TGP1_TETTH
ID TGP1_TETTH Reviewed; 725 AA.
AC O43952;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=G-quartet DNA-binding protein TGP1;
GN Name=TGP1;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 368-390.
RC STRAIN=C3-V;
RX PubMed=9512530; DOI=10.1093/nar/26.7.1613;
RA Lu Q., Schierer T.P., Kang S.-G., Henderson E.;
RT "Purification, characterization and molecular cloning of TGP1, a novel G-
RT DNA binding protein from Tetrahymena thermophila.";
RL Nucleic Acids Res. 26:1613-1620(1998).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=C3-V;
RX PubMed=7509637; DOI=10.1021/bi00174a034;
RA Schierer T., Henderson E.;
RT "A protein from Tetrahymena thermophila that specifically binds parallel-
RT stranded G4-DNA.";
RL Biochemistry 33:2240-2246(1994).
CC -!- FUNCTION: Binds specifically to parallel G4-DNA, a four-stranded
CC structure stabilized by tetrads of hydrogen-bonded guanines.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; AF006380; AAC48333.1; -; mRNA.
DR PIR; T03219; T03219.
DR AlphaFoldDB; O43952; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR SUPFAM; SSF50249; SSF50249; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Nucleus.
FT CHAIN 1..725
FT /note="G-quartet DNA-binding protein TGP1"
FT /id="PRO_0000072510"
FT REGION 252..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..258
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 260..275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 385
FT /note="K -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 83212 MW; 7175AC9FA9C85205 CRC64;
MTDQGVAKEQ YITVGSLKEI ADPVKKFLRK GNRKGRNQKE LKFRAKVVNQ QLADETGSIN
FTTEGVAVNN NQTYEFTGSL KVVDYKLNLA VTSATPAKDQ IANLGSEQLS KADIDQHSGK
HIVLIKDLIN LRIGQSFFAR PKDIVHNNEQ RRMTATLADN TAAIQAEISV NKKSITQEVL
ESLNSDKVYL FSDVVLNFNE SNKLVARFNY RSNIVEANDR QIQQLSNNNL SAKEYSDETE
KKALTDVLQI HEKKERVHKQ QNKNKNPRNA HKNHNRQRPN LQETEPVKIS GLQQWNNNQT
VIGKIVSLRT EDKSLPAKQD GTSTTMVYLK GTIGDETGVI DFDMAEKRDC PRFKENDVVK
FTSVMNKGRQ SAEGKVGGHY IEVKKFGQYI ILSDHNINNV NLNNNLSNLE LTARPKNPNP
RFIKGEFVGV KEEEKDGNIQ YTYTVRSKEG EEQSITIRNK ITTLKVGEIH KIDRERKRSS
SRPNHQGGQR GNRSHSQNNR NQRNRDKHHN SQNNQPNKYK NTSVQNNNNN KNQQRSQSQN
QRPPRNYDNR QGGENRNNRQ RNENNRNNFN GNGHRVNNQN NQRNRNSSYP RNNNYDHHHN
QQTDISGLEP GKRGQNVTGQ VIEVSEFSKQ INDKTLHFVK GRIADENANI RFDIKKPQNL
EIKVGEVYNF KDVNNKVDDN GYHYIDLNRF GRVFPSHKKF QSINDKRNCD ADRSSIEYVK
KTVPN