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Conserved domains on  [gi|393906012|gb|EJD74141|]
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hypothetical protein LOAG_18501 [Loa loa]

Protein Classification

hPOT1_OB1_like and POT1PC domain-containing protein( domain architecture ID 11137175)

hPOT1_OB1_like and POT1PC domain-containing protein

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 ...
199-339 3.56e-30

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: 116.22  E-value: 3.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012  199 LNEFFLGGYNDITVQAIALFIDDRNNVILRCWDTTSPPRkiFVLNPEFINKVIYRDGKMEMTAV--------NYWCDIVL 270
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPP--LFLYVSPEDGDFRGDDDDFKPRIgkwigpfgKLTLQITL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393906012  271 YEEHGDFARNNVKCGDILLLINIHL-YHSLNGA-AFAMHGGRRYNRSIIIL---DDNNKLKLDLLRNIDEFNAK 339
Cdd:pfam16686  79 YDPHASFARENLKPGDFVRLRNVHIkYGRNGLNlEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKREYEKT 152
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
25-149 1.29e-10

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: 59.68  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012   25 VNIYAYV--AHLKIRSRSTDVSEDALVITQlelrDGSLDTDT--TCIIYSEPLESFSSQIQSGQIIRMHRAKIRKMtNGE 100
Cdd:pfam02765  14 VNVIGVVidASFPKKTGGSDYCCTFTIVDP----SLKGDSNDglRVVFFRKNFEDLPIVKKVGDIILLHRVKIQSF-NGE 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 393906012  101 -LFIYGKLKTVGFAvlLFSGRLGDSFTPIYQSSAKFTIASDYEDRINSLR 149
Cdd:pfam02765  89 pQGLANIGFSSSWA--LFNGKLNRLYTPPILGSNFFEFSAEEKKYLESLR 136
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
199-339 3.56e-30

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: 116.22  E-value: 3.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012  199 LNEFFLGGYNDITVQAIALFIDDRNNVILRCWDTTSPPRkiFVLNPEFINKVIYRDGKMEMTAV--------NYWCDIVL 270
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPP--LFLYVSPEDGDFRGDDDDFKPRIgkwigpfgKLTLQITL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393906012  271 YEEHGDFARNNVKCGDILLLINIHL-YHSLNGA-AFAMHGGRRYNRSIIIL---DDNNKLKLDLLRNIDEFNAK 339
Cdd:pfam16686  79 YDPHASFARENLKPGDFVRLRNVHIkYGRNGLNlEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKREYEKT 152
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
25-149 1.29e-10

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: 59.68  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012   25 VNIYAYV--AHLKIRSRSTDVSEDALVITQlelrDGSLDTDT--TCIIYSEPLESFSSQIQSGQIIRMHRAKIRKMtNGE 100
Cdd:pfam02765  14 VNVIGVVidASFPKKTGGSDYCCTFTIVDP----SLKGDSNDglRVVFFRKNFEDLPIVKKVGDIILLHRVKIQSF-NGE 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 393906012  101 -LFIYGKLKTVGFAvlLFSGRLGDSFTPIYQSSAKFTIASDYEDRINSLR 149
Cdd:pfam02765  89 pQGLANIGFSSSWA--LFNGKLNRLYTPPILGSNFFEFSAEEKKYLESLR 136
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
6-150 1.58e-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: 50.78  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012     6 YITLAELRELSHTadenfKVNIYAYVAHLK--IRSRSTDVSEdALVITQLELRDGSLdtdTTCIIYSEPLESFSSQIQSG 83
Cdd:smart00976   1 FTPIKDLTSATNK-----YVNVIGVVVDFKppKRSRGTDFTC-TLTITDPSYADGYG---LTVKLFSPTLESLPVIKYVG 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393906012    84 QIIRMHRAKIRKMtNGELFIygkLKTVGFAVLLFSGRLGDSFTPIYQSSAKFTIASDYEDRINSLRI 150
Cdd:smart00976  72 DIILLHRVKIQDF-NNRIQG---LCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQYVEELRN 134
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
4-142 1.38e-06

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: 48.04  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012   4 YHYITLAELRELSHTadenfKVNIYAYV--AHLKIRSRSTDvsedaLVITqLELRDGSLDTDT--TCIIYSEPLESFSsQ 79
Cdd:cd04497    1 YKYTPLSSALKESGG-----SVNVIGVVvdAGPPVRSKGTD-----YCCT-LTITDPSLANSDglTVKLFRPNEESLP-I 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393906012  80 IQSGQIIRMHRAKIRKMtNGElfIYGKLKTVGFAVLLFSGRlgDSFTPIYQSSAKFTIASDYE 142
Cdd:cd04497   69 VKVGDIILLRRVKIQSY-NGK--PQGISNDRGSSWAVFRGD--DGVVPIPQQSSKPVEFGPEE 126
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
207-319 1.13e-04

