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Conserved domains on  [gi|367024081|ref|XP_003661325|]
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uncharacterized protein MYCTH_2300579 [Thermothelomyces thermophilus ATCC 42464]

Protein Classification

single-stranded DNA-binding protein( domain architecture ID 10858872)

single-stranded DNA (ssDNA)-binding protein plays a key role in DNA replication, recombination, and repair

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 196-360 5.86e-63

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: 205.97  E-value: 5.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  196 LKDVQEGKFCDLIVQVVRDPYDGLTALTLYVSDYTENPRFHPRAWEGLSDSGLGDGDPYgyttgvadVPNKEWVGPYGRM 275
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFK--------PRIGKWIGPFGKL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  276 SLQITCFEPHATFIREEVKAGQWVGLRNVQIKYGRDGRFLEGFLREERGSSSRRVNVDIldlanADTIDPNLKEAIRRCR 355
Cdd:pfam16686  73 TLQITLYDPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVI-----DDNNDPRLKELKRRKR 147


                  ....*
gi 367024081  356 DYHKK 360
Cdd:pfam16686 148 EYEKT 152
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 29-163 6.17e-28

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: 109.29  E-value: 6.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  29 PILDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTdEDNHDINFVVFRP-EADMPRVTAGDVVVATNVKVQ 107
Cdd:cd04497    5 PLSSALKESGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSL-ANSDGLTVKLFRPnEESLPIVKVGDIILLRRVKIQ 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 367024081 108 RYRGDLSLITN-RTTSIRVYTASKIPPRPqsAKIALAPASKRDTHVPTVAETAYVSH 163
Cdd:cd04497   84 SYNGKPQGISNdRGSSWAVFRGDDGVVPI--PQQSSKPVEFGPEEEPSVEELRKWAS 138
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 196-360 5.86e-63

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: 205.97  E-value: 5.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  196 LKDVQEGKFCDLIVQVVRDPYDGLTALTLYVSDYTENPRFHPRAWEGLSDSGLGDGDPYgyttgvadVPNKEWVGPYGRM 275
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFK--------PRIGKWIGPFGKL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  276 SLQITCFEPHATFIREEVKAGQWVGLRNVQIKYGRDGRFLEGFLREERGSSSRRVNVDIldlanADTIDPNLKEAIRRCR 355
Cdd:pfam16686  73 TLQITLYDPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVI-----DDNNDPRLKELKRRKR 147


                  ....*
gi 367024081  356 DYHKK 360
Cdd:pfam16686 148 EYEKT 152
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 29-163 6.17e-28

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: 109.29  E-value: 6.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  29 PILDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTdEDNHDINFVVFRP-EADMPRVTAGDVVVATNVKVQ 107
Cdd:cd04497    5 PLSSALKESGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSL-ANSDGLTVKLFRPnEESLPIVKVGDIILLRRVKIQ 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 367024081 108 RYRGDLSLITN-RTTSIRVYTASKIPPRPqsAKIALAPASKRDTHVPTVAETAYVSH 163
Cdd:cd04497   84 SYNGKPQGISNdRGSSWAVFRGDDGVVPI--PQQSSKPVEFGPEEEPSVEELRKWAS 138
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 31-166 8.35e-18

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: 80.48  E-value: 8.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081   31 LDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTDEDNHD-INFVVFRP-EADMPRV-TAGDVVVATNVKVQ 107
Cdd:pfam02765   4 LDKALAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDSNDgLRVVFFRKnFEDLPIVkKVGDIILLHRVKIQ 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367024081  108 RYRGD-LSLITNRTT-SIRVYtaskippRPQSAKIALAPASKRDTHVPTVAETAYVSHIYH 166
Cdd:pfam02765  84 SFNGEpQGLANIGFSsSWALF-------NGKLNRLYTPPILGSNFFEFSAEEKKYLESLRK 137
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-166 1.29e-14

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: 71.20  E-value: 1.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081    29 PILDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTdEDNHDINFVVFRPEA-DMPRVTA-GDVVVATNVKV 106
Cdd:smart00976   3 PIKDLTSATNKYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSY-ADGYGLTVKLFSPTLeSLPVIKYvGDIILLHRVKI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081   107 QRYRGDLSLITNRTTSIRVYtaskipPRPQSAKIALAPASKRDTHVPTvAETAYVSHIYH 166
Cdd:smart00976  82 QDFNNRIQGLCSFGTSSWAV------FGPLNGVVRERESSPPSTFTPE-DEKQYVEELRN 134
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 196-360 5.86e-63

