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Conserved domains on  [gi|500260285|gb|EOO02974|]
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putative telomere-binding alpha subunit central domain-containing protein [Phaeoacremonium minimum UCRPA7]

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 ...
 197-371 1.13e-62

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: 205.58  E-value: 1.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  197 LKDVKDGKFADIIVQVVKEPYDLGDKMTLWVTDYTENPAFFHKTYDGVDDLVARERDGDPygytkkfnaktaksvspdLS 276
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKP------------------RI 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  277 QQWNGPFGKKTMQVTCWEPHASFIRSNIQMSEWVRLRNVQIKFGHNSANIEGFLREDRTFMGKMLVDILDPADdaemiDP 356
Cdd:pfam16686  63 GKWIGPFGKLTLQITLYDPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVIDDNN-----DP 137

                         170
                  ....*....|....*
gi 500260285  357 RFKEAIRRKRDYERE 371
Cdd:pfam16686 138 RLKELKRRKREYEKT 152
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 23-136 2.27e-23

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: 96.19  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  23 SNFTSIKDILDEQvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTeEDNDGVNVNIFRPEKE-MPHFNAGDIVM 101
Cdd:cd04497    1 YKYTPLSSALKES---GGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSL-ANSDGLTVKLFRPNEEsLPIVKVGDIIL 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 500260285 102 VLMVKVQKWNGSLSLLTNF-NTDIHVYDGSKIPKPP 136
Cdd:cd04497   77 LRRVKIQSYNGKPQGISNDrGSSWAVFRGDDGVVPI 112
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 197-371 1.13e-62

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: 205.58  E-value: 1.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  197 LKDVKDGKFADIIVQVVKEPYDLGDKMTLWVTDYTENPAFFHKTYDGVDDLVARERDGDPygytkkfnaktaksvspdLS 276
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKP------------------RI 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  277 QQWNGPFGKKTMQVTCWEPHASFIRSNIQMSEWVRLRNVQIKFGHNSANIEGFLREDRTFMGKMLVDILDPADdaemiDP 356
Cdd:pfam16686  63 GKWIGPFGKLTLQITLYDPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVIDDNN-----DP 137

                         170
                  ....*....|....*
gi 500260285  357 RFKEAIRRKRDYERE 371
Cdd:pfam16686 138 RLKELKRRKREYEKT 152
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 23-136 2.27e-23

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: 96.19  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  23 SNFTSIKDILDEQvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTeEDNDGVNVNIFRPEKE-MPHFNAGDIVM 101
Cdd:cd04497    1 YKYTPLSSALKES---GGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSL-ANSDGLTVKLFRPNEEsLPIVKVGDIIL 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 500260285 102 VLMVKVQKWNGSLSLLTNF-NTDIHVYDGSKIPKPP 136
Cdd:cd04497   77 LRRVKIQSYNGKPQGISNDrGSSWAVFRGDDGVVPI 112
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 25-120 8.41e-15

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: 72.00  E-value: 8.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285   25 FTSIKDILDEqvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTEED-NDGVNVNIFRPEKE-MPH-FNAGDIVM 101
Cdd:pfam02765   1 FVDLDKALAE----GKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDsNDGLRVVFFRKNFEdLPIvKKVGDIIL 76

                          90
                  ....*....|....*....
gi 500260285  102 VLMVKVQKWNGSLSLLTNF 120
Cdd:pfam02765  77 LHRVKIQSFNGEPQGLANI 95
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 25-168 2.37e-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: 70.42  E-value: 2.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285    25 FTSIKDILDEQvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTeEDNDGVNVNIFRPEKE-MPH-FNAGDIVMV 102
Cdd:smart00976   1 FTPIKDLTSAT---NKYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSY-ADGYGLTVKLFSPTLEsLPViKYVGDIILL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500260285   103 LMVKVQKWNGSLSLLTNFNTDIHVYDGskipkpPKSAFAALREPRGRVKREPNaKEHEYVSWMYQQ 168
Cdd:smart00976  77 HRVKIQDFNNRIQGLCSFGTSSWAVFG------PLNGVVRERESSPPSTFTPE-DEKQYVEELRNW 135
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 197-371 1.13e-62

