TTF2_DROME
ID TTF2_DROME Reviewed; 1061 AA.
AC P34739; Q9VHY1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcription termination factor 2;
DE EC=3.6.4.-;
DE AltName: Full=Protein lodestar;
DE AltName: Full=RNA polymerase II termination factor;
DE AltName: Full=Transcription release factor 2;
GN Name=lds; ORFNames=CG2684;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1916263; DOI=10.1101/gad.5.10.1786;
RA Girdham C.G., Glover D.M.;
RT "Chromosome tangling and breakage at anaphase result from mutations in
RT lodestar, a Drosophila gene encoding a putative nucleoside triphosphate-
RT binding protein.";
RL Genes Dev. 5:1786-1799(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP PROTEIN SEQUENCE OF 255-266; 626-638 AND 1033-1045, AND FUNCTION.
RX PubMed=9748214; DOI=10.1074/jbc.273.40.25541;
RA Liu M., Xie Z., Price D.H.;
RT "A human RNA polymerase II transcription termination factor is a SWI2/SNF2
RT family member.";
RL J. Biol. Chem. 273:25541-25544(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-110; SER-214;
RP SER-215 AND THR-216, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: DsDNA-dependent ATPase which acts as a transcription
CC termination factor by coupling ATP hydrolysis with removal of RNA
CC polymerase II from the DNA template. {ECO:0000269|PubMed:9748214}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44496.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X62629; CAA44496.1; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF54167.1; -; Genomic_DNA.
DR PIR; A40580; A40580.
DR RefSeq; NP_524850.2; NM_080111.4.
DR AlphaFoldDB; P34739; -.
DR SMR; P34739; -.
DR BioGRID; 69962; 9.
DR DIP; DIP-20026N; -.
DR IntAct; P34739; 6.
DR MINT; P34739; -.
DR STRING; 7227.FBpp0081255; -.
DR iPTMnet; P34739; -.
DR PaxDb; P34739; -.
DR PRIDE; P34739; -.
DR EnsemblMetazoa; FBtr0081758; FBpp0081255; FBgn0002542.
DR GeneID; 45894; -.
DR KEGG; dme:Dmel_CG2684; -.
DR CTD; 45894; -.
DR FlyBase; FBgn0002542; lds.
DR VEuPathDB; VectorBase:FBgn0002542; -.
DR eggNOG; KOG4439; Eukaryota.
DR GeneTree; ENSGT00940000162718; -.
DR HOGENOM; CLU_000315_2_9_1; -.
DR InParanoid; P34739; -.
DR OMA; FAQFLFQ; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; P34739; -.
DR SignaLink; P34739; -.
DR BioGRID-ORCS; 45894; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 45894; -.
DR PRO; PR:P34739; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002542; Expressed in secondary oocyte and 19 other tissues.
DR ExpressionAtlas; P34739; baseline and differential.
DR Genevisible; P34739; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:FlyBase.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IDA:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Transcription termination.
FT CHAIN 1..1061
FT /note="Transcription termination factor 2"
FT /id="PRO_0000074378"
FT DOMAIN 452..652
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 891..1056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 603..606
FT /note="DEAH box"
FT COMPBIAS 15..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 465..472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 167
FT /note="R -> G (in Ref. 1; CAA44496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1061 AA; 118375 MW; 536BC893B1A90509 CRC64;
MSSENSEYYS DKEEDSVVNN SSLGRSRKSS RLSKSSRLSK SSRPSSAGVV IDETQSEEEE
SQSSETAESE KSDESDNSQN SQESEDSEDD SVRPSARNTK RKPLGIPSDS EDEEDELEQR
ALSPSTRMSI TGVRPQDLSD DDSEIEYSDE VQEGPTEAPT AEAVVPRYTT QFAGNIQNDL
HSTIGAADSE VLDDSSGSDV LILSNKETPI EILSSTDDDA TTNKENMSGP PFERPSKSLS
PRSSAGASVV KTSKNLSQPT IQAVLKQKTS PAAPRRSRIK SEDQKVVSQV VYDEEMRKLA
EKRVQVSDAE KLFEKVAHKL PDKGSQIMKR IDTLRRELAM DEQWISALRV QQSNVPAVRV
VKPTLNPPRA PSIDTLDWDE LSEAVNEIKP VYTGAQGMAT FNNQKALTLE SLKDLHVSLE
DLPGPEVLAE DPVGLKVSLM NHQKHALAWM SWRERKLPRG GILADDMGLG KTLTMISSVL
ACKNGQEMSE GKDESSDSDS EDDKNKKRKS VTGWKSKGRK DTRRGGTLVV CPASLLRQWE
SEVESKVSRQ KLTVCVHHGN NRETKGKYLR DYDIVVTTYQ IVAREHKSLS AVFGVKWRRI
ILDEAHVVRN HKSQSSLAVC DLRGKYRWAL TGTPIQNKEL DVYALLKFLR CSPFDDLHTW
KKWIDNKSAG GQNRLNLLMK SLMLRRTKAQ LQSDGKLNSL PNKELRLIEI SLDKEEMNVY
QTVMTYSRTL FAQFLHQRAE RETDFNYRSD ANKPTYNQIK DPNGAYYKMH EKFARMAGSK
KEVKSHDILV LLLRLRQICC HPGLIDAMLD GEESQTMGDH SSDSDTPEID LLAQLNKLAI
TDTSTDGQQS VANAGDDGPP LLPDEARIAK ASKNLLKRSN PVFNLHRPSS KINMVIQILK
TSILKSSDDK AIVVSQWTSV LDILRDHLSK DGVATLSLNG TIPVKNRQDI VNEFNDRNNQ
KRVLLLSLTA GGVGLNLIGA NHLLLLDLHW NPQLEAQAQD RIYRVGQKKN VIIYKFMCVD
TVEQRIKGLQ DKKLDLADGV LTGAKVSSKL TIDDLKGLFG M
