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Conserved domains on  [gi|209364530|ref|NP_001129220|]
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endonuclease 8-like 2 isoform c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FpgNei_N super family cl03119
N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) ...
 1-69 7.05e-32

N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases; DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. These enzymes initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycolsylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. The FpgNei DNA glycosylases represent one of the two structural superfamilies of DNA glycosylases that recognize oxidized bases (the other is the HTH-GPD superfamily exemplified by Escherichia coli Nth). Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. One exception is mouse Nei-like glycosylase 3 (Neil3) which forms a Schiff base intermediate via its N-terminal valine. In addition to this FpgNei_N domain, FpgNei proteins have a helix-two-turn-helix (H2TH) domain and a zinc (or zincless)-finger motif which also contribute residues to the active site. FpgNei DNA glycosylases have a broad substrate specificity. They are bifunctional, in addition to the glycosylase (recognition) activity, they have a lyase (cleaving) activity on the phosphodiester backbone of the DNA at the AP site. This superfamily includes eukaryotic, bacterial, and viral proteins.


The actual alignment was detected with superfamily member cd08968:

Pssm-ID: 470740  Cd Length: 126  Bit Score: 112.55  E-value: 7.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530   1 MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQV--------------------------------- 47
Cdd:cd08968    1 MPEGPSVRKFHHLVSPFVGQRVVKVGGSSKKINPNDLQGLRLQDSQVhgknlflhfdldeemgpdrdagrwlrfhfglfg 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 209364530  48 ------------------------RLVLHFGGGGFLAFYNCQLSWS 69
Cdd:cd08968   81 svranefsrakkankrgdwkdpnpRLVLHFESGGFLVFYNCRMSWC 126
Nei super family cl33822
Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair];
46-204 1.08e-21

Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0266:

Pssm-ID: 440036 [Multi-domain]  Cd Length: 272  Bit Score: 89.80  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  46 QVRLVLHFGGGGFLAFYN------CQLSWSSSPVVTPTC-----DILSEKFHRGQALEAL-GQAQPVCYTLLDQRYFSGL 113
Cdd:COG0266   91 HDHVRLVLDDGTELRFADprrfgaLELLTPDELEVHPLLarlgpEPLDPDFDPEYLAARLrRRRRPIKALLLDQSVVAGV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530 114 GNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQ----------------GKFQgrpQHTQVYQK--EQC 175
Cdd:COG0266  171 GNIYADEALFRAGIHPLRPAGSLSRAELERLAAAIREVLREAIEaggttlrdyvnadgepGYFQ---QRLYVYGRegEPC 247

                        170       180       190
                 ....*....|....*....|....*....|
gi 209364530 176 PA-GHQVMKEAFGpedglQRLTWWCPQCQP 204
Cdd:COG0266  248 PRcGTPIERIVLG-----GRSTYYCPRCQR 272
 
Name Accession Description Interval E-value
MeNeil2_N cd08968
N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the ...
 1-69 7.05e-32

N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the N-terminal domain of the metazoan protein Neil2. It belongs to the FpgNei_N, [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL2 repairs 5-hydroxyuracil (5-OHU) and other oxidized derivatives of cytosine, but it shows preference for DNA bubble structures. In addition to this MeNeil2_N domain, NEIL2 contains a helix-two turn-helix (H2TH) domain and a characteristic CHCC zinc finger motif. Neil2 is one of three homologs found in eukaryotes.


Pssm-ID: 176802  Cd Length: 126  Bit Score: 112.55  E-value: 7.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530   1 MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQV--------------------------------- 47
Cdd:cd08968    1 MPEGPSVRKFHHLVSPFVGQRVVKVGGSSKKINPNDLQGLRLQDSQVhgknlflhfdldeemgpdrdagrwlrfhfglfg 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 209364530  48 ------------------------RLVLHFGGGGFLAFYNCQLSWS 69
Cdd:cd08968   81 svranefsrakkankrgdwkdpnpRLVLHFESGGFLVFYNCRMSWC 126
Nei COG0266
Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair];
46-204 1.08e-21

Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 440036 [Multi-domain]  Cd Length: 272  Bit Score: 89.80  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  46 QVRLVLHFGGGGFLAFYN------CQLSWSSSPVVTPTC-----DILSEKFHRGQALEAL-GQAQPVCYTLLDQRYFSGL 113
Cdd:COG0266   91 HDHVRLVLDDGTELRFADprrfgaLELLTPDELEVHPLLarlgpEPLDPDFDPEYLAARLrRRRRPIKALLLDQSVVAGV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530 114 GNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQ----------------GKFQgrpQHTQVYQK--EQC 175
Cdd:COG0266  171 GNIYADEALFRAGIHPLRPAGSLSRAELERLAAAIREVLREAIEaggttlrdyvnadgepGYFQ---QRLYVYGRegEPC 247