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: 205.97  E-value: 5.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  196 LKDVQEGKFCDLIVQVVRDPYDGLTALTLYVSDYTENPRFHPRAWEGLSDSGLGDGDPYgyttgvadVPNKEWVGPYGRM 275
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFK--------PRIGKWIGPFGKL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  276 SLQITCFEPHATFIREEVKAGQWVGLRNVQIKYGRDGRFLEGFLREERGSSSRRVNVDIldlanADTIDPNLKEAIRRCR 355
Cdd:pfam16686  73 TLQITLYDPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVI-----DDNNDPRLKELKRRKR 147


                  ....*
gi 367024081  356 DYHKK 360
Cdd:pfam16686 148 EYEKT 152
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 29-163 6.17e-28

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: 109.29  E-value: 6.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  29 PILDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTdEDNHDINFVVFRP-EADMPRVTAGDVVVATNVKVQ 107
Cdd:cd04497    5 PLSSALKESGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSL-ANSDGLTVKLFRPnEESLPIVKVGDIILLRRVKIQ 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 367024081 108 RYRGDLSLITN-RTTSIRVYTASKIPPRPqsAKIALAPASKRDTHVPTVAETAYVSH 163
Cdd:cd04497   84 SYNGKPQGISNdRGSSWAVFRGDDGVVPI--PQQSSKPVEFGPEEEPSVEELRKWAS 138
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 31-166 8.35e-18

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: 80.48  E-value: 8.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081   31 LDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTDEDNHD-INFVVFRP-EADMPRV-TAGDVVVATNVKVQ 107
Cdd:pfam02765   4 LDKALAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDSNDgLRVVFFRKnFEDLPIVkKVGDIILLHRVKIQ 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367024081  108 RYRGD-LSLITNRTT-SIRVYtaskippRPQSAKIALAPASKRDTHVPTVAETAYVSHIYH 166
Cdd:pfam02765  84 SFNGEpQGLANIGFSsSWALF-------NGKLNRLYTPPILGSNFFEFSAEEKKYLESLRK 137
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-166 1.29e-14

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: 71.20  E-value: 1.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081    29 PILDEVVSPGGLVNVIGVVKDCRLPIPTNGNDHKCTITLYDLSTdEDNHDINFVVFRPEA-DMPRVTA-GDVVVATNVKV 106
Cdd:smart00976   3 PIKDLTSATNKYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSY-ADGYGLTVKLFSPTLeSLPVIKYvGDIILLHRVKI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081   107 QRYRGDLSLITNRTTSIRVYtaskipPRPQSAKIALAPASKRDTHVPTvAETAYVSHIYH 166
Cdd:smart00976  82 QDFNNRIQGLCSFGTSSWAV------FGPLNGVVRERESSPPSTFTPE-DEKQYVEELRN 134
RPA2_OBF_family cd03524
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold ...
 42-120 1.46e-03

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: 37.73  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  42 NVIGVVKDCRlpiPTNGNDHKCTITLydlsTDEDNHDINFVVFRP--EADMPRVTAGDVVVATnVKVQRYRGDLSLITNR 119
Cdd:cd03524    1 TIVGIVVAVE---EIRTEGKVLIFTL----TDGTGGTIRVTLFGElaEELENLLKEGQVVYIK-GKVKKFRGRLQLIVES 72


                 .
gi 367024081 120 T 120
Cdd:cd03524   73 I 73
SoSSB_OBF cd04491
SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus ...
 42-125 8.18e-03

SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus solfataricus single-stranded (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB fold, and it physically and functionally interacts with RNA polymerase. In vitro, SSoSSB can substitute for the basal transcription factor TBP, stimulating transcription from promoters under conditions in which TBP is limiting, and supporting transcription when TBP is absent. SSoSSB selectively melts the duplex DNA of promoter sequences. It also relieves transcriptional repression by the chromatin Alba. In addition, SSoSSB activates reverse gyrase activity, which involves DNA binding, DNA cleavage, strand passage and ligation. SSoSSB stimulates all these steps in the presence of the chromatin protein, Sul7d. SSoSSB antagonizes the inhibitory effect of Sul7d on reverse gyrase supercoiling activity. It also physically and functionally interacts with Mini-chromosome Maintenance (MCM), stimulating the DNA helicase activity of MCM.


Pssm-ID: 239937 [Multi-domain]  Cd Length: 82  Bit Score: 35.68  E-value: 8.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367024081  42 NVIGVVKDC--RLPIPTNGNDHK-CTITLYDlstdeDNHDINFVVFRPEADmPRVTAGDVVVATNVKVQRYRGDLSLITN 118
Cdd:cd04491    1 SVEGKVLSIsePREFTRDGSEGKvQSGLVGD-----ETGTIRFTLWDEKAA-DDLEPGDVVRIENAYVREFNGRLELSVG 74


                 ....*..
gi 367024081 119 RTTSIRV 125
Cdd:cd04491   75 KNSEIEK 81
 
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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