VTIVLENTAGQGSELGRRFEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 149 LARLWDAVGEFG-AGFCLDTCHAHSAGEDLV----GIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPE 221
Cdd:PRK01060 161 LARIIDGVEDKSrVGVCLDTCHAFAAGYDLRedfeGVLAEFDRIVGldRLKVMHLNDSKNEFGSRKDRHANLGEGTIGFD 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 518694670 222 VLREVC---ATANAPVVLETP--PEGQAEDIAYLR 251
Cdd:PRK01060 241 ALRYIVhdpRFDGIPKILETPyvGEIWKEEIAMLR 275
 
Name Accession Description Interval E-value
PRK01060 PRK01060
endonuclease IV; Provisional
1-251 1.52e-92

endonuclease IV; Provisional


Pssm-ID: 179214  Cd Length: 281  Bit Score: 273.60  E-value: 1.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   1 MQIGAHVR----DDDPLAAAAELDAEVVQFFLSDPQGWKAP--------QPHPRAAELKDSEVRVFVHSPYVINVASLNN 68
Cdd:PRK01060   2 KLIGAHVSaaggLEGAVAEAAEIGANAFMIFTGNPQQWKRKpleelnieAFKAACEKYGISPEDILVHAPYLINLGNPNK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  69 RIRIPSRKAVLQQVAAAAEVGAEGVVVHGGHVTKNDDPAEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDD 148
Cdd:PRK01060  82 EILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEALDKTQG-VTIVLENTAGQGSELGRRFEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 149 LARLWDAVGEFG-AGFCLDTCHAHSAGEDLV----GIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPE 221
Cdd:PRK01060 161 LARIIDGVEDKSrVGVCLDTCHAFAAGYDLRedfeGVLAEFDRIVGldRLKVMHLNDSKNEFGSRKDRHANLGEGTIGFD 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 518694670 222 VLREVC---ATANAPVVLETP--PEGQAEDIAYLR 251
Cdd:PRK01060 241 ALRYIVhdpRFDGIPKILETPyvGEIWKEEIAMLR 275
Nfo COG0648
Endonuclease IV [Replication, recombination and repair];
23-251 9.56e-67

Endonuclease IV [Replication, recombination and repair];


Pssm-ID: 440413  Cd Length: 280  Bit Score: 208.05  E-value: 9.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  23 VVQFFLSDPQGWKAPQPHPRAAE-----LKDSEVR-VFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVH 96
Cdd:COG0648   28 AFQIFTKNPRGWKAKPLDEEDIEafreaMEEHGIGpVVVHAPYLINLASPKPELREKSVAALRDELERCEALGAKYLVFH 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  97 GGHVTKnDDPAEGVANWRKLFERQQQEGGFEVPVLIENTAGGANAMARGFDDLARLWDAVGEFG-AGFCLDTCHAHSAGE 175
Cdd:COG0648  108 PGSHVG-AGEEAGIARIAEALNEVLEETPGGVTILLENTAGQGTELGRTFEELAAIIDRVEDKErVGVCLDTCHAFAAGY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 176 DLV------GIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPEVLREVC---ATANAPVVLETP--PEG 242
Cdd:COG0648  187 DLRtpegydGVLDEFDRIIGldRLKVIHLNDSKNPLGSRKDRHAHIGEGEIGLEAFRRLVndpRLAGIPFILETPkeDPG 266

                 ....*....
gi 518694670 243 QAEDIAYLR 251
Cdd:COG0648  267 YAEEIALLR 275
AP2Ec smart00518
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
23-251 1.28e-50

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: 166.71  E-value: 1.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670    23 VVQFFLSDPQGWKAPQPHPRAAE-----LKDSEVRVFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVHG 97
Cdd:smart00518  26 SFQLFLGNPRSWKGVRLSEETAEkfkeaLKENNIDVSVHAPYLINLASPDKEKVEKSIERLIDEIKRCEELGIKALVFHP 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670    98 GHVTKNDDPaEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDDLARLWDAVGEF-GAGFCLDTCHAHSAG-- 174
Cdd:smart00518 106 GSYLKQSKE-EALNRIIESLNEVIDETKG-VVILLETTAGKGSQIGSTFEDLKEIIDLIKELdRIGVCIDTCHIFAAGyd 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   175 ----EDLVGIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPEVLREVCA---TANAPVVLETP--PEGQ 243
Cdd:smart00518 184 intvEGFEKVLEEFENVLGleYLKAIHLNDSKIELGSGKDRHENLGEGYIGFEPFRLLMAdkrFDGIPLILETPpgPEMY 263

