NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19527150|ref|NP_598692|]
View 

protection of telomeres protein 1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Pot1C cd20374
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a ...
349-635 3.09e-163

Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a hexameric nucleoprotein complex (comprising TRF1, TRF2, TIN2, RAP1, POT1 and TPP1 in humans) that protects telomeres, the physical ends of chromosomes. Shelterin protects against these ends being recognized as double-stranded DNA breaks, as well as against degradation of the telomeric overhang by endonucleases. It also helps control access of telomerase to the telomeric overhang, thereby affecting telomore length. This C-terminal region has an OB-fold domain and a holiday junction resolvase (HJR) domain which make dimer contacts with TPP1.


:

Pssm-ID: 380669  Cd Length: 286  Bit Score: 468.69  E-value: 3.09e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 349 LEKTPLCAILTQKAPQQYRVRAKLRSYLPRRLSQSVKLLCPKCHSVQEVPHGDSLDKILQDAATEAPdiklkaTSLYYSK 428
Cdd:cd20374   1 LEQTPLSEVKKSTPPQQYHVRAKLRSYQPQRLYQSVKLFCPKCKSLQEVPDEEALANIFQEAATDSP------TSWYSSE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 429 VWTTED-----QGGRQVAVHFVKNN-GILPASseCLILIEGGRLCEVSKLSSKFHSVMPVRSGPESLELLTLSAPFLIQG 502
Cdd:cd20374  75 VWTLTGsldsgQGGRKVAVHFVKNMmLQSPEK--ELIFIEGGTLEEICKLSKKFKNIIPVRSSEEDLTLLDLSAPFLFQG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 503 KVHHYGCKQCSSLKPIQNLNSRFHKGPWTPSSVAEALGVVPLQYVFVMVFTLDDGTGVLEAYL-KDSEHFFKIPASEVLT 581
Cdd:cd20374 153 KKRYYGCKQCSSPKSIENLSSLVEKESWDESSVAEALGIQLLQYVFLMKFTLDDGTGTLEALLwLDAEKFFQISASEVLT 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 19527150 582 DDDLQRSLETIMDMICPPGIKVDAYPWLECLLKSYNVTIGTERRICYQIFDTTV 635
Cdd:cd20374 233 DQELQEKIQMIMDTLCPPGISIDERPWLECCIKSYNVEDGGRNQVCYQIFDTTV 286
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
11-141 1.00e-45

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: 158.64  E-value: 1.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150     11 YTPLNLLKEGT--IANVYGVVKFFKPPYVSKGTDYCSVVTIVDQTNVK---LTCMLFSGNYEALPIIYKVGDIVRFHRLK 85
Cdd:smart00976   1 FTPIKDLTSATnkYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADgygLTVKLFSPTLESLPVIKYVGDIILLHRVK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19527150     86 IQVYKNELQGINCSGFASLTFEGTVGMPVTARTSSKVFSFTPQDQKM-VEALRVWAS 141
Cdd:smart00976  81 IQDFNNRIQGLCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQyVEELRNWAF 137
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
153-295 1.22e-43

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: 153.58  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150   153 LCDAQPMQYYDLTCQLLGKAQVDSTAFLLKVWDGTQTVLPSWRVSTQDLTFEGDL--------SHIERLQSLVVDILVYD 224
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDddfkprigKWIGPFGKLTLQITLYD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527150   225 NHVQVARS-IEVGCFLRLYSLHTKLQPGNsetsssesLRLEFHLHGGTSYGRGIRVL---PDTSPCVDQLKKALE 295
Cdd:pfam16686  81 PHASFAREnLKPGDFVRLRNVHIKYGRNG--------LNLEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKR 147
 
Name Accession Description Interval E-value
Pot1C cd20374
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a ...
349-635 3.09e-163

Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a hexameric nucleoprotein complex (comprising TRF1, TRF2, TIN2, RAP1, POT1 and TPP1 in humans) that protects telomeres, the physical ends of chromosomes. Shelterin protects against these ends being recognized as double-stranded DNA breaks, as well as against degradation of the telomeric overhang by endonucleases. It also helps control access of telomerase to the telomeric overhang, thereby affecting telomore length. This C-terminal region has an OB-fold domain and a holiday junction resolvase (HJR) domain which make dimer contacts with TPP1.


