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Conserved domains on  [gi|2115026345|gb|KAH2345124|]
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hypothetical protein KXV29_008547 [Sartorya fumigata]

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 ...
 187-340 2.42e-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: 203.27  E-value: 2.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345 187 IKDVEERTFVDLTGEVVKIFTNDSEKVALYLTDYTANEGLHNYTIDANNAREGDQFAYLSHpKRQWQGPAGRMTLQITLW 266
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKPR-IGKWIGPFGKLTLQITLY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2115026345 267 EPHASFAREHLKEGSFVRLRNVHIKRSRiEGSPLEGAMHCDRQNPDEMNIRLIDAKNDDRGRELLRRRKKYWES 340
Cdd:pfam16686  80 DPHASFARENLKPGDFVRLRNVHIKYGR-NGLNLEGVLHGDRGYGRGIIVLVIDDNNDPRLKELKRRKREYEKT 152
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 40-148 6.36e-30

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: 114.76  E-value: 6.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345  40 RSWCITFTLKDTDFgNGHVWDGLKIKYFKANQSQLPPV-RVHDVILLRNITITKFNGRPLGVAPDETTILWAIYRPEPGF 118
Cdd:pfam02765  32 SDYCCTFTIVDPSL-KGDSNDGLRVVFFRKNFEDLPIVkKVGDIILLHRVKIQSFNGEPQGLANIGFSSSWALFNGKLNR 110

                          90       100       110
                  ....*....|....*....|....*....|
gi 2115026345 119 VDISPICGPVPFEPSYSEKSYALSLIDKSS 148
Cdd:pfam02765 111 LYTPPILGSNFFEFSAEEKKYLESLRKWAE 140
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 187-340 2.42e-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: 203.27  E-value: 2.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345 187 IKDVEERTFVDLTGEVVKIFTNDSEKVALYLTDYTANEGLHNYTIDANNAREGDQFAYLSHpKRQWQGPAGRMTLQITLW 266
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKPR-IGKWIGPFGKLTLQITLY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2115026345 267 EPHASFAREHLKEGSFVRLRNVHIKRSRiEGSPLEGAMHCDRQNPDEMNIRLIDAKNDDRGRELLRRRKKYWES 340
Cdd:pfam16686  80 DPHASFARENLKPGDFVRLRNVHIKYGR-NGLNLEGVLHGDRGYGRGIIVLVIDDNNDPRLKELKRRKREYEKT 152
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 40-148 6.36e-30

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: 114.76  E-value: 6.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345  40 RSWCITFTLKDTDFgNGHVWDGLKIKYFKANQSQLPPV-RVHDVILLRNITITKFNGRPLGVAPDETTILWAIYRPEPGF 118
Cdd:pfam02765  32 SDYCCTFTIVDPSL-KGDSNDGLRVVFFRKNFEDLPIVkKVGDIILLHRVKIQSFNGEPQGLANIGFSSSWALFNGKLNR 110

                          90       100       110
                  ....*....|....*....|....*....|
gi 2115026345 119 VDISPICGPVPFEPSYSEKSYALSLIDKSS 148
Cdd:pfam02765 111 LYTPPILGSNFFEFSAEEKKYLESLRKWAE 140
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 32-142 1.21e-29

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: 113.91  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345  32 FGTPFQSSRSWCITFTLKDTDFGNghvWDGLKIKYFKANQSQLPPVRVHDVILLRNITITKFNGRPLGVAPDETTiLWAI 111
Cdd:cd04497    27 GPPVRSKGTDYCCTLTITDPSLAN---SDGLTVKLFRPNEESLPIVKVGDIILLRRVKIQSYNGKPQGISNDRGS-SWAV 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2115026345 112 YRPEPGFVDISPICGPVPF-----EPSYSEKSYALS 142
Cdd:cd04497   103 FRGDDGVVPIPQQSSKPVEfgpeeEPSVEELRKWAS 138
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-148 3.02e-22

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: 92.77  E-value: 3.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345   29 VDVFGTPFQSS-RSWCITFTLKDTDFGNGHvwdGLKIKYFKANQSQLPPVR-VHDVILLRNITITKFNGRPLGVApDETT 106
Cdd:smart00976  21 VVDFKPPKRSRgTDFTCTLTITDPSYADGY---GLTVKLFSPTLESLPVIKyVGDIILLHRVKIQDFNNRIQGLC-SFGT 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2115026345  107 ILWAIYRPEPGFVDISPICGPVPFEPSySEKSYALSLIDKSS 148
Cdd:smart00976  97 SSWAVFGPLNGVVRERESSPPSTFTPE-DEKQYVEELRNWAF 137
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 195-338 1.79e-16

