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Conserved domains on  [gi|645066016|ref|NP_001280125|]
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adenine DNA glycosylase isoform 8 [Homo sapiens]

Protein Classification

A/G-specific adenine glycosylase( domain architecture ID 11439777)

A/G-specific adenine glycosylase prevents DNA mutations by excising adenine (A) from the oxidatively damaged guanine (7,8-dihydro-8-oxoguanine or 7-oxoG):adenine base pair

EC:  3.2.2.-
Gene Ontology:  GO:0046872|GO:0000701|GO:0006284|GO:0051539
PubMed:  19778963|26673696

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 4-379 5.47e-144

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


:

Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 414.15  E-value: 5.47e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   4 DRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPR 83
Cdd:COG1194   26 TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  84 TAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAM 163
Cdd:COG1194  106 TYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALM 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 164 ELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKAS 243
Cdd:COG1194  185 DLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL-----------------------------------------PVKKP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 244 RKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVV 323
Cdd:COG1194  224 KKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVR 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 645066016 324 HTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVFRVYQG 379
Cdd:COG1194  297 HVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 4-379 5.47e-144

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 414.15  E-value: 5.47e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   4 DRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPR 83
Cdd:COG1194   26 TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  84 TAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAM 163
Cdd:COG1194  106 TYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALM 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 164 ELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKAS 243
Cdd:COG1194  185 DLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL-----------------------------------------PVKKP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 244 RKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVV 323
Cdd:COG1194  224 KKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVR 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 645066016 324 HTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVFRVYQG 379
Cdd:COG1194  297 HVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 3-305 2.48e-91

A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 130156  Cd Length: 275  Bit Score: 277.37  E-value: 2.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016    3 LDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMP 82
Cdd:TIGR01084  22 QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARARNLHKAAQEVVEEFGGEFP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   83 RTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAA 162
Cdd:TIGR01084 102 QDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWTLAESLLPKADPEAFNQAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  163 MELGATVCTPQRPLCSQCPVESLCRARQRVEQEQllasgslsgspdveecapntgqchlclppsepwdqtlgvvnFPRKA 242
Cdd:TIGR01084 181 MDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEE-----------------------------------------YPVKK 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 645066016  243 SRKPPREESSATCVLEQPgalGAQILLVQRPNSGLLAGLWEFPsvtwepseQLQRKALLQELQ 305
Cdd:TIGR01084 220 PKAAPPERTTYFLVLQNY---DGEVLLEQRPEKGLWGGLYCFP--------QFEDEDSLAFLL 271
PRK10880 PRK10880
adenine DNA glycosylase;
3-331 3.49e-68

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 220.35  E-value: 3.49e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   3 LDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMP 82
Cdd:PRK10880  26 IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  83 RTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQA 161
Cdd:PRK10880 106 ETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 162 AMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSlsgspdveecapntgqchlclppsepWDQtlgvvnFPRK 241
Cdd:PRK10880 184 MMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS--------------------------WAL------YPGK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 242 ASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEFPSVTWEpseqlqrkallQELQRW--AGPLPATHLRHL 319
Cdd:PRK10880 223 KPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCFPQFADE-----------EELRQWlaQRGIAADNLTQL 287

                        330
                 ....*....|..
gi 645066016 320 GEVVHTFSHIKL 331
Cdd:PRK10880 288 TAFRHTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 8-166 2.28e-47

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 238013 [Multi-domain]  Cd Length: 158  Bit Score: 159.71  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   8 YAVWVSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPR 83
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  84 TAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAM 163
Cdd:cd00056   81 AREELLA-LPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155


                 ...
gi 645066016 164 ELG 166
Cdd:cd00056  156 DLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 16-168 1.72e-43

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 214684 [Multi-domain]  Cd Length: 149  Bit Score: 149.34  E-value: 1.72e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016    16 MLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 94
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 645066016    95 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 168
Cdd:smart00478  80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 12-148 2.15e-41

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 143.58  E-value: 2.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   12 VSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 89
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 645066016   90 QLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 148
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 4-379 5.47e-144

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 414.15  E-value: 5.47e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   4 DRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPR 83
Cdd:COG1194   26 TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  84 TAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAM 163
Cdd:COG1194  106 TYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALM 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 164 ELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKAS 243
Cdd:COG1194  185 DLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL-----------------------------------------PVKKP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 244 RKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVV 323
Cdd:COG1194  224 KKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVR 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 645066016 324 HTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVFRVYQG 379
Cdd:COG1194  297 HVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 3-305 2.48e-91