                        170       180       190
                 ....*....|....*....|....*....|
gi 209364530 176 PA-GHQVMKEAFGpedglQRLTWWCPQCQP 204
Cdd:COG0266  248 PRcGTPIERIVLG-----GRSTYYCPRCQR 272
PRK01103 PRK01103
bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
103-205 8.13e-18

bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase;


Pssm-ID: 234899 [Multi-domain]  Cd Length: 274  Bit Score: 79.36  E-value: 8.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530 103 TLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE---------------FSTAwlQGK---FQgrp 164
Cdd:PRK01103 161 ALLDQTVVVGVGNIYADEALFRAGIHPERPAGSLSRAEAERLVDAIKAvlaeaieqggttlrdYVNA--DGKpgyFQ--- 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 209364530 165 QHTQVY--QKEQCPA-GHQVMKEAFGpedglQRLTWWCPQCQPQ 205
Cdd:PRK01103 236 QSLQVYgrEGEPCRRcGTPIEKIKQG-----GRSTFFCPRCQKR 274
fpg TIGR00577
DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are ...
 104-203 1.61e-15

DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are FAPY-DNA glycosylases that function in base excision repair. Homologous to endonuclease VIII (nei). 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: 273150 [Multi-domain]  Cd Length: 272  Bit Score: 73.10  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  104 LLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE------------FST----AWLQGKFQGRpqhT 167
Cdd:TIGR00577 162 LLDQRLVAGIGNIYADEVLFRAGIHPERLASSLSKEECELLHRAIKEvlrkaiemggttIRDfsqsDGHNGYFQQE---L 238

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 209364530  168 QVYQK--EQCPA-GHQVMKEAFGpedglQRLTWWCPQCQ 203
Cdd:TIGR00577 239 QVYGRkgEPCRRcGTTIEKEKVG-----GRGTHFCPQCQ 272
H2TH pfam06831
Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is ...
 104-150 2.95e-12

Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. This family is the central domain containing the DNA-binding helix-two turn-helix domain.


Pssm-ID: 399664 [Multi-domain]  Cd Length: 89  Bit Score: 60.38  E-value: 2.95e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 209364530  104 LLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE 150
Cdd:pfam06831  30 LLDQTLVAGLGNIYADEVLFRAGIHPERLANSLSKEECELLHQAIKA 76
 
Name Accession Description Interval E-value
MeNeil2_N cd08968
N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the ...
 1-69 7.05e-32

N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the N-terminal domain of the metazoan protein Neil2. It belongs to the FpgNei_N, [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL2 repairs 5-hydroxyuracil (5-OHU) and other oxidized derivatives of cytosine, but it shows preference for DNA bubble structures. In addition to this MeNeil2_N domain, NEIL2 contains a helix-two turn-helix (H2TH) domain and a characteristic CHCC zinc finger motif. Neil2 is one of three homologs found in eukaryotes.


Pssm-ID: 176802  Cd Length: 126  Bit Score: 112.55  E-value: 7.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530   1 MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQV--------------------------------- 47
Cdd:cd08968    1 MPEGPSVRKFHHLVSPFVGQRVVKVGGSSKKINPNDLQGLRLQDSQVhgknlflhfdldeemgpdrdagrwlrfhfglfg 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 209364530  48 ------------------------RLVLHFGGGGFLAFYNCQLSWS 69
Cdd:cd08968   81 svranefsrakkankrgdwkdpnpRLVLHFESGGFLVFYNCRMSWC 126
Nei COG0266
Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair];
46-204 1.08e-21

Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 440036 [Multi-domain]  Cd Length: 272  Bit Score: 89.80  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  46 QVRLVLHFGGGGFLAFYN------CQLSWSSSPVVTPTC-----DILSEKFHRGQALEAL-GQAQPVCYTLLDQRYFSGL 113
Cdd:COG0266   91 HDHVRLVLDDGTELRFADprrfgaLELLTPDELEVHPLLarlgpEPLDPDFDPEYLAARLrRRRRPIKALLLDQSVVAGV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530 114 GNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQ----------------GKFQgrpQHTQVYQK--EQC 175
Cdd:COG0266  171 GNIYADEALFRAGIHPLRPAGSLSRAELERLAAAIREVLREAIEaggttlrdyvnadgepGYFQ---QRLYVYGRegEPC 247

                        170       180       190
                 ....*....|....*....|....*....|
gi 209364530 176 PA-GHQVMKEAFGpedglQRLTWWCPQCQP 204
Cdd:COG0266  248 PRcGTPIERIVLG-----GRSTYYCPRCQR 272
PRK01103 PRK01103
bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
103-205 8.13e-18

bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase;


Pssm-ID: 234899 [Multi-domain]  Cd Length: 274  Bit Score: 79.36  E-value: 8.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530 103 TLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE---------------FSTAwlQGK---FQgrp 164
Cdd:PRK01103 161 ALLDQTVVVGVGNIYADEALFRAGIHPERPAGSLSRAEAERLVDAIKAvlaeaieqggttlrdYVNA--DGKpgyFQ--- 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 209364530 165 QHTQVY--QKEQCPA-GHQVMKEAFGpedglQRLTWWCPQCQPQ 205
Cdd:PRK01103 236 QSLQVYgrEGEPCRRcGTPIEKIKQG-----GRSTFFCPRCQKR 274
fpg TIGR00577
DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are ...
 104-203 1.61e-15

DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are FAPY-DNA glycosylases that function in base excision repair. Homologous to endonuclease VIII (nei). 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: 273150 [Multi-domain]  Cd Length: 272  Bit Score: 73.10  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  104 LLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE------------FST----AWLQGKFQGRpqhT 167
Cdd:TIGR00577 162 LLDQRLVAGIGNIYADEVLFRAGIHPERLASSLSKEECELLHRAIKEvlrkaiemggttIRDfsqsDGHNGYFQQE---L 238

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 209364530  168 QVYQK--EQCPA-GHQVMKEAFGpedglQRLTWWCPQCQ 203
Cdd:TIGR00577 239 QVYGRkgEPCRRcGTTIEKEKVG-----GRGTHFCPQCQ 272
H2TH pfam06831
Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is ...
 104-150 2.95e-12

Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. This family is the central domain containing the DNA-binding helix-two turn-helix domain.


Pssm-ID: 399664 [Multi-domain]  Cd Length: 89  Bit Score: 60.38  E-value: 2.95e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 209364530  104 LLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE 150
Cdd:pfam06831  30 LLDQTLVAGLGNIYADEVLFRAGIHPERLANSLSKEECELLHQAIKA 76
PRK14811 PRK14811
formamidopyrimidine-DNA glycosylase; Provisional
 81-204 1.87e-10

formamidopyrimidine-DNA glycosylase; Provisional


Pssm-ID: 184831 [Multi-domain]  Cd Length: 269  Bit Score: 59.04  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  81 LSEKFHRGQALEALGQAQPVCYTLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASR--------REVLVDHVVEFS 152
Cdd:PRK14811 127 LSDDFTEPEFVRALATARPVKPWLLSQKPVAGVGNIYADESLWRARIHPARPATSLKAPEarrlyraiREVMAEAVEAGG 206

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209364530 153 TAWLQGKFQ---GRPQHTQ----VYQKE--QCPA-GHQVMKEAFGpedglQRLTWWCPQCQP 204
Cdd:PRK14811 207 STLSDGSYRqpdGEPGGFQfqhaVYGREgqPCPRcGTPIEKIVVG-----GRGTHFCPQCQP 263
PRK13945 PRK13945
formamidopyrimidine-DNA glycosylase; Provisional
 104-204 7.46e-08

formamidopyrimidine-DNA glycosylase; Provisional


Pssm-ID: 184410 [Multi-domain]  Cd Length: 282  Bit Score: 51.47  E-value: 7.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530 104 LLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVE------------FS----TAWLQGKFQGRpqhT 167
Cdd:PRK13945 171 LLDQSIVAGIGNIYADESLFKAGIHPTTPAGQLKKKQLERLREAIIEvlktsigaggttFSdfrdLEGVNGNYGGQ---A 247

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 209364530 168 QVYQKEQCP---AGHQVMKEAFGpedglQRLTWWCPQCQP 204
Cdd:PRK13945 248 WVYRRTGKPcrkCGTPIERIKLA-----GRSTHWCPNCQK 282
PRK14810 PRK14810
formamidopyrimidine-DNA glycosylase; Provisional
 95-203 1.03e-07

formamidopyrimidine-DNA glycosylase; Provisional


Pssm-ID: 173271 [Multi-domain]  Cd Length: 272  Bit Score: 51.06  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  95 GQAQPVCYTLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQ----------------G 158
Cdd:PRK14810 152 GRKTRIKSALLNQTLLRGVGNIYADEALFRAGIRPQRLASSLSRERLRKLHDAIGEVLREAIElggssvsdyvdaegrsG 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 209364530 159 KFQGRpqHtQVYQK--EQCPAGHQVMKEAFGPedglQRLTWWCPQCQ 203
Cdd:PRK14810 232 FFQLS--H-RVYQRtgEPCLNCKTPIRRVVVA----GRSSHYCPHCQ 271
PRK10445 PRK10445
endonuclease VIII; Provisional
 80-204 5.31e-06

endonuclease VIII; Provisional


Pssm-ID: 182467 [Multi-domain]  Cd Length: 263  Bit Score: 45.79  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209364530  80 ILSEKFHRGQaLEALgqaqpvcytLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQ-- 157
Cdd:PRK10445 144 LLSPRFRNRQ-FSGL---------LLDQAFLAGLGNYLRVEILWQAGLTPQHKAKDLNEAQLDALAHALLDIPRLSYAtr 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 209364530 158 -----GKFQGRPQHTQVYQK-----EQCpaGHQVMKEAFGpedglQRLTWWCPQCQP 204
Cdd:PRK10445 214 gqvdeNKHHGALFRFKVFHRdgeacERC--GGIIEKTTLS-----SRPFYWCPGCQK 263
 
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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