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Conserved domains on  [gi|284055716]
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Chain A, Protection of telomeres protein 1

Protein Classification

hPOT1_OB1_like and hPOT1_OB2 domain-containing protein( domain architecture ID 10659501)

hPOT1_OB1_like and hPOT1_OB2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 161-278 2.84e-53

hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation.


:

Pssm-ID: 239944  Cd Length: 123  Bit Score: 169.91  E-value: 2.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716 161 YFDLTCQLLGKAEVDGASFLLKVWDGTRTPFPSWRVLIQDL-VLEGDLSHIHRLQN---LTIDILVYDNHVHVARSLKVG 236
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRKVKVEDDvVLEGDRSLKHREEGgkqLTIDILVYDNHVELAKSLKPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 284055716 237 SFLRIYSLHTKLQSMNSENQTMLSLEFHL-HGGTSYGRGIRVL 278
Cdd:cd04498   81 DFVRIYNVHAKSYSSKNEHDENDHLHFHLvHGGTEYGRGIRVL 123
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 11-141 1.44e-49

Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a heterodimer in ciliates consisting of an alpha and a beta subunit. This complex may function as a protective cap for the single-stranded telomeric overhang. Alpha subunit consists of 3 structural domains, all with the same beta-barrel OB fold.


:

Pssm-ID: 214949  Cd Length: 137  Bit Score: 160.95  E-value: 1.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716    11 YTPLNQLKGGT--IVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQTNVK---LTCLLFSGNYEALPIIYKNGDIVRFHRLK 85
Cdd:smart00976   1 FTPIKDLTSATnkYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADgygLTVKLFSPTLESLPVIKYVGDIILLHRVK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 284055716    86 IQVYKKETQGITSSGFASLTFEGTLGAPIIPRTSSKYFNFTTEDHKM-VEALRVWAS 141
Cdd:smart00976  81 IQDFNNRIQGLCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQyVEELRNWAF 137
 
Name Accession Description Interval E-value
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 161-278 2.84e-53

hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation.


Pssm-ID: 239944  Cd Length: 123  Bit Score: 169.91  E-value: 2.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716 161 YFDLTCQLLGKAEVDGASFLLKVWDGTRTPFPSWRVLIQDL-VLEGDLSHIHRLQN---LTIDILVYDNHVHVARSLKVG 236
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRKVKVEDDvVLEGDRSLKHREEGgkqLTIDILVYDNHVELAKSLKPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 284055716 237 SFLRIYSLHTKLQSMNSENQTMLSLEFHL-HGGTSYGRGIRVL 278
Cdd:cd04498   81 DFVRIYNVHAKSYSSKNEHDENDHLHFHLvHGGTEYGRGIRVL 123
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 153-298 1.02e-50

ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a family of fungal telomere protection protein 1 proteins. POT1PC is able to accommodate heterogeneous ssDNA ligands. Pot1 proteins are the proteins responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres.


Pssm-ID: 435514  Cd Length: 152  Bit Score: 164.37  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716  153 LCDVQPMQYFDLTCQLLGKAEVDGASFLLKVWDGTRTPFPSWRVLIQDLVLEGDL--------SHIHRLQNLTIDILVYD 224
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDddfkprigKWIGPFGKLTLQITLYD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284055716  225 NHVHVARS-LKVGSFLRIYSLHTKLQSMNsenqtmLSLEFHLHGGTSYGRGIRVL---PESNSDVDQLKKDLESANLT 298
Cdd:pfam16686  81 PHASFAREnLKPGDFVRLRNVHIKYGRNG------LNLEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKREYEKT 152
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 11-141 1.44e-49

Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a heterodimer in ciliates consisting of an alpha and a beta subunit. This complex may function as a protective cap for the single-stranded telomeric overhang. Alpha subunit consists of 3 structural domains, all with the same beta-barrel OB fold.


Pssm-ID: 214949  Cd Length: 137  Bit Score: 160.95  E-value: 1.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716    11 YTPLNQLKGGT--IVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQTNVK---LTCLLFSGNYEALPIIYKNGDIVRFHRLK 85
Cdd:smart00976   1 FTPIKDLTSATnkYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADgygLTVKLFSPTLESLPVIKYVGDIILLHRVK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 284055716    86 IQVYKKETQGITSSGFASLTFEGTLGAPIIPRTSSKYFNFTTEDHKM-VEALRVWAS 141
Cdd:smart00976  81 IQDFNNRIQGLCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQyVEELRNWAF 137
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 9-141 4.66e-48

hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection of telomeres 1 protein (hPOT1), the single OB fold of the N-terminal domain of Schizosaccharomyces pombe POT1 (SpPOT1), and the first OB fold of the N-terminal domain of the alpha subunit (OB1Nalpha) of Oxytricha nova telomere end binding protein (OnTEBP). POT1 proteins recognize single-stranded (ss) 3-prime ends of the telomere. A 3-prime ss overhang is conserved in ciliated protozoa, yeast, and mammals. SpPOT1 is essential for telomere maintenance. It binds specifically to the ss G-rich telomeric sequence (GGTTAC) of S. pombe. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. Deletion of the S. pombe pot1+ gene results in a rapid loss of telomere sequences, chromosome mis-segregation and chromosome circularization. hPOT1 is implicated in telomere length regulation. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. A second OB fold has not been predicted in S. pombe POT1. OnTEBP binds the extreme 3-prime end of telomeric DNA. It is heterodimeric and contains four OB folds - three in the alpha subunit (two in the N-terminal domain and one in the C-terminal domain) and one in the beta subunit. OB1Nalpha, together with the second OB fold of the N-terminal domain of OnTEBP alpha subunit and the beta subunit OB fold, forms a deep cleft that binds ssDNA.


Pssm-ID: 239943  Cd Length: 138  Bit Score: 157.05  E-value: 4.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716   9 YIYTPLNQLKG--GTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQT---NVKLTCLLFSGNYEALPIIyKNGDIVRFHR 83
Cdd:cd04497    1 YKYTPLSSALKesGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSlanSDGLTVKLFRPNEESLPIV-KVGDIILLRR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 284055716  84 LKIQVYKKETQGITS-SGFASLTFEGTLGAPIIPRTSSKYFNFTTEDHKMVEALRVWAS 141
Cdd:cd04497   80 VKIQSYNGKPQGISNdRGSSWAVFRGDDGVVPIPQQSSKPVEFGPEEEPSVEELRKWAS 138
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 11-141 2.02e-39

Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric DNA and adopts an OB fold. It includes the proteins POT1 and CDC13 which have been shown to regulate telomere length, replication and capping. POT1 is one component of the shelterin complex that protects telomere-ends from attack by DNA-repair mechanisms.


Pssm-ID: 397060  Cd Length: 140  Bit Score: 134.79  E-value: 2.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716   11 YTPLNQL-KGGTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQT-----NVKLTCLLFSGNYEALPIIYKNGDIVRFHRL 84
Cdd:pfam02765   1 FVDLDKAlAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSlkgdsNDGLRVVFFRKNFEDLPIVKKVGDIILLHRV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716   85 KIQVYKKETQGITSSGFAS--LTFEGTLG-APIIPRTSSKYFNFTTEDHKMVEALRVWAS 141
Cdd:pfam02765  81 KIQSFNGEPQGLANIGFSSswALFNGKLNrLYTPPILGSNFFEFSAEEKKYLESLRKWAE 140
 
Name Accession Description Interval E-value
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 161-278 2.84e-53

hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation.


Pssm-ID: 239944  Cd Length: 123  Bit Score: 169.91  E-value: 2.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716 161 YFDLTCQLLGKAEVDGASFLLKVWDGTRTPFPSWRVLIQDL-VLEGDLSHIHRLQN---LTIDILVYDNHVHVARSLKVG 236
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRKVKVEDDvVLEGDRSLKHREEGgkqLTIDILVYDNHVELAKSLKPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 284055716 237 SFLRIYSLHTKLQSMNSENQTMLSLEFHL-HGGTSYGRGIRVL 278
Cdd:cd04498   81 DFVRIYNVHAKSYSSKNEHDENDHLHFHLvHGGTEYGRGIRVL 123
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 153-298 1.02e-50

ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a family of fungal telomere protection protein 1 proteins. POT1PC is able to accommodate heterogeneous ssDNA ligands. Pot1 proteins are the proteins responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres.


Pssm-ID: 435514  Cd Length: 152  Bit Score: 164.37  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716  153 LCDVQPMQYFDLTCQLLGKAEVDGASFLLKVWDGTRTPFPSWRVLIQDLVLEGDL--------SHIHRLQNLTIDILVYD 224
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDddfkprigKWIGPFGKLTLQITLYD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284055716  225 NHVHVARS-LKVGSFLRIYSLHTKLQSMNsenqtmLSLEFHLHGGTSYGRGIRVL---PESNSDVDQLKKDLESANLT 298
Cdd:pfam16686  81 PHASFAREnLKPGDFVRLRNVHIKYGRNG------LNLEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKREYEKT 152
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 11-141 1.44e-49

Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a heterodimer in ciliates consisting of an alpha and a beta subunit. This complex may function as a protective cap for the single-stranded telomeric overhang. Alpha subunit consists of 3 structural domains, all with the same beta-barrel OB fold.


