NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|39654773|pdb|1QZH|E]
View 

Chain E, Protection of telomeres protein 1

Protein Classification

hPOT1_OB1_like domain-containing protein( domain architecture ID 10659500)

hPOT1_OB1_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-173 8.41e-38

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: 127.05  E-value: 8.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E          29 FQSIRSSQELQKKntIVNLFGIVKDFTPSRQSlHGTkDWVTTVYLWDPTCDtSSIGLQIHLFSKQGNDLPVIKQVGQPLL 108
Cdd:smart00976   1 FTPIKDLTSATNK--YVNVIGVVVDFKPPKRS-RGT-DFTCTLTITDPSYA-DGYGLTVKLFSPTLESLPVIKYVGDIIL 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
1QZH_E         109 LHQITLRSYRDRTQGLSKdqFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLnKIWDE 173
Cdd:smart00976  76 LHRVKIQDFNNRIQGLCS--FGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQYVEEL-RNWAF 137
 
Name Accession Description Interval E-value
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-173 8.41e-38

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: 127.05  E-value: 8.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E          29 FQSIRSSQELQKKntIVNLFGIVKDFTPSRQSlHGTkDWVTTVYLWDPTCDtSSIGLQIHLFSKQGNDLPVIKQVGQPLL 108
Cdd:smart00976   1 FTPIKDLTSATNK--YVNVIGVVVDFKPPKRS-RGT-DFTCTLTITDPSYA-DGYGLTVKLFSPTLESLPVIKYVGDIIL 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
1QZH_E         109 LHQITLRSYRDRTQGLSKdqFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLnKIWDE 173
Cdd:smart00976  76 LHRVKIQDFNNRIQGLCS--FGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQYVEEL-RNWAF 137
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 28-172 1.06e-35

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: 121.61  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E       28 TFQSIRSSQElqKKNTIVNLFGIVKDFTPSRQSlhGTKDWVTTVYLWDPTCDTSSiGLQIHLFSKQGNDLPVIKqVGQPL 107
Cdd:cd04497   2 KYTPLSSALK--ESGGSVNVIGVVVDAGPPVRS--KGTDYCCTLTITDPSLANSD-GLTVKLFRPNEESLPIVK-VGDII 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1QZH_E      108 LLHQITLRSYRDRTQGLSKD-QFRYALWPDFSSNSKDtlcPQPMPRLMKTGDKEEQFALLLNKIWD 172
Cdd:cd04497  76 LLRRVKIQSYNGKPQGISNDrGSSWAVFRGDDGVVPI---PQQSSKPVEFGPEEEPSVEELRKWAS 138
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 36-169 1.56e-27

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: 100.89  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E         36 QELQKKNTIVNLFGIVKDFTPSRQSlhGTKDWVTTVYLWDPT-CDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITL 114
Cdd:pfam02765   5 DKALAEGKVVNVIGVVIDASFPKKT--GGSDYCCTFTIVDPSlKGDSNDGLRVVFFRKNFEDLPIVKKVGDIILLHRVKI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1QZH_E        115 RSYRDRTQGLSKDQFRYAlWPDFSSNSK-DTLCPQPMPRLMKTGDKEEQFALLLNK 169
Cdd:pfam02765  83 QSFNGEPQGLANIGFSSS-WALFNGKLNrLYTPPILGSNFFEFSAEEKKYLESLRK 137
 
Name Accession Description Interval E-value
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-173 8.41e-38

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: 127.05  E-value: 8.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E          29 FQSIRSSQELQKKntIVNLFGIVKDFTPSRQSlHGTkDWVTTVYLWDPTCDtSSIGLQIHLFSKQGNDLPVIKQVGQPLL 108
Cdd:smart00976   1 FTPIKDLTSATNK--YVNVIGVVVDFKPPKRS-RGT-DFTCTLTITDPSYA-DGYGLTVKLFSPTLESLPVIKYVGDIIL 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
1QZH_E         109 LHQITLRSYRDRTQGLSKdqFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLnKIWDE 173
Cdd:smart00976  76 LHRVKIQDFNNRIQGLCS--FGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQYVEEL-RNWAF 137
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 28-172 1.06e-35

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: 121.61  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E       28 TFQSIRSSQElqKKNTIVNLFGIVKDFTPSRQSlhGTKDWVTTVYLWDPTCDTSSiGLQIHLFSKQGNDLPVIKqVGQPL 107
Cdd:cd04497   2 KYTPLSSALK--ESGGSVNVIGVVVDAGPPVRS--KGTDYCCTLTITDPSLANSD-GLTVKLFRPNEESLPIVK-VGDII 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1QZH_E      108 LLHQITLRSYRDRTQGLSKD-QFRYALWPDFSSNSKDtlcPQPMPRLMKTGDKEEQFALLLNKIWD 172
Cdd:cd04497  76 LLRRVKIQSYNGKPQGISNDrGSSWAVFRGDDGVVPI---PQQSSKPVEFGPEEEPSVEELRKWAS 138
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 36-169 1.56e-27

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: 100.89  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E         36 QELQKKNTIVNLFGIVKDFTPSRQSlhGTKDWVTTVYLWDPT-CDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITL 114
Cdd:pfam02765   5 DKALAEGKVVNVIGVVIDASFPKKT--GGSDYCCTFTIVDPSlKGDSNDGLRVVFFRKNFEDLPIVKKVGDIILLHRVKI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1QZH_E        115 RSYRDRTQGLSKDQFRYAlWPDFSSNSK-DTLCPQPMPRLMKTGDKEEQFALLLNK 169
Cdd:pfam02765  83 QSFNGEPQGLANIGFSSS-WALFNGKLNrLYTPPILGSNFFEFSAEEKKYLESLRK 137
RPA2_OBF_family cd03524
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold ...
 46-127 3.95e-05

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: 40.42  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QZH_E       46 NLFGIVKDFTPSRqslhgTKDWVTTVYLWDPTCDTssigLQIHLFSKQGNDLPVIKQVGQPLLLHqITLRSYRDRTQGLS 125
Cdd:cd03524   1 TIVGIVVAVEEIR-----TEGKVLIFTLTDGTGGT----IRVTLFGELAEELENLLKEGQVVYIK-GKVKKFRGRLQLIV 70


                ..
1QZH_E      126 KD 127
Cdd:cd03524  71 ES 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH