TEBA_STENO
ID TEBA_STENO Reviewed; 495 AA.
AC P29549;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Telomere-binding protein subunit alpha;
DE AltName: Full=TEBP alpha;
DE AltName: Full=Telomere-binding protein 56 kDa subunit;
GN Name=MAC-56A;
GN and
GN Name=MAC-56K;
GN and
GN Name=MAC-56S;
OS Sterkiella nova (Ciliate) (Oxytricha nova).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Sterkiella.
OX NCBI_TaxID=200597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1840510; DOI=10.1016/0092-8674(91)90075-a;
RA Gray J.T., Celander D.W., Price C.M., Cech T.R.;
RT "Cloning and expression of genes for the Oxytricha telomere-binding
RT protein: specific subunit interactions in the telomeric complex.";
RL Cell 67:807-814(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1577273; DOI=10.1101/gad.6.5.788;
RA Mitcham J.L., Lynn A.J., Prescott D.M.;
RT "Analysis of a scrambled gene: the gene encoding alpha-telomere-binding
RT protein in Oxytricha nova.";
RL Genes Dev. 6:788-800(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9875850; DOI=10.1016/s0092-8674(00)81720-1;
RA Horvath M.P., Schweiker V.L., Bevilacqua J.M., Ruggles J.A., Schultz S.C.;
RT "Crystal structure of the Oxytricha nova telomere end binding protein
RT complexed with single strand DNA.";
RL Cell 95:963-974(1998).
CC -!- FUNCTION: May function as protective capping of the single-stranded
CC telomeric overhang. May also participate in telomere length regulation
CC during DNA replication. Binds specifically to the T4G4-containing
CC extension on the 3'strand and protects this region of the telomere from
CC nuclease digestion and chemical modification.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
CC -!- MISCELLANEOUS: The sequence of the A (or alanine) version is shown. The
CC S (or serine) version differs in only two positions, and the K version
CC in only one. There may be other versions in addition to the S, A, and K
CC versions.
CC -!- SIMILARITY: Belongs to the telombin family. {ECO:0000305}.
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DR EMBL; M68931; AAA29398.1; -; Genomic_DNA.
DR EMBL; M68930; AAA29399.1; -; Genomic_DNA.
DR EMBL; X59724; CAA42409.1; -; Genomic_DNA.
DR PIR; A41221; A41221.
DR PDB; 1JB7; X-ray; 1.86 A; A=1-495.
DR PDB; 1K8G; X-ray; 2.60 A; A/B/C=1-320.
DR PDB; 1KIX; X-ray; 2.70 A; A=1-495.
DR PDB; 1OTC; X-ray; 2.80 A; A=1-495.
DR PDB; 1PA6; X-ray; 2.45 A; A=36-495.
DR PDB; 1PH1; X-ray; 2.51 A; A=35-495.
DR PDB; 1PH2; X-ray; 3.10 A; A=36-494.
DR PDB; 1PH3; X-ray; 2.30 A; A=36-495.
DR PDB; 1PH4; X-ray; 2.30 A; A=36-495.
DR PDB; 1PH5; X-ray; 2.30 A; A=36-494.
DR PDB; 1PH6; X-ray; 2.10 A; A=35-495.
DR PDB; 1PH7; X-ray; 2.90 A; A=36-495.
DR PDB; 1PH8; X-ray; 2.36 A; A=36-495.
DR PDB; 1PH9; X-ray; 2.50 A; A=36-495.
DR PDB; 1PHJ; X-ray; 2.50 A; A=35-495.
DR PDB; 2I0Q; X-ray; 1.91 A; A=1-495.
DR PDBsum; 1JB7; -.
DR PDBsum; 1K8G; -.
DR PDBsum; 1KIX; -.
DR PDBsum; 1OTC; -.
DR PDBsum; 1PA6; -.
DR PDBsum; 1PH1; -.
DR PDBsum; 1PH2; -.
DR PDBsum; 1PH3; -.
DR PDBsum; 1PH4; -.
DR PDBsum; 1PH5; -.
DR PDBsum; 1PH6; -.
DR PDBsum; 1PH7; -.
DR PDBsum; 1PH8; -.
DR PDBsum; 1PH9; -.
DR PDBsum; 1PHJ; -.
DR PDBsum; 2I0Q; -.
DR AlphaFoldDB; P29549; -.
DR SMR; P29549; -.
DR DIP; DIP-6194N; -.
DR MINT; P29549; -.
DR EvolutionaryTrace; P29549; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0000782; C:telomere cap complex; IMP:CAFA.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IMP:CAFA.
DR GO; GO:0016233; P:telomere capping; IMP:CAFA.
DR Gene3D; 2.40.50.140; -; 3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR028389; POT1.
DR InterPro; IPR011564; Telomer_end-bd_POT1/Cdc13.
DR InterPro; IPR003415; Telomere-bd_alpha.
DR PANTHER; PTHR14513; PTHR14513; 2.
DR Pfam; PF02765; POT1; 2.
DR PIRSF; PIRSF015848; TEBP_alpha; 1.
DR SMART; SM00976; Telo_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Telomere.
FT CHAIN 1..495
FT /note="Telomere-binding protein subunit alpha"
FT /id="PRO_0000121735"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 21
FT /note="A -> S (in K version)"
FT VARIANT 311
FT /note="A -> S (in S version)"
FT VARIANT 456
FT /note="D -> E (in S version)"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1PH8"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2I0Q"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1PH6"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1OTC"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1OTC"
FT STRAND 224..235
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2I0Q"
FT STRAND 287..299
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1OTC"
FT HELIX 350..355
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 367..382
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1PH3"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 408..418
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 425..434
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1PH2"
FT TURN 439..444
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 455..469
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1KIX"
FT STRAND 473..482
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 485..493
FT /evidence="ECO:0007829|PDB:1JB7"
SQ SEQUENCE 495 AA; 56082 MW; 9FD3CD40E623359B CRC64;
MSTAAKQNRS TSRVSKKKTA APKEGAAKKS DKGHKYEYVE LAKASLTSAQ PQHFYAVVID
ATFPYKTNQE RYICSLKIVD PTLYLKQQKG AGDASDYATL VLYAKRFEDL PIIHRAGDII
RVHRATLRLY NGQRQFNANV FYSSSWALFS TDKRSVTQEI NNQDAVSDTT PFSFSSKHAT
IEKNEISILQ NLRKWANQYF SSYSVISSDM YTALNKAQAQ KGDFDVVAKI LQVHELDEYT
NELKLKDASG QVFYTLSLKL KFPHVRTGEV VRIRSATYDE TSTQKKVLIL SHYSNIITFI
QSSKLAKELR AKIQDDHSVE VASLKKNVSL NAVVLTEVDK KHAALPSTSL QDLFHHADSD
KELQAQDTFR TQFYVTKIEP SDVKEWVKGY DRKTKKSSSL KGASGKGDNI FQVQFLVKDA
STQLNNNTYR VLLYTQDGLG ANFFNVKADN LHKNADARKK LEDSAELLTK FNSYVDAVVE
RRNGFYLIKD TKLIY