Pssm-ID: 214949  Cd Length: 137  Bit Score: 160.95  E-value: 1.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716    11 YTPLNQLKGGT--IVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQTNVK---LTCLLFSGNYEALPIIYKNGDIVRFHRLK 85
Cdd:smart00976   1 FTPIKDLTSATnkYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADgygLTVKLFSPTLESLPVIKYVGDIILLHRVK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 284055716    86 IQVYKKETQGITSSGFASLTFEGTLGAPIIPRTSSKYFNFTTEDHKM-VEALRVWAS 141
Cdd:smart00976  81 IQDFNNRIQGLCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQyVEELRNWAF 137
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 9-141 4.66e-48

hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection of telomeres 1 protein (hPOT1), the single OB fold of the N-terminal domain of Schizosaccharomyces pombe POT1 (SpPOT1), and the first OB fold of the N-terminal domain of the alpha subunit (OB1Nalpha) of Oxytricha nova telomere end binding protein (OnTEBP). POT1 proteins recognize single-stranded (ss) 3-prime ends of the telomere. A 3-prime ss overhang is conserved in ciliated protozoa, yeast, and mammals. SpPOT1 is essential for telomere maintenance. It binds specifically to the ss G-rich telomeric sequence (GGTTAC) of S. pombe. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. Deletion of the S. pombe pot1+ gene results in a rapid loss of telomere sequences, chromosome mis-segregation and chromosome circularization. hPOT1 is implicated in telomere length regulation. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. A second OB fold has not been predicted in S. pombe POT1. OnTEBP binds the extreme 3-prime end of telomeric DNA. It is heterodimeric and contains four OB folds - three in the alpha subunit (two in the N-terminal domain and one in the C-terminal domain) and one in the beta subunit. OB1Nalpha, together with the second OB fold of the N-terminal domain of OnTEBP alpha subunit and the beta subunit OB fold, forms a deep cleft that binds ssDNA.


Pssm-ID: 239943  Cd Length: 138  Bit Score: 157.05  E-value: 4.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716   9 YIYTPLNQLKG--GTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQT---NVKLTCLLFSGNYEALPIIyKNGDIVRFHR 83
Cdd:cd04497    1 YKYTPLSSALKesGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSlanSDGLTVKLFRPNEESLPIV-KVGDIILLRR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 284055716  84 LKIQVYKKETQGITS-SGFASLTFEGTLGAPIIPRTSSKYFNFTTEDHKMVEALRVWAS 141
Cdd:cd04497   80 VKIQSYNGKPQGISNdRGSSWAVFRGDDGVVPIPQQSSKPVEFGPEEEPSVEELRKWAS 138
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 11-141 2.02e-39

Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric DNA and adopts an OB fold. It includes the proteins POT1 and CDC13 which have been shown to regulate telomere length, replication and capping. POT1 is one component of the shelterin complex that protects telomere-ends from attack by DNA-repair mechanisms.


Pssm-ID: 397060  Cd Length: 140  Bit Score: 134.79  E-value: 2.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716   11 YTPLNQL-KGGTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQT-----NVKLTCLLFSGNYEALPIIYKNGDIVRFHRL 84
Cdd:pfam02765   1 FVDLDKAlAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSlkgdsNDGLRVVFFRKNFEDLPIVKKVGDIILLHRV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 284055716   85 KIQVYKKETQGITSSGFAS--LTFEGTLG-APIIPRTSSKYFNFTTEDHKMVEALRVWAS 141
Cdd:pfam02765  81 KIQSFNGEPQGLANIGFSSswALFNGKLNrLYTPPILGSNFFEFSAEEKKYLESLRKWAE 140
RPA2_OBF_family cd03524
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold ...
 24-99 4.71e-07

RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold of the single strand (ss) DNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA contains six OB folds, which are involved in ssDNA binding and in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. This family also includes OB folds similar to those found in Escherichia coli SSB, the wedge domain of E. coli RecG (a branched-DNA-specific helicase), E. coli ssDNA specific exodeoxyribonuclease VII large subunit, Pyrococcus abyssi DNA polymerase II (Pol II) small subunit, Sulfolobus solfataricus SSB, and Bacillus subtilis YhaM (a 3'-to-5'exoribonuclease). It also includes the OB folds of breast cancer susceptibility gene 2 protein (BRCA2), Oxytricha nova telomere end binding protein (TEBP), Saccharomyces cerevisiae telomere-binding protein (Cdc13), and human protection of telomeres 1 protein (POT1).


Pssm-ID: 239601 [Multi-domain]  Cd Length: 75  Bit Score: 46.59  E-value: 4.71e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284055716  24 NVYGVVKFFKPPYLSKgtdYCSVVTIVDQTNVKLTCLLFSGNYEALPIIYKNGDIVRFHrLKIQVYKKETQGITSS 99
Cdd:cd03524    1 TIVGIVVAVEEIRTEG---KVLIFTLTDGTGGTIRVTLFGELAEELENLLKEGQVVYIK-GKVKKFRGRLQLIVES 72
 
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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