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Conserved domains on  [gi|325090575|gb|EGC43885|]
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telomere-binding alpha subunit central domain-containing protein [Histoplasma capsulatum var. duboisii H88]

Protein Classification

single-stranded DNA-binding protein( domain architecture ID 11137175)

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 ...
 188-340 4.26e-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: 4.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575  188 IRDLSCGTFVDLVVQVVKTYAEDYQRFLLYVTDYTQNKQLFNYTAEEGGPRDGDEYGYTSRSKRtWPGPYGQMTLQVTLW 267
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKPRIGK-WIGPFGKLTLQITLY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325090575  268 EPHSYYARQNVKENDFVLLQNVNIKMGRVSGAMEGSLHTDRRFPEKVQVIPINDNdSDEDVKKLVKRKIDYWK 340
Cdd:pfam16686  80 DPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVIDDN-NDPRLKELKRRKREYEK 151
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 9-149 1.44e-24

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: 99.74  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575    9 FDDIQTVkSKPGRVVNVIAVVVDALPPKLSGGDSYTSTFTLKDHDFSGETWNGLKIRYFQRCESDLPAPQQ-GDVVLLRQ 87
Cdd:pfam02765   1 FVDLDKA-LAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDSNDGLRVVFFRKNFEDLPIVKKvGDIILLHR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325090575   88 IKLRPYQGAVIGLCTQQDFSPWIIFRQGSNPKVSPQvIMCPGTRELMATEKSYALSLIGAAS 149
Cdd:pfam02765  80 VKIQSFNGEPQGLANIGFSSSWALFNGKLNRLYTPP-ILGSNFFEFSAEEKKYLESLRKWAE 140
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 188-340 4.26e-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: 4.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575  188 IRDLSCGTFVDLVVQVVKTYAEDYQRFLLYVTDYTQNKQLFNYTAEEGGPRDGDEYGYTSRSKRtWPGPYGQMTLQVTLW 267
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKPRIGK-WIGPFGKLTLQITLY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325090575  268 EPHSYYARQNVKENDFVLLQNVNIKMGRVSGAMEGSLHTDRRFPEKVQVIPINDNdSDEDVKKLVKRKIDYWK 340
Cdd:pfam16686  80 DPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVIDDN-NDPRLKELKRRKREYEK 151
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 9-149 1.44e-24

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: 99.74  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575    9 FDDIQTVkSKPGRVVNVIAVVVDALPPKLSGGDSYTSTFTLKDHDFSGETWNGLKIRYFQRCESDLPAPQQ-GDVVLLRQ 87
Cdd:pfam02765   1 FVDLDKA-LAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDSNDGLRVVFFRKNFEDLPIVKKvGDIILLHR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325090575   88 IKLRPYQGAVIGLCTQQDFSPWIIFRQGSNPKVSPQvIMCPGTRELMATEKSYALSLIGAAS 149
Cdd:pfam02765  80 VKIQSFNGEPQGLANIGFSSSWALFNGKLNRLYTPP-ILGSNFFEFSAEEKKYLESLRKWAE 140
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 31-130 3.46e-19

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: 84.25  E-value: 3.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575  31 DALPPKLSGGDSYTSTFTLKDHDFsgETWNGLKIRYFQRCESDLPAPQQGDVVLLRQIKLRPYQGAVIGLCTqQDFSPWI 110
Cdd:cd04497   25 DAGPPVRSKGTDYCCTLTITDPSL--ANSDGLTVKLFRPNEESLPIVKVGDIILLRRVKIQSYNGKPQGISN-DRGSSWA 101

                         90       100
                 ....*....|....*....|
gi 325090575 111 IFRQGSNPKVSPQVIMCPGT 130
Cdd:cd04497  102 VFRGDDGVVPIPQQSSKPVE 121
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 196-295 6.76e-10

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: 57.04  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575 196 FVDLVVQVVKTYAEDYQRFLLYVTDYTQNK-QLFNYTAEEGGPRDGDEYGytsrsKRTWPGPyGQMTLQVTLWEPHSYYA 274
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPpPLRKVKVEDDVVLEGDRSL-----KHREEGG-KQLTIDILVYDNHVELA 74

                         90       100
                 ....*....|....*....|.
gi 325090575 275 RQnVKENDFVLLQNVNIKMGR 295
Cdd:cd04498   75 KS-LKPGDFVRIYNVHAKSYS 94
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 9-144 3.06e-07

