TEBB_STENO
ID TEBB_STENO Reviewed; 385 AA.
AC P16458;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Telomere-binding protein subunit beta;
DE AltName: Full=TEBP beta;
DE AltName: Full=Telomere-binding protein 41 kDa subunit;
GN Name=MAC-41A;
GN and
GN Name=MAC-41S;
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 PROTEIN SEQUENCE OF 100-140.
RX PubMed=1689486; DOI=10.1073/pnas.87.4.1481;
RA Hicke B.J., Celander D.W., Macdonald G.H., Price C.M., Cech T.R.;
RT "Two versions of the gene encoding the 41-kilodalton subunit of the
RT telomere binding protein of Oxytricha nova.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1481-1485(1990).
RN [2]
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 MAC-41A is shown. MAC-41S differs in
CC only one position.
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DR EMBL; M31309; AAA29400.1; -; Genomic_DNA.
DR EMBL; M31310; AAA29401.1; -; Genomic_DNA.
DR PIR; A34843; A34843.
DR PDB; 1JB7; X-ray; 1.86 A; B=1-260.
DR PDB; 1OTC; X-ray; 2.80 A; B=1-260.
DR PDB; 1PA6; X-ray; 2.45 A; B=9-224.
DR PDB; 1PH1; X-ray; 2.51 A; B=8-224.
DR PDB; 1PH2; X-ray; 3.10 A; B=9-224.
DR PDB; 1PH3; X-ray; 2.30 A; B=9-224.
DR PDB; 1PH4; X-ray; 2.30 A; B=9-224.
DR PDB; 1PH5; X-ray; 2.30 A; B=9-224.
DR PDB; 1PH6; X-ray; 2.10 A; B=8-224.
DR PDB; 1PH7; X-ray; 2.90 A; B=9-224.
DR PDB; 1PH8; X-ray; 2.36 A; B=9-224.
DR PDB; 1PH9; X-ray; 2.50 A; B=9-224.
DR PDB; 1PHJ; X-ray; 2.50 A; B=9-224.
DR PDB; 2I0Q; X-ray; 1.91 A; B=1-385.
DR PDBsum; 1JB7; -.
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; P16458; -.
DR SMR; P16458; -.
DR DIP; DIP-6195N; -.
DR MINT; P16458; -.
DR EvolutionaryTrace; P16458; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IMP: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 DisProt; DP00659; -.
DR Gene3D; 2.40.200.10; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR010874; TEBB.
DR InterPro; IPR023113; TEBP_beta_dom_sf.
DR Pfam; PF07404; TEBP_beta; 1.
DR PIRSF; PIRSF018412; TEBP_beta; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Telomere.
FT CHAIN 1..385
FT /note="Telomere-binding protein subunit beta"
FT /id="PRO_0000121737"
FT REGION 231..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 110
FT /note="A -> S (in MAC-41S)"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 87..99
FT /evidence="ECO:0007829|PDB:1JB7"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 112..124
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 142..163
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2I0Q"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1JB7"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1JB7"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1JB7"
SQ SEQUENCE 385 AA; 41446 MW; 743B51EFD7886352 CRC64;
MSKGASAPQQ QSAFKQLYTE LFNNEGDFSK VSSNLKKPLK CYVKESYPHF LVTDGYFFVA
PYFTKEAVNE FHAKFPNVNI VDLTDKVIVI NNWSLELRRV NSAEVFTSYA NLEARLIVHS
FKPNLQERLN PTRYPVNLFR DDEFKTTIQH FRHTALQAAI NKTVKGDNLV DISKVADAAG
KKGKVDAGIV KASASKGDEF SDFSFKEGNT ATLKIADIFV QEKGKDALNK AADHTDGAKV
KGGAKGKGKA AAKAAKGKKL SAKKGDSSAA DVRKSVDKIV KYTPSKGSRK DTPQKSQAPA
AGKSSAKKGG KKAVPSAPSP SGKKSALTTD KMTMAQFVKY LDWHEKKKGG KVSSGGKVLG
KRSAGKASAT SGKASKASKK TAAKK