Pssm-ID: 380669  Cd Length: 286  Bit Score: 468.69  E-value: 3.09e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 349 LEKTPLCAILTQKAPQQYRVRAKLRSYLPRRLSQSVKLLCPKCHSVQEVPHGDSLDKILQDAATEAPdiklkaTSLYYSK 428
Cdd:cd20374   1 LEQTPLSEVKKSTPPQQYHVRAKLRSYQPQRLYQSVKLFCPKCKSLQEVPDEEALANIFQEAATDSP------TSWYSSE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 429 VWTTED-----QGGRQVAVHFVKNN-GILPASseCLILIEGGRLCEVSKLSSKFHSVMPVRSGPESLELLTLSAPFLIQG 502
Cdd:cd20374  75 VWTLTGsldsgQGGRKVAVHFVKNMmLQSPEK--ELIFIEGGTLEEICKLSKKFKNIIPVRSSEEDLTLLDLSAPFLFQG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 503 KVHHYGCKQCSSLKPIQNLNSRFHKGPWTPSSVAEALGVVPLQYVFVMVFTLDDGTGVLEAYL-KDSEHFFKIPASEVLT 581
Cdd:cd20374 153 KKRYYGCKQCSSPKSIENLSSLVEKESWDESSVAEALGIQLLQYVFLMKFTLDDGTGTLEALLwLDAEKFFQISASEVLT 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 19527150 582 DDDLQRSLETIMDMICPPGIKVDAYPWLECLLKSYNVTIGTERRICYQIFDTTV 635
Cdd:cd20374 233 DQELQEKIQMIMDTLCPPGISIDERPWLECCIKSYNVEDGGRNQVCYQIFDTTV 286
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
11-141 1.00e-45

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: 158.64  E-value: 1.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150     11 YTPLNLLKEGT--IANVYGVVKFFKPPYVSKGTDYCSVVTIVDQTNVK---LTCMLFSGNYEALPIIYKVGDIVRFHRLK 85
Cdd:smart00976   1 FTPIKDLTSATnkYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADgygLTVKLFSPTLESLPVIKYVGDIILLHRVK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19527150     86 IQVYKNELQGINCSGFASLTFEGTVGMPVTARTSSKVFSFTPQDQKM-VEALRVWAS 141
Cdd:smart00976  81 IQDFNNRIQGLCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQyVEELRNWAF 137
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
153-295 1.22e-43

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: 153.58  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150   153 LCDAQPMQYYDLTCQLLGKAQVDSTAFLLKVWDGTQTVLPSWRVSTQDLTFEGDL--------SHIERLQSLVVDILVYD 224
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDddfkprigKWIGPFGKLTLQITLYD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527150   225 NHVQVARS-IEVGCFLRLYSLHTKLQPGNsetsssesLRLEFHLHGGTSYGRGIRVL---PDTSPCVDQLKKALE 295
Cdd:pfam16686  81 PHASFAREnLKPGDFVRLRNVHIKYGRNG--------LNLEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKR 147
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
9-141 5.36e-41

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: 145.50  E-value: 5.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150   9 YTYTPLNLLKE--GTIANVYGVVKFFKPPYVSKGTDYCSVVTIVDQT---NVKLTCMLFSGNYEALPIIyKVGDIVRFHR 83
Cdd:cd04497   1 YKYTPLSSALKesGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSlanSDGLTVKLFRPNEESLPIV-KVGDIILLRR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19527150  84 LKIQVYKNELQGI-NCSGFASLTFEGTVGMPVTARTSSKVFSFTPQDQKMVEALRVWAS 141
Cdd:cd04497  80 VKIQSYNGKPQGIsNDRGSSWAVFRGDDGVVPIPQQSSKPVEFGPEEEPSVEELRKWAS 138
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
161-280 2.03e-37