A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 130156  Cd Length: 275  Bit Score: 277.37  E-value: 2.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016    3 LDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMP 82
Cdd:TIGR01084  22 QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARARNLHKAAQEVVEEFGGEFP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   83 RTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAA 162
Cdd:TIGR01084 102 QDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWTLAESLLPKADPEAFNQAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  163 MELGATVCTPQRPLCSQCPVESLCRARQRVEQEQllasgslsgspdveecapntgqchlclppsepwdqtlgvvnFPRKA 242
Cdd:TIGR01084 181 MDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEE-----------------------------------------YPVKK 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 645066016  243 SRKPPREESSATCVLEQPgalGAQILLVQRPNSGLLAGLWEFPsvtwepseQLQRKALLQELQ 305
Cdd:TIGR01084 220 PKAAPPERTTYFLVLQNY---DGEVLLEQRPEKGLWGGLYCFP--------QFEDEDSLAFLL 271
PRK10880 PRK10880
adenine DNA glycosylase;
3-331 3.49e-68

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 220.35  E-value: 3.49e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   3 LDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMP 82
Cdd:PRK10880  26 IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  83 RTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQA 161
Cdd:PRK10880 106 ETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 162 AMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSlsgspdveecapntgqchlclppsepWDQtlgvvnFPRK 241
Cdd:PRK10880 184 MMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS--------------------------WAL------YPGK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 242 ASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEFPSVTWEpseqlqrkallQELQRW--AGPLPATHLRHL 319
Cdd:PRK10880 223 KPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCFPQFADE-----------EELRQWlaQRGIAADNLTQL 287

                        330
                 ....*....|..
gi 645066016 320 GEVVHTFSHIKL 331
Cdd:PRK10880 288 TAFRHTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 8-166 2.28e-47

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 238013 [Multi-domain]  Cd Length: 158  Bit Score: 159.71  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   8 YAVWVSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPR 83
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  84 TAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAM 163
Cdd:cd00056   81 AREELLA-LPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155


                 ...
gi 645066016 164 ELG 166
Cdd:cd00056  156 DLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 16-168 1.72e-43

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 214684 [Multi-domain]  Cd Length: 149  Bit Score: 149.34  E-value: 1.72e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016    16 MLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 94
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 645066016    95 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 168
Cdd:smart00478  80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 12-148 2.15e-41

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 143.58  E-value: 2.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   12 VSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 89
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 645066016   90 QLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 148
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 16-197 2.42e-35

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 132.07  E-value: 2.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  16 MLQQTQVATVIN-YYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPG 94
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  95 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVraIGADPSSTlvSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPqR 174
Cdd:PRK13910  80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154

                        170       180
                 ....*....|....*....|...
gi 645066016 175 PLCSQCPVESLCRARQRVEQEQL 197
Cdd:PRK13910 155 PKCAICPLNPYCLGKNNPEKHTL 177
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 247-374 5.44e-31

C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.


Pssm-ID: 467537 [Multi-domain]  Cd Length: 118  Bit Score: 115.09  E-value: 5.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 247 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 326
Cdd:cd03431    1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 645066016 327 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 374
Cdd:cd03431   72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
Nth COG0177
Endonuclease III [Replication, recombination and repair];
34-190 9.54e-31

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 117.12  E-value: 9.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  34 QKWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 112
Cdd:COG0177   47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 113 GVVDGNVARVLCRvraIG-ADPSSTL-VSQQLwglaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQ 190
Cdd:COG0177  126 IAVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
NUDIX_4 pfam14815
NUDIX domain;
266-375 2.09e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 94.30  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  266 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKalLQELQRWAgpLPATHLRHlGEVVHTFSHIKLTYQVYGLALEGQTP 345
Cdd:pfam14815  11 RVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEA--LARLEELG--IEVEVLEP-GTVKHVFTHFRLTLHVYLVREVEGEE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 645066016  346 vtTVPPGARWLTQEEFHTAAVSTAMKKVFR 375
Cdd:pfam14815  86 --EPQQELRWVTPEELDKYALPAAVRKILE 113
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 34-177 2.33e-22

endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273434 [Multi-domain]  Cd Length: 192  Bit Score: 93.98  E-value: 2.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016   34 QKWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 112
Cdd:TIGR01083  54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 645066016  113 GVVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 177
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 59-192 1.33e-08

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 55.02  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  59 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVraiGADPSSTLv 138
Cdd:PRK10702  82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT---QFAPGKNV- 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 645066016 139 sQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 192
Cdd:PRK10702 157 -EQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 38-192 1.20e-06

3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 49.07  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016  38 TLQDLASASLEEVNQLWAGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFG 109
Cdd:COG2231   61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 110 QATGVVDGNVARVLCRVrAIGADPSStlvsqqlWGLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSQCPVE 183
Cdd:COG2231  141 RPVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211


                 ....*....
gi 645066016 184 SLCRARQRV 192
Cdd:COG2231  212 DLCPYGGQE 220
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 256-363 1.96e-05

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.