                   ....*...
gi 518694670   244 AEDIAYLR 251
Cdd:smart00518 264 EKEIALLK 271
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
23-251 8.72e-40

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: 138.61  E-value: 8.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  23 VVQFFLSDPQGWKAPQPHP------RAAELKDSEVRVFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVH 96
Cdd:cd00019   26 TVAMFLGNPRSWLSRPLKKeraekfKAIAEEGPSICLSVHAPYLINLASPDKEKREKSIERLKDEIERCEELGIRLLVFH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  97 GGHVTKNDDPaEGVANWRK-LFERQQQEGGFEVPVLIENTAGGANAMARGFDDLARLWDAVGEF-GAGFCLDTCHAHSAG 174
Cdd:cd00019  106 PGSYLGQSKE-EGLKRVIEaLNELIDKAETKGVVIALETMAGQGNEIGSSFEELKEIIDLIKEKpRVGVCIDTCHIFAAG 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 175 ------EDLVGIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDP-EVLREVCATA--NAPVVLETPPEGQ 243
Cdd:cd00019  185 ydistvEGFEKVLEEFDKVIGleYLKAIHLNDSKGELGSGKDRHEPIGEGDIDGeELFKELKKDPyqNIPLILETPSENR 264
                        250
                 ....*....|...
gi 518694670 244 -----AEDIAYLR 251
Cdd:cd00019  265 daakiKKEIKLLR 277
nfo TIGR00587
apurinic endonuclease (APN1); All proteins in this family for which functions are known are 5' ...
23-250 6.07e-25

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: 99.74  E-value: 6.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   23 VVQFFLSDPQGWKAPQP--------HPRAAELKDSEVRVFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVV 94
Cdd:TIGR00587  27 AFMFFLKSPRWWRRPMLeeevidwfKAALETNKNLSQIVLVHAPYLINLASPDEEKEEKSLDVLDEELKRCELLGIMLYN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   95 VHGGHVTKNDDpAEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDDLARLWDA-VGEFGAGFCLDTCHAHSA 173
Cdd:TIGR00587 107 FHPGSALKCSE-EEGLDNLIESLNVVIKETKI-VTILLENMAGQGSELGRSFEELAYIIKViVDKRRIGVCLDTCHFFAA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  174 G------EDLVGIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPEVLREVCA---TANAPVVLETP--P 240
Cdd:TIGR00587 185 GydittkAYFEVVKNEFDVVVGfkYLKAIHLNDSKNVLGSRKDRHENIGEGIIGFDAFRLIMDderFKGIPIILETPenP 264
                         250
                  ....*....|
gi 518694670  241 EGQAEDIAYL 250
Cdd:TIGR00587 265 KYYEEEIEML 274
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
43-248 1.68e-21

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: 89.74  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   43 AAELKDSEVRVFVHSPYVI-NVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVHGGHVTkNDDPAEG----VANWRKLF 117
Cdd:pfam01261  33 KAALKEHGLEIVVHAPYLGdNLASPDEEEREKAIDRLKRAIELAAALGAKLVVFHPGSDL-GDDPEEAlarlAESLRELA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  118 ERQQQEGgfeVPVLIENTAGGANAMARGFDDLARLWDAVGEFGAGFCLDTCHAHSAGEDlvgivERVRSITG--RLDLVH 195
Cdd:pfam01261 112 DLAEREG---VRLALEPLAGKGTNVGNTFEEALEIIDEVDSPNVGVCLDTGHLFAAGDG-----DLFELRLGdrYIGHVH 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518694670  196 LNNSRDGFGSRRDRHANIGSGSID-PEVLREVCATA-NAPVVLETPPEGQAEDIA 248
Cdd:pfam01261 184 LKDSKNPLGSGPDRHVPIGEGVIDfEALFRALKEIGyDGPLSLETFNDGPPEEGA 238
 
Name Accession Description Interval E-value
PRK01060 PRK01060
endonuclease IV; Provisional
1-251 1.52e-92