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: 135.24  E-value: 2.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 161 YYDLTCQLLGKAQVDSTAFLLKVWDGTQTVLPSWRVSTQDLTF-EGDLSHIERLQS---LVVDILVYDNHVQVARSIEVG 236
Cdd:cd04498   1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRKVKVEDDVVlEGDRSLKHREEGgkqLTIDILVYDNHVELAKSLKPG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19527150 237 CFLRLYSLHTKlqPGNSETSSSESLRLEFHL-HGGTSYGRGIRVL 280
Cdd:cd04498  81 DFVRIYNVHAK--SYSSKNEHDENDHLHFHLvHGGTEYGRGIRVL 123
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
11-141 1.34e-35

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: 130.94  E-value: 1.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150    11 YTPLN-LLKEGTIANVYGVVKFFKPPYVSKGTDYCSVVTIVDQT-----NVKLTCMLFSGNYEALPIIYKVGDIVRFHRL 84
Cdd:pfam02765   1 FVDLDkALAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSlkgdsNDGLRVVFFRKNFEDLPIVKKVGDIILLHRV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150    85 KIQVYKNELQGINCSGFAS--LTFEGTVGMPVTA-RTSSKVFSFTPQDQKMVEALRVWAS 141
Cdd:pfam02765  81 KIQSFNGEPQGLANIGFSSswALFNGKLNRLYTPpILGSNFFEFSAEEKKYLESLRKWAE 140
 
Name Accession Description Interval E-value
Pot1C cd20374
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a ...
349-635 3.09e-163

Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a hexameric nucleoprotein complex (comprising TRF1, TRF2, TIN2, RAP1, POT1 and TPP1 in humans) that protects telomeres, the physical ends of chromosomes. Shelterin protects against these ends being recognized as double-stranded DNA breaks, as well as against degradation of the telomeric overhang by endonucleases. It also helps control access of telomerase to the telomeric overhang, thereby affecting telomore length. This C-terminal region has an OB-fold domain and a holiday junction resolvase (HJR) domain which make dimer contacts with TPP1.


Pssm-ID: 380669  Cd Length: 286  Bit Score: 468.69  E-value: 3.09e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 349 LEKTPLCAILTQKAPQQYRVRAKLRSYLPRRLSQSVKLLCPKCHSVQEVPHGDSLDKILQDAATEAPdiklkaTSLYYSK 428
Cdd:cd20374   1 LEQTPLSEVKKSTPPQQYHVRAKLRSYQPQRLYQSVKLFCPKCKSLQEVPDEEALANIFQEAATDSP------TSWYSSE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 429 VWTTED-----QGGRQVAVHFVKNN-GILPASseCLILIEGGRLCEVSKLSSKFHSVMPVRSGPESLELLTLSAPFLIQG 502
Cdd:cd20374  75 VWTLTGsldsgQGGRKVAVHFVKNMmLQSPEK--ELIFIEGGTLEEICKLSKKFKNIIPVRSSEEDLTLLDLSAPFLFQG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 503 KVHHYGCKQCSSLKPIQNLNSRFHKGPWTPSSVAEALGVVPLQYVFVMVFTLDDGTGVLEAYL-KDSEHFFKIPASEVLT 581
Cdd:cd20374 153 KKRYYGCKQCSSPKSIENLSSLVEKESWDESSVAEALGIQLLQYVFLMKFTLDDGTGTLEALLwLDAEKFFQISASEVLT 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 19527150 582 DDDLQRSLETIMDMICPPGIKVDAYPWLECLLKSYNVTIGTERRICYQIFDTTV 635
Cdd:cd20374 233 DQELQEKIQMIMDTLCPPGISIDERPWLECCIKSYNVEDGGRNQVCYQIFDTTV 286
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
11-141 1.00e-45

