2M9V


Conserved Protein Domain Family
TPP1

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pfam10341: TPP1 
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Shelterin complex subunit, TPP1/ACD
TPP1 is a component of the telomerase holoenzyme, involved in telomere replication. It has been demonstrated that TPP1 dimerizes and binds to DNA and RNA. Furthermore, TPP1 stimulates the dissociation of RNA/DNA hetero-duplexes. Yeast telomerase protein TPP1 (Est3 in yeast) is a novel type of GTPase. The key residues in yeast EST3 are an Asp at residue 86 and the Arg at residue 110. The Asp is totally conserved in the family, whereas the Arg is not so well conserved. The N-terminal of TPP1 is likely to be the binding surface for TINF2, whereas the C-terminus probably binds to POT1, thereby tethering POT1 to the shelterin complex. The complex bound to telomeric DNA increases the activity and processivity of the human telomerase core enzyme, thus helping to maintain the length of the telomeres. This domain is conserved from fungi to mammals, hence family Telomere_Pot1 has been merged into the family. The human shelterin complex includes six proteins: telomere repeat binding factor 1 (TRF1), TRF2, repressor/activator protein 1 (RAP1), TRF1-interacting nuclear protein 2 (TIN2), TIN2-interacting protein 1 (TPP1) and protection of telomeres 1 (POT1).
Statistics
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PSSM-Id: 402108
View PSSM: pfam10341
Aligned: 43 rows
Threshold Bit Score: 61.1738
Threshold Setting Gi: 229279160
Created: 21-May-2020
Updated: 7-Aug-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
2M9V_A                 9 PWIKALIEDNSEHDQYHpsghvipslt---------kqdlalphmsPTILTN--PCHFAKITK----------------F 61   Saccha...
XP_003853578           8 PWIADFVKNEIEAVLAWadrkkvksfvklendgrfsddgsnfrnavSSLEPEkdQLQLIKVLA----------------- 70   Zymose...
EEQ85467               6 PWIAPLVEAALCLCLG------------------------------QPLPEDvaLRNPLKLVDddsihrv---rvrdrkF 52   Blasto...
WGS:ABKH:PAAG_06378    6 PWIVLVVEAALCLCLG------------------------------QPLPDKlpLRNPLQLVEddnkvrv---rvkdrkI 52   Paraco...
XP_001537470           6 KWIAPLVEAALCSYLG------------------------------EPFPDEaaLRNSLKLVEddntlrv---rvgdqkL 52   Histop...
EEQ29629               6 SWIEPLVEAAIRQSID---------------------------------AEEssSKELGETVNdesnfri---pvkrpkC 49   Micros...
EGE06843               6 KWIEPLVATAISQSVD-------------------------------KDNLNpkPRELKPTVDdgnifri---pimrpkY 51   Tricho...
EFR04452               6 dWIEPLVEQAFRQSVD------------------------------TEAQKKpsCRELGKTIDdgsnfrt---pvkrpkY 52   Nanniz...
EFW15848               6 KWIHPHIQRALCLCLD-------------------------------DLPDDkdSRQNPKLSEprddgkyfrvgvfgsqV 54   Coccid...
EEP77472               6 dWVHAYVHEAISLGLD---------------------------------GPPnnRRIRAKLTNqgndgtccrvrvrgpqV 52   Uncino...
2M9V_A                62 YN-----VCDYKVYASIRDSSHQILVEFSQECVSNFE--RTHNCRITSETTNCLMIIGDADLVYVTNSRAMSHFKI 130  Saccharomy...
XP_003853578          71 --------AGNTVNAVLSDGQTCIKARLSDNAVEIFEsaLDDGEQLDLEVTGDVIRLKSFTIVTTAFGS---EEDY 135  Zymoseptor...
EEQ85467              53 VQvaewsPATGPVRGILSDSVTAISSTFSRESTESYR--RKTRKPLNRNTKGAIIKINEFDIVISHVKA----PPE 122  Blastomyce...
WGS:ABKH:PAAG_06378   53 VQvaqwsPPSQSIQGTLSDSLTTILGIFSKESTQRYQ--IKARKPLNSGTKGAILKIVEFEVVISYVRA---QTPQ 123  Paracoccid...
XP_001537470          53 VQvaqwsPDPEPIRGTLSDSVTTISSVFSRESTEIFL--KKARKRLTNNTRGAIIKINEFDIVISYARA---HSPE 123  Histoplasm...
EEQ29629              50 AQlvkwlAKEPVPRALLSDRFTKIHAIFSESSCLNYD--RENNSDFRKTLTGCILKISKFYITIGQSRT---APPE 120  Microsporu...
EGE06843              52 AQllewlPEAPTPQAILSDSHTFVPARFSERVCQNFN--WNNNSASRSNVTPCLLRIKQCEIIIAKSNR---FPPE 122  Trichophyt...
EFR04452              53 TQllewlPKTPTPQAVLSDGHTCIRARFSERVCQDFK--KENGSDIRSNPTPCLLRLSKLEITIAQLYT---SPPE 123  Nannizzia ...
EFW15848              55 VQvvkwqDSSSPIEALLSDSCTTIRGHLSNDAVAKYR--LERKTDVRANTRGALMKITDFEIVINKKKT---PAPS 125  Coccidioid...
EEP77472              53 AQiiqweDHQSRLRAVLSDSVSSIRGHFSDDAVAKYR--RENKSDIRAGTKGAVMKLANFDILITNQSHAVSvald 126  Uncinocarp...
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