endonuclease IV; Provisional


Pssm-ID: 179214  Cd Length: 281  Bit Score: 273.60  E-value: 1.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   1 MQIGAHVR----DDDPLAAAAELDAEVVQFFLSDPQGWKAP--------QPHPRAAELKDSEVRVFVHSPYVINVASLNN 68
Cdd:PRK01060   2 KLIGAHVSaaggLEGAVAEAAEIGANAFMIFTGNPQQWKRKpleelnieAFKAACEKYGISPEDILVHAPYLINLGNPNK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  69 RIRIPSRKAVLQQVAAAAEVGAEGVVVHGGHVTKNDDPAEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDD 148
Cdd:PRK01060  82 EILEKSRDFLIQEIERCAALGAKLLVFHPGSHLGDIDEEDCLARIAESLNEALDKTQG-VTIVLENTAGQGSELGRRFEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 149 LARLWDAVGEFG-AGFCLDTCHAHSAGEDLV----GIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPE 221
Cdd:PRK01060 161 LARIIDGVEDKSrVGVCLDTCHAFAAGYDLRedfeGVLAEFDRIVGldRLKVMHLNDSKNEFGSRKDRHANLGEGTIGFD 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 518694670 222 VLREVC---ATANAPVVLETP--PEGQAEDIAYLR 251
Cdd:PRK01060 241 ALRYIVhdpRFDGIPKILETPyvGEIWKEEIAMLR 275
Nfo COG0648
Endonuclease IV [Replication, recombination and repair];
23-251 9.56e-67

Endonuclease IV [Replication, recombination and repair];


Pssm-ID: 440413  Cd Length: 280  Bit Score: 208.05  E-value: 9.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  23 VVQFFLSDPQGWKAPQPHPRAAE-----LKDSEVR-VFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVH 96
Cdd:COG0648   28 AFQIFTKNPRGWKAKPLDEEDIEafreaMEEHGIGpVVVHAPYLINLASPKPELREKSVAALRDELERCEALGAKYLVFH 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  97 GGHVTKnDDPAEGVANWRKLFERQQQEGGFEVPVLIENTAGGANAMARGFDDLARLWDAVGEFG-AGFCLDTCHAHSAGE 175
Cdd:COG0648  108 PGSHVG-AGEEAGIARIAEALNEVLEETPGGVTILLENTAGQGTELGRTFEELAAIIDRVEDKErVGVCLDTCHAFAAGY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 176 DLV------GIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPEVLREVC---ATANAPVVLETP--PEG 242
Cdd:COG0648  187 DLRtpegydGVLDEFDRIIGldRLKVIHLNDSKNPLGSRKDRHAHIGEGEIGLEAFRRLVndpRLAGIPFILETPkeDPG 266

                 ....*....
gi 518694670 243 QAEDIAYLR 251
Cdd:COG0648  267 YAEEIALLR 275
AP2Ec smart00518
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
23-251 1.28e-50

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: 166.71  E-value: 1.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670    23 VVQFFLSDPQGWKAPQPHPRAAE-----LKDSEVRVFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVHG 97
Cdd:smart00518  26 SFQLFLGNPRSWKGVRLSEETAEkfkeaLKENNIDVSVHAPYLINLASPDKEKVEKSIERLIDEIKRCEELGIKALVFHP 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670    98 GHVTKNDDPaEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDDLARLWDAVGEF-GAGFCLDTCHAHSAG-- 174
Cdd:smart00518 106 GSYLKQSKE-EALNRIIESLNEVIDETKG-VVILLETTAGKGSQIGSTFEDLKEIIDLIKELdRIGVCIDTCHIFAAGyd 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   175 ----EDLVGIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPEVLREVCA---TANAPVVLETP--PEGQ 243
Cdd:smart00518 184 intvEGFEKVLEEFENVLGleYLKAIHLNDSKIELGSGKDRHENLGEGYIGFEPFRLLMAdkrFDGIPLILETPpgPEMY 263

                   ....*...
gi 518694670   244 AEDIAYLR 251
Cdd:smart00518 264 EKEIALLK 271
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
23-251 8.72e-40

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: 138.61  E-value: 8.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  23 VVQFFLSDPQGWKAPQPHP------RAAELKDSEVRVFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVH 96
Cdd:cd00019   26 TVAMFLGNPRSWLSRPLKKeraekfKAIAEEGPSICLSVHAPYLINLASPDKEKREKSIERLKDEIERCEELGIRLLVFH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  97 GGHVTKNDDPaEGVANWRK-LFERQQQEGGFEVPVLIENTAGGANAMARGFDDLARLWDAVGEF-GAGFCLDTCHAHSAG 174
Cdd:cd00019  106 PGSYLGQSKE-EGLKRVIEaLNELIDKAETKGVVIALETMAGQGNEIGSSFEELKEIIDLIKEKpRVGVCIDTCHIFAAG 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 175 ------EDLVGIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDP-EVLREVCATA--NAPVVLETPPEGQ 243
Cdd:cd00019  185 ydistvEGFEKVLEEFDKVIGleYLKAIHLNDSKGELGSGKDRHEPIGEGDIDGeELFKELKKDPyqNIPLILETPSENR 264
                        250
                 ....*....|...
gi 518694670 244 -----AEDIAYLR 251
Cdd:cd00019  265 daakiKKEIKLLR 277
nfo TIGR00587
apurinic endonuclease (APN1); All proteins in this family for which functions are known are 5' ...
23-250 6.07e-25

