ID   TBP7_CAEBR              Reviewed;        1285 AA.
AC   A8X0L9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Tat-binding homolog 7;
DE   AltName: Full=Lin-48 expression abnormal protein 1;
GN   Name=lex-1 {ECO:0000250|UniProtKB:P54816}; ORFNames=CBG06222;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Thought to form a complex that enhances transcription from
CC       repetitive DNA sequences by modulating chromatin structure.
CC       {ECO:0000250|UniProtKB:P54816}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255}.
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DR   EMBL; HE600986; CAP26179.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8X0L9; -.
DR   SMR; A8X0L9; -.
DR   STRING; 6238.CBG06222; -.
DR   WormBase; CBG06222; CBP46987; WBGene00028529; Cbr-lex-1.
DR   eggNOG; KOG0732; Eukaryota.
DR   HOGENOM; CLU_001448_3_1_1; -.
DR   InParanoid; A8X0L9; -.
DR   OMA; RPKYFGR; -.
DR   OrthoDB; 184252at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR045199; ATAD2-like.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23069; PTHR23069; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bromodomain; Nucleotide-binding; Reference proteome;
KW   Transcription.
FT   CHAIN           1..1285
FT                   /note="Tat-binding homolog 7"
FT                   /id="PRO_0000328998"
FT   DOMAIN          945..1015
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1100..1196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..239
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..321
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1108..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1171
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         446..453
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1285 AA;  146499 MW;  0675971F18E86F9C CRC64;
     MARSDGFSPR KSLRRSAREH SRSYVGQGSN DDFDDMYSPP SRRRGSGGGD GNGYTRSGRK
     IHHSRYYEED YQDAISSDDE RMYRPRRNSN SLTYRQQCKQ AIDESKRIQK VPPAKRKRIY
     MSDDEEEFVE TRQMENTAPD RPTRRSSRRM SSTHEEPDVL DQEDVSPIRR TRRTTIRFGS
     EPVEENMEVP RVLETNDMAN EAIVQAVDNT ENGETEEDVI EKIGREEEEE GDEEEAESGE
     KEQVGLLFHR IFNQAYLQED EESSNAESSE ESTAPRQYSL RRRQPVVQFN QSEARENRRA
     RLEHHRAANA NRHHRNRNTS NRRRRSGSDS DSDDMVLPRP DKRQSRPHMH NRGERERGRF
     MPINMTEKEL QSAQHILMDR MRKTDAGQGA SDIDPMSVDS SVGFDQVGGL SHHIQSLKEV
     VLFPMLYPEV FAKFKINPPK GVVFYGPPGT GKTLVARALA NECRRGANKV AFFMRKGADC
     LSKWVGESER QLRLLFDQAY AMRPSIIFFD EIDGLAPVRS SKQDQIHASI VSTLLALMDG
     LDGRGEVVVI GATNRLDSLD PALRRPGRFD RELRFSLPDL NARRHILDIH TSKWEENKPT
     PETLDGIAEK TSGYCGADLK FLCTESVLIG LRSRYPHIYM CSERLKLDIT TIKITEEHFG
     HAMRRITPAS RRDLTIPSRP LDERTSILLG DIVKNLISLR IPQGYRCVEN AMATASTELE
     QVVRALEPNL TVPAIRLLLC GSPSLSDGGQ TSYVLPAILA KLDHLPVFSL SVSSLLTDGR
     PEEAFSNAVQ SAMRASATGP CIMLLPSIDE WIKVIPVSVQ HMLITCLESM TGFTPILFLS
     TLDSSFEDAP EYATEVFRHA NCISLNPSRR SVRKRYFEFV IDGVRRKPKV FDPTIYEMPQ
     ADDDSPEAKP SRKLNDDETR ELLKMYTALQ RQMRMFFKER LSRLIRDRRF VEFVEPVDPE
     EAEDYYEIIE TPICMQDIME KLNKCEYNHA DKFIADLVLI QSNALEYNPS NTKDGKLIRQ
     MANTFRDAID DMIDCELDES FVERIEMVSR MLQDAGVTPT SDQLLTEIPK GFSRKKPWTM
     ANTLAKEIEQ WKAEREAENE KLKEKLGIST DTAQSAIEEN KSEEGTSSSV EEIKKKLNKK
     KKDQKRNKKA SSQDPDGDDT EETEEAVAEN NVDADVEMKE TPADPVPTIQ SSSSQEREII
     VSADSITDLI KLCVEKSEGW SVSELERLSS VLSHTIERFR DEWNRENLPE QLAQIVREWE
     ATDATNEKIA NGKASNKNGI VFNGY