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: 50.01  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575     9 FDDIQTVKSKPGRVVNVIAVVVDALPPKLSGGDSYTSTFTLKDHDFSGETwnGLKIRYFQRCESDLPA-PQQGDVVLLRQ 87
Cdd:smart00976   1 FTPIKDLTSATNKYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADGY--GLTVKLFSPTLESLPViKYVGDIILLHR 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 325090575    88 IKLRPYQGAVIGLCTqQDFSPWIIFRqGSNPKVSPQVImCPGTRELMATEKSYALSL 144
Cdd:smart00976  79 VKIQDFNNRIQGLCS-FGTSSWAVFG-PLNGVVRERES-SPPSTFTPEDEKQYVEEL 132
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 188-340 4.26e-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: 4.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575  188 IRDLSCGTFVDLVVQVVKTYAEDYQRFLLYVTDYTQNKQLFNYTAEEGGPRDGDEYGYTSRSKRtWPGPYGQMTLQVTLW 267
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKPRIGK-WIGPFGKLTLQITLY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325090575  268 EPHSYYARQNVKENDFVLLQNVNIKMGRVSGAMEGSLHTDRRFPEKVQVIPINDNdSDEDVKKLVKRKIDYWK 340
Cdd:pfam16686  80 DPHASFARENLKPGDFVRLRNVHIKYGRNGLNLEGVLHGDRGYGRGIIVLVIDDN-NDPRLKELKRRKREYEK 151
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 9-149 1.44e-24

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: 99.74  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575    9 FDDIQTVkSKPGRVVNVIAVVVDALPPKLSGGDSYTSTFTLKDHDFSGETWNGLKIRYFQRCESDLPAPQQ-GDVVLLRQ 87
Cdd:pfam02765   1 FVDLDKA-LAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSLKGDSNDGLRVVFFRKNFEDLPIVKKvGDIILLHR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325090575   88 IKLRPYQGAVIGLCTQQDFSPWIIFRQGSNPKVSPQvIMCPGTRELMATEKSYALSLIGAAS 149
Cdd:pfam02765  80 VKIQSFNGEPQGLANIGFSSSWALFNGKLNRLYTPP-ILGSNFFEFSAEEKKYLESLRKWAE 140
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 31-130 3.46e-19

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: 84.25  E-value: 3.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575  31 DALPPKLSGGDSYTSTFTLKDHDFsgETWNGLKIRYFQRCESDLPAPQQGDVVLLRQIKLRPYQGAVIGLCTqQDFSPWI 110
Cdd:cd04497   25 DAGPPVRSKGTDYCCTLTITDPSL--ANSDGLTVKLFRPNEESLPIVKVGDIILLRRVKIQSYNGKPQGISN-DRGSSWA 101

                         90       100
                 ....*....|....*....|
gi 325090575 111 IFRQGSNPKVSPQVIMCPGT 130
Cdd:cd04497  102 VFRGDDGVVPIPQQSSKPVE 121
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 196-295 6.76e-10

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: 57.04  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575 196 FVDLVVQVVKTYAEDYQRFLLYVTDYTQNK-QLFNYTAEEGGPRDGDEYGytsrsKRTWPGPyGQMTLQVTLWEPHSYYA 274
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPpPLRKVKVEDDVVLEGDRSL-----KHREEGG-KQLTIDILVYDNHVELA 74

                         90       100
                 ....*....|....*....|.
gi 325090575 275 RQnVKENDFVLLQNVNIKMGR 295
Cdd:cd04498   75 KS-LKPGDFVRIYNVHAKSYS 94
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 9-144 3.06e-07

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: 50.01  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325090575     9 FDDIQTVKSKPGRVVNVIAVVVDALPPKLSGGDSYTSTFTLKDHDFSGETwnGLKIRYFQRCESDLPA-PQQGDVVLLRQ 87
Cdd:smart00976   1 FTPIKDLTSATNKYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADGY--GLTVKLFSPTLESLPViKYVGDIILLHR 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 325090575    88 IKLRPYQGAVIGLCTqQDFSPWIIFRqGSNPKVSPQVImCPGTRELMATEKSYALSL 144
Cdd:smart00976  79 VKIQDFNNRIQGLCS-FGTSSWAVFG-PLNGVVRERES-SPPSTFTPEDEKQYVEEL 132
 
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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