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: 99.74  E-value: 6.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   23 VVQFFLSDPQGWKAPQP--------HPRAAELKDSEVRVFVHSPYVINVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVV 94
Cdd:TIGR00587  27 AFMFFLKSPRWWRRPMLeeevidwfKAALETNKNLSQIVLVHAPYLINLASPDEEKEEKSLDVLDEELKRCELLGIMLYN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   95 VHGGHVTKNDDpAEGVANWRKLFERQQQEGGFeVPVLIENTAGGANAMARGFDDLARLWDA-VGEFGAGFCLDTCHAHSA 173
Cdd:TIGR00587 107 FHPGSALKCSE-EEGLDNLIESLNVVIKETKI-VTILLENMAGQGSELGRSFEELAYIIKViVDKRRIGVCLDTCHFFAA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  174 G------EDLVGIVERVRSITG--RLDLVHLNNSRDGFGSRRDRHANIGSGSIDPEVLREVCA---TANAPVVLETP--P 240
Cdd:TIGR00587 185 GydittkAYFEVVKNEFDVVVGfkYLKAIHLNDSKNVLGSRKDRHENIGEGIIGFDAFRLIMDderFKGIPIILETPenP 264
                         250
                  ....*....|
gi 518694670  241 EGQAEDIAYL 250
Cdd:TIGR00587 265 KYYEEEIEML 274
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
43-248 1.68e-21

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: 89.74  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670   43 AAELKDSEVRVFVHSPYVI-NVASLNNRIRIPSRKAVLQQVAAAAEVGAEGVVVHGGHVTkNDDPAEG----VANWRKLF 117
Cdd:pfam01261  33 KAALKEHGLEIVVHAPYLGdNLASPDEEEREKAIDRLKRAIELAAALGAKLVVFHPGSDL-GDDPEEAlarlAESLRELA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  118 ERQQQEGgfeVPVLIENTAGGANAMARGFDDLARLWDAVGEFGAGFCLDTCHAHSAGEDlvgivERVRSITG--RLDLVH 195
Cdd:pfam01261 112 DLAEREG---VRLALEPLAGKGTNVGNTFEEALEIIDEVDSPNVGVCLDTGHLFAAGDG-----DLFELRLGdrYIGHVH 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518694670  196 LNNSRDGFGSRRDRHANIGSGSID-PEVLREVCATA-NAPVVLETPPEGQAEDIA 248
Cdd:pfam01261 184 LKDSKNPLGSGPDRHVPIGEGVIDfEALFRALKEIGyDGPLSLETFNDGPPEEGA 238
PTZ00372 PTZ00372
endonuclease 4-like protein; Provisional
128-239 5.13e-16

endonuclease 4-like protein; Provisional


Pssm-ID: 240388  Cd Length: 413  Bit Score: 76.68  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 128 VPVLIENTAGGANAMARGFDDLARLWDAVGEFG-AGFCLDTCHAHSAGEDLV------GIVERVRSITG--RLDLVHLNN 198
Cdd:PTZ00372 269 VIIVLENTAGQKNSVGSKFEDLRDIIALVEDKSrVGVCLDTCHLFAAGYDIRtkesfdKVMKEFDEIVGlkYLKAVHLND 348
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 518694670 199 SRDGFGSRRDRHANIGSGSIDPEVLREVCATA---NAPVVLETP 239
Cdd:PTZ00372 349 SKSDLGSGLDRHENIGKGKLGMETFKFIMNSKyfkNIPIILETP 392
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
96-251 7.83e-13

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 66.19  E-value: 7.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670  96 HGGHVTKNDDPAEG-----VANWRKLFERQQQEGgfeVPVLIENTAGGanaMARGFDDLARLWDAVGEFGAGFCLDTCHA 170
Cdd:COG1082   98 HPGSPPPPDLPPEEawdrlAERLRELAELAEEAG---VTLALENHEGT---FVNTPEEALRLLEAVDSPNVGLLLDTGHA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518694670 171 HSAGEDLVGIVERVRsitGRLDLVHLNNsrdgfgSRRDRHANIGSGSID-PEVLREVCATA-NAPVVLE------TPPEG 242
Cdd:COG1082  172 LLAGEDPVELLRKLG---DRIKHVHLKD------ADGDQHLPPGEGDIDfAAILRALKEAGyDGWLSLEvesdpdDPEEA 242

                 ....*....
gi 518694670 243 QAEDIAYLR 251
Cdd:COG1082  243 ARESLEYLR 251
 
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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