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: 42.41  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012 207 YNDITVQAIALFIDDRNNVILRCWDTTSPPRKIF-VLNPEFIN-------KVIYRDGKmEMTAvnywcDIVLYEEHGDFA 278
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRkVKVEDDVVlegdrslKHREEGGK-QLTI-----DILVYDNHVELA 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 393906012 279 RnNVKCGDILLLINIHL-YHSLNGAAFAM--------HGGRRYNRSIIIL 319
Cdd:cd04498   75 K-SLKPGDFVRIYNVHAkSYSSKNEHDENdhlhfhlvHGGTEYGRGIRVL 123
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
199-339 3.56e-30

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: 116.22  E-value: 3.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012  199 LNEFFLGGYNDITVQAIALFIDDRNNVILRCWDTTSPPRkiFVLNPEFINKVIYRDGKMEMTAV--------NYWCDIVL 270
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPP--LFLYVSPEDGDFRGDDDDFKPRIgkwigpfgKLTLQITL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393906012  271 YEEHGDFARNNVKCGDILLLINIHL-YHSLNGA-AFAMHGGRRYNRSIIIL---DDNNKLKLDLLRNIDEFNAK 339
Cdd:pfam16686  79 YDPHASFARENLKPGDFVRLRNVHIkYGRNGLNlEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKREYEKT 152
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
25-149 1.29e-10

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: 59.68  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012   25 VNIYAYV--AHLKIRSRSTDVSEDALVITQlelrDGSLDTDT--TCIIYSEPLESFSSQIQSGQIIRMHRAKIRKMtNGE 100
Cdd:pfam02765  14 VNVIGVVidASFPKKTGGSDYCCTFTIVDP----SLKGDSNDglRVVFFRKNFEDLPIVKKVGDIILLHRVKIQSF-NGE 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 393906012  101 -LFIYGKLKTVGFAvlLFSGRLGDSFTPIYQSSAKFTIASDYEDRINSLR 149
Cdd:pfam02765  89 pQGLANIGFSSSWA--LFNGKLNRLYTPPILGSNFFEFSAEEKKYLESLR 136
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
6-150 1.58e-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: 50.78  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012     6 YITLAELRELSHTadenfKVNIYAYVAHLK--IRSRSTDVSEdALVITQLELRDGSLdtdTTCIIYSEPLESFSSQIQSG 83
Cdd:smart00976   1 FTPIKDLTSATNK-----YVNVIGVVVDFKppKRSRGTDFTC-TLTITDPSYADGYG---LTVKLFSPTLESLPVIKYVG 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393906012    84 QIIRMHRAKIRKMtNGELFIygkLKTVGFAVLLFSGRLGDSFTPIYQSSAKFTIASDYEDRINSLRI 150
Cdd:smart00976  72 DIILLHRVKIQDF-NNRIQG---LCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQYVEELRN 134
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
4-142 1.38e-06

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: 48.04  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012   4 YHYITLAELRELSHTadenfKVNIYAYV--AHLKIRSRSTDvsedaLVITqLELRDGSLDTDT--TCIIYSEPLESFSsQ 79
Cdd:cd04497    1 YKYTPLSSALKESGG-----SVNVIGVVvdAGPPVRSKGTD-----YCCT-LTITDPSLANSDglTVKLFRPNEESLP-I 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393906012  80 IQSGQIIRMHRAKIRKMtNGElfIYGKLKTVGFAVLLFSGRlgDSFTPIYQSSAKFTIASDYE 142
Cdd:cd04497   69 VKVGDIILLRRVKIQSY-NGK--PQGISNDRGSSWAVFRGD--DGVVPIPQQSSKPVEFGPEE 126
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
207-319 1.13e-04

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: 42.41  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393906012 207 YNDITVQAIALFIDDRNNVILRCWDTTSPPRKIF-VLNPEFIN-------KVIYRDGKmEMTAvnywcDIVLYEEHGDFA 278
Cdd:cd04498    1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRkVKVEDDVVlegdrslKHREEGGK-QLTI-----DILVYDNHVELA 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 393906012 279 RnNVKCGDILLLINIHL-YHSLNGAAFAM--------HGGRRYNRSIIIL 319
Cdd:cd04498   75 K-SLKPGDFVRIYNVHAkSYSSKNEHDENdhlhfhlvHGGTEYGRGIRVL 123
 
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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