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: 158.64  E-value: 1.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150     11 YTPLNLLKEGT--IANVYGVVKFFKPPYVSKGTDYCSVVTIVDQTNVK---LTCMLFSGNYEALPIIYKVGDIVRFHRLK 85
Cdd:smart00976   1 FTPIKDLTSATnkYVNVIGVVVDFKPPKRSRGTDFTCTLTITDPSYADgygLTVKLFSPTLESLPVIKYVGDIILLHRVK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19527150     86 IQVYKNELQGINCSGFASLTFEGTVGMPVTARTSSKVFSFTPQDQKM-VEALRVWAS 141
Cdd:smart00976  81 IQDFNNRIQGLCSFGTSSWAVFGPLNGVVRERESSPPSTFTPEDEKQyVEELRNWAF 137
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
153-295 1.22e-43

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: 153.58  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150   153 LCDAQPMQYYDLTCQLLGKAQVDSTAFLLKVWDGTQTVLPSWRVSTQDLTFEGDL--------SHIERLQSLVVDILVYD 224
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDddfkprigKWIGPFGKLTLQITLYD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527150   225 NHVQVARS-IEVGCFLRLYSLHTKLQPGNsetsssesLRLEFHLHGGTSYGRGIRVL---PDTSPCVDQLKKALE 295
Cdd:pfam16686  81 PHASFAREnLKPGDFVRLRNVHIKYGRNG--------LNLEGVLHGDRGYGRGIIVLvidDNNDPRLKELKRRKR 147
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
9-141 5.36e-41

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: 145.50  E-value: 5.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150   9 YTYTPLNLLKE--GTIANVYGVVKFFKPPYVSKGTDYCSVVTIVDQT---NVKLTCMLFSGNYEALPIIyKVGDIVRFHR 83
Cdd:cd04497   1 YKYTPLSSALKesGGSVNVIGVVVDAGPPVRSKGTDYCCTLTITDPSlanSDGLTVKLFRPNEESLPIV-KVGDIILLRR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19527150  84 LKIQVYKNELQGI-NCSGFASLTFEGTVGMPVTARTSSKVFSFTPQDQKMVEALRVWAS 141
Cdd:cd04497  80 VKIQSYNGKPQGIsNDRGSSWAVFRGDDGVVPIPQQSSKPVEFGPEEEPSVEELRKWAS 138
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
161-280 2.03e-37

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: 135.24  E-value: 2.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150 161 YYDLTCQLLGKAQVDSTAFLLKVWDGTQTVLPSWRVSTQDLTF-EGDLSHIERLQS---LVVDILVYDNHVQVARSIEVG 236
Cdd:cd04498   1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFPPPLRKVKVEDDVVlEGDRSLKHREEGgkqLTIDILVYDNHVELAKSLKPG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19527150 237 CFLRLYSLHTKlqPGNSETSSSESLRLEFHL-HGGTSYGRGIRVL 280
Cdd:cd04498  81 DFVRIYNVHAK--SYSSKNEHDENDHLHFHLvHGGTEYGRGIRVL 123
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
11-141 1.34e-35

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: 130.94  E-value: 1.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150    11 YTPLN-LLKEGTIANVYGVVKFFKPPYVSKGTDYCSVVTIVDQT-----NVKLTCMLFSGNYEALPIIYKVGDIVRFHRL 84
Cdd:pfam02765   1 FVDLDkALAEGKVVNVIGVVIDASFPKKTGGSDYCCTFTIVDPSlkgdsNDGLRVVFFRKNFEDLPIVKKVGDIILLHRV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527150    85 KIQVYKNELQGINCSGFAS--LTFEGTVGMPVTA-RTSSKVFSFTPQDQKMVEALRVWAS 141
Cdd:pfam02765  81 KIQSFNGEPQGLANIGFSSswALFNGKLNRLYTPpILGSNFFEFSAEEKKYLESLRKWAE 140
RPA2_OBF_family cd03524
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold ...
24-99 3.00e-08

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: 50.82  E-value: 3.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527150  24 NVYGVVKFFKPPYVSKgtdYCSVVTIVDQTNVKLTCMLFSGNYEALPIIYKVGDIVRFHrLKIQVYKNELQGINCS 99
Cdd:cd03524   1 TIVGIVVAVEEIRTEG---KVLIFTLTDGTGGTIRVTLFGELAEELENLLKEGQVVYIK-GKVKKFRGRLQLIVES 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