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: 205.58  E-value: 1.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  197 LKDVKDGKFADIIVQVVKEPYDLGDKMTLWVTDYTENPAFFHKTYDGVDDLVARERDGDPygytkkfnaktaksvspdLS 276
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKP------------------RI 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  277 QQWNGPFGKKTMQVTCWEPHASFIRSNIQMSEWVRLRNVQIKFGHNSANIEGFLREDRTFMGKMLVDILDPADdaemiDP 356
Cdd:pfam16686  63 GKWIGPFGKLTLQITLYDPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVIDDNN-----DP 137

                         170
                  ....*....|....*
gi 500260285  357 RFKEAIRRKRDYERE 371
Cdd:pfam16686 138 RLKELKRRKREYEKT 152
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 23-136 2.27e-23

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: 96.19  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  23 SNFTSIKDILDEQvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTeEDNDGVNVNIFRPEKE-MPHFNAGDIVM 101
Cdd:cd04497    1 YKYTPLSSALKES---GGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSL-ANSDGLTVKLFRPNEEsLPIVKVGDIIL 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 500260285 102 VLMVKVQKWNGSLSLLTNF-NTDIHVYDGSKIPKPP 136
Cdd:cd04497   77 LRRVKIQSYNGKPQGISNDrGSSWAVFRGDDGVVPI 112
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 25-120 8.41e-15

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: 72.00  E-value: 8.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285   25 FTSIKDILDEqvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTEED-NDGVNVNIFRPEKE-MPH-FNAGDIVM 101
Cdd:pfam02765   1 FVDLDKALAE----GKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDsNDGLRVVFFRKNFEdLPIvKKVGDIIL 76

                          90
                  ....*....|....*....
gi 500260285  102 VLMVKVQKWNGSLSLLTNF 120
Cdd:pfam02765  77 LHRVKIQSFNGEPQGLANI 95
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 25-168 2.37e-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: 70.42  E-value: 2.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285    25 FTSIKDILDEQvpvGRQVCVLGIVKDFRAPIATGRTDHKCTVTLYDESTeEDNDGVNVNIFRPEKE-MPH-FNAGDIVMV 102
Cdd:smart00976   1 FTPIKDLTSAT---NKYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSY-ADGYGLTVKLFSPTLEsLPViKYVGDIILL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500260285   103 LMVKVQKWNGSLSLLTNFNTDIHVYDGskipkpPKSAFAALREPRGRVKREPNaKEHEYVSWMYQQ 168
Cdd:smart00976  77 HRVKIQDFNNRIQGLCSFGTSSWAVFG------PLNGVVRERESSPPSTFTPE-DEKQYVEELRNW 135
RPA1_DBD_B cd04475
RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding ...
 44-119 3.25e-03

RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding domain (DBD)-B, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-B, RPA1 contains three other OB folds: DBD-A, DBD-C, and RPA1N. The major DNA binding activity of human RPA (hRPA) and Saccharomyces cerevisiae RPA (ScRPA) is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. Although ScRPA and the hRPA have similar ssDNA-binding properties, they differ functionally. Antibodies to hRPA do not cross-react with ScRPA, and null mutations in the ScRPA subunits are not complemented by corresponding human genes. Also, ScRPA cannot support Simian virus 40 (SV40) DNA replication in vitro, whereas human RPA can.


Pssm-ID: 239921 [Multi-domain]  Cd Length: 101  Bit Score: 37.56  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500260285  44 VLGIVKDFRAPI-----ATGRTDHKCTVTLYDESteedNDGVNVNIFRPEKEMPHFNAGDIVMVLMVKVQKWNG-SLSLL 117
Cdd:cd04475    4 VIGVVKSVGPVTtittkSTGRELDKREITLVDES----GHSVELTLWGEQAELFDGSENPVIAIKGVKVSEFNGkSLSTG 79


                 ..
gi 500260285 118 TN 119
Cdd:cd04475   80 SS 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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