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: 75.92  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345 195 FVDLTGEVVKIFTNDSEKVALYLTDYTAN-EGLHNYTIDANNAREGDQfaylSHpKRQWQGPaGRMTLQITLWEPHASFA 273
Cdd:cd04498     1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFpPPLRKVKVEDDVVLEGDR----SL-KHREEGG-KQLTIDILVYDNHVELA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2115026345 274 REhLKEGSFVRLRNVHIKRSrieGSPLEGAMHcdrqnpDEMNIRLIdaknddRGRELLRRRKKYW 338
Cdd:cd04498    75 KS-LKPGDFVRIYNVHAKSY---SSKNEHDEN------DHLHFHLV------HGGTEYGRGIRVL 123
 
Name Accession Description Interval E-value
POT1PC pfam16686
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
 187-340 2.42e-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: 203.27  E-value: 2.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345 187 IKDVEERTFVDLTGEVVKIFTNDSEKVALYLTDYTANEGLHNYTIDANNAREGDQFAYLSHpKRQWQGPAGRMTLQITLW 266
Cdd:pfam16686   1 LKDVQPGQFFDLIVQVVKKAYDDGGKVLLYVWDYTENPPLFLYVSPEDGDFRGDDDDFKPR-IGKWIGPFGKLTLQITLY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2115026345 267 EPHASFAREHLKEGSFVRLRNVHIKRSRiEGSPLEGAMHCDRQNPDEMNIRLIDAKNDDRGRELLRRRKKYWES 340
Cdd:pfam16686  80 DPHASFARENLKPGDFVRLRNVHIKYGR-NGLNLEGVLHGDRGYGRGIIVLVIDDNNDPRLKELKRRKREYEKT 152
POT1 pfam02765
Telomeric single stranded DNA binding POT1/CDC13; This domain binds single stranded telomeric ...
 40-148 6.36e-30

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: 114.76  E-value: 6.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345  40 RSWCITFTLKDTDFgNGHVWDGLKIKYFKANQSQLPPV-RVHDVILLRNITITKFNGRPLGVAPDETTILWAIYRPEPGF 118
Cdd:pfam02765  32 SDYCCTFTIVDPSL-KGDSNDGLRVVFFRKNFEDLPIVkKVGDIILLHRVKIQSFNGEPQGLANIGFSSSWALFNGKLNR 110

                          90       100       110
                  ....*....|....*....|....*....|
gi 2115026345 119 VDISPICGPVPFEPSYSEKSYALSLIDKSS 148
Cdd:pfam02765 111 LYTPPILGSNFFEFSAEEKKYLESLRKWAE 140
hPOT1_OB1_like cd04497
hPOT1_OB1_like: A subfamily of OB folds similar to the first OB fold (OB1) of human protection ...
 32-142 1.21e-29

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: 113.91  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345  32 FGTPFQSSRSWCITFTLKDTDFGNghvWDGLKIKYFKANQSQLPPVRVHDVILLRNITITKFNGRPLGVAPDETTiLWAI 111
Cdd:cd04497    27 GPPVRSKGTDYCCTLTITDPSLAN---SDGLTVKLFRPNEESLPIVKVGDIILLRRVKIQSYNGKPQGISNDRGS-SWAV 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2115026345 112 YRPEPGFVDISPICGPVPF-----EPSYSEKSYALS 142
Cdd:cd04497   103 FRGDDGVVPIPQQSSKPVEfgpeeEPSVEELRKWAS 138
Telo_bind smart00976
Telomeric single stranded DNA binding POT1/CDC13; The telomere-binding protein forms a ...
 29-148 3.02e-22

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: 92.77  E-value: 3.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345   29 VDVFGTPFQSS-RSWCITFTLKDTDFGNGHvwdGLKIKYFKANQSQLPPVR-VHDVILLRNITITKFNGRPLGVApDETT 106
Cdd:smart00976  21 VVDFKPPKRSRgTDFTCTLTITDPSYADGY---GLTVKLFSPTLESLPVIKyVGDIILLHRVKIQDFNNRIQGLC-SFGT 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2115026345  107 ILWAIYRPEPGFVDISPICGPVPFEPSySEKSYALSLIDKSS 148
Cdd:smart00976  97 SSWAVFGPLNGVVRERESSPPSTFTPE-DEKQYVEELRNWAF 137
hPOT1_OB2 cd04498
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
 195-338 1.79e-16

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: 75.92  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115026345 195 FVDLTGEVVKIFTNDSEKVALYLTDYTAN-EGLHNYTIDANNAREGDQfaylSHpKRQWQGPaGRMTLQITLWEPHASFA 273
Cdd:cd04498     1 YFDLLCQLLSVVETDSSSTLLKVWDGTKFpPPLRKVKVEDDVVLEGDR----SL-KHREEGG-KQLTIDILVYDNHVELA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2115026345 274 REhLKEGSFVRLRNVHIKRSrieGSPLEGAMHcdrqnpDEMNIRLIdaknddRGRELLRRRKKYW 338
Cdd:cd04498    75 KS-LKPGDFVRIYNVHAKSY---SSKNEHDEN------DHLHFHLV------HGGTEYGRGIRVL 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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