Pssm-ID: 467531 [Multi-domain]  Cd Length: 123  Bit Score: 43.59  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 256 VLEQPGalgaQILLVQRPNSGLLAGLWEFP--SVtwEPSEQLQrKALLQELQ---RWAgplpATHLRHLGEVVHTFSHIK 330
Cdd:cd03425    7 IIVDDG----RVLIAQRPEGKHLAGLWEFPggKV--EPGETPE-QALVRELReelGIE----VEVGEPLGTVEHDYPDFH 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 645066016 331 LTYQVYGLALEGQTPVTTVPPGARWLTQEEFHT 363
Cdd:cd03425   76 VRLHVYLCTLWSGEPQLLEHQELRWVTPEELDD 108
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
256-305 2.06e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.96  E-value: 2.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 645066016 256 VLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlQRKALLQELQ 305
Cdd:PRK10546  10 IIERDG----KILLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 169-189 3.39e-05

iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 40.23  E-value: 3.39e-05
                           10        20
                   ....*....|....*....|.
gi 645066016   169 VCTPQRPLCSQCPVESLCRAR 189
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 76-106 8.20e-05

Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 425789 [Multi-domain]  Cd Length: 30  Bit Score: 39.32  E-value: 8.20e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 645066016   76 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 106
Cdd:pfam00633   1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
266-360 1.21e-04

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 41.51  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 266 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrKALLQELQRWAGpLPATHLRHLGEVVHTFS--HIKLTY--------QV 335
Cdd:PRK10776  17 EIFITRRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITLWFwlveswegEP 94

                         90       100
                 ....*....|....*....|....*
gi 645066016 336 YGlaLEGQtpvttvpPGaRWLTQEE 360
Cdd:PRK10776  95 WG--KEGQ-------PG-RWVSQVA 109
PRK08999 PRK08999
Nudix family hydrolase;
266-361 2.31e-03

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 39.86  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 266 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLqRKALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLT---YQVYG----- 337
Cdd:PRK08999  18 RILLARRPEGKHQGGLWEFPGGKVEPGETV-EQALARELQEELG-IEVTAARPLITVRHDYPDKRVRldvRRVTAwqgep 95

                         90       100
                 ....*....|....*....|....
gi 645066016 338 LALEGQtPVTTVPPgaRWLTQEEF 361
Cdd:PRK08999  96 HGREGQ-PLAWVAP--DELAVYPF 116
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 170-186 2.56e-03

Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99.18) is a DNA repair enzyme that acts both as a DNA N-glycosylase, removing oxidized pyrimidines from DNA, and as an apurinic/apyrimidinic (AP) endonuclease, introducing a single-strand nick at the site from which the damaged base was removed. Endonuclease III is an iron-sulfur protein that binds a single 4Fe-4S cluster. The 4Fe-4S cluster does not seem to be important for catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand. The 4Fe-4S cluster is bound by four cysteines which are all located in a 17 amino acid region at the C-terminal end of endonuclease III. A similar region is also present in the central section of mutY and in the C-terminus of ORF-10 and of the Micro-coccus UV endonuclease.


Pssm-ID: 463153 [Multi-domain]  Cd Length: 17  Bit Score: 35.05  E-value: 2.56e-03
                          10
                  ....*....|....*..
gi 645066016  170 CTPQRPLCSQCPVESLC 186
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
252-375 6.74e-03

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 36.49  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645066016 252 SATCVLEQPGAlgaQILLVQRPNsGLLAGLWEFPSVTWEPSEQLqRKALLQELqrW--AGpLPATHLRHLGEVVHTFSHI 329
Cdd:COG1051    8 AVDAVIFRKDG---RVLLVRRAD-EPGKGLWALPGGKVEPGETP-EEAALREL--ReeTG-LEVEVLELLGVFDHPDRGH 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 645066016 330 KLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFR 375
Cdd:COG1051   80 VVSVAFLAEVLSGEPRADDEIDEARWFPLDELPELAFTPADHEILE 125
 
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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