PELET_DROME
ID PELET_DROME Reviewed; 751 AA.
AC Q7M3K2;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Transposable element P transposase;
DE Short=P-element transposase;
DE EC=2.7.7.-;
DE AltName: Full=THAP domain-containing protein;
DE Short=DmTHAP;
GN Name=T {ECO:0000312|FlyBase:FBgn0013311};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3000622; DOI=10.1016/0092-8674(86)90480-0;
RA Laski F.A., Rio D.C., Rubin G.M.;
RT "Tissue specificity of Drosophila P element transposition is regulated at
RT the level of mRNA splicing.";
RL Cell 44:7-19(1986).
RN [2] {ECO:0000305, ECO:0000312|PIR:A24786}
RP FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=2416475; DOI=10.1016/0092-8674(86)90481-2;
RA Rio D.C., Laski F.A., Rubin G.M.;
RT "Identification and immunochemical analysis of biologically active
RT Drosophila P element transposase.";
RL Cell 44:21-32(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-77 IN COMPLEX WITH DNA,
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF HIS-18; GLN-42; ARG-65; ARG-66
RP AND ARG-67.
RX PubMed=20010837; DOI=10.1038/nsmb.1742;
RA Sabogal A., Lyubimov A.Y., Corn J.E., Berger J.M., Rio D.C.;
RT "THAP proteins target specific DNA sites through bipartite recognition of
RT adjacent major and minor grooves.";
RL Nat. Struct. Mol. Biol. 17:117-123(2010).
CC -!- FUNCTION: P-element transposase that specifically mediates
CC transposition of P-elements. Mediates both; precise and imprecise
CC excision. {ECO:0000269|PubMed:20010837, ECO:0000269|PubMed:2416475}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000269|PubMed:2416475}; Synonyms=87000Da
CC {ECO:0000303|PubMed:2416475};
CC IsoId=Q7M3K2-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:2416475}; Synonyms=66000Da
CC {ECO:0000303|PubMed:2416475};
CC IsoId=Q7M3K2-2; Sequence=VSP_051943, VSP_051944;
CC Name=C {ECO:0000269|PubMed:2416475};
CC IsoId=Q7M3K2-3; Sequence=VSP_051942;
CC -!- DOMAIN: The THAP-type zinc finger mediates DNA-binding and specifically
CC recognizes sequence elements in a bipartite manner using both the major
CC and minor grooves of its target DNA site. Minor-groove recognition is
CC achieved by a combination of direct base contacts and indirect sequence
CC readout of DNA deformation through a variable, basic loop. By contrast,
CC the adjacent major groove is sequence-specifically recognized by the
CC central beta-sheet of the domain (PubMed:20010837).
CC {ECO:0000269|PubMed:20010837}.
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DR PIR; A24786; A24786.
DR PDB; 3KDE; X-ray; 1.74 A; C=1-77.
DR PDB; 6P5A; EM; 3.60 A; A/G=1-561, B/H=617-751.
DR PDB; 6PE2; EM; 4.00 A; A/G=1-561, B/H=617-751.
DR PDBsum; 3KDE; -.
DR PDBsum; 6P5A; -.
DR PDBsum; 6PE2; -.
DR AlphaFoldDB; Q7M3K2; -.
DR SMR; Q7M3K2; -.
DR PRIDE; Q7M3K2; -.
DR FlyBase; FBgn0013311; P\T.
DR PRO; PR:Q7M3K2; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003693; F:P-element binding; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004803; F:transposase activity; IDA:UniProtKB.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006313; P:transposition, DNA-mediated; IDA:UniProtKB.
DR Gene3D; 6.20.210.20; -; 1.
DR InterPro; IPR022242; 87kDa_transposase.
DR InterPro; IPR006612; THAP_Znf.
DR InterPro; IPR038441; THAP_Znf_sf.
DR InterPro; IPR021896; Transposase_37.
DR Pfam; PF05485; THAP; 1.
DR Pfam; PF12017; Tnp_P_element; 1.
DR Pfam; PF12596; Tnp_P_element_C; 1.
DR SMART; SM00692; DM3; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA integration; DNA recombination;
KW DNA-binding; Metal-binding; Transferase; Transposable element; Zinc;
KW Zinc-finger.
FT CHAIN 1..751
FT /note="Transposable element P transposase"
FT /id="PRO_0000068656"
FT ZN_FING 1..77
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT VAR_SEQ 316..319
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:2416475"
FT /id="VSP_051942"
FT VAR_SEQ 562..576
FT /note="GMTNLKECVNKNVIP -> ARNTEMLRNSGNIEE (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2416475"
FT /id="VSP_051943"
FT VAR_SEQ 577..751
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2416475"
FT /id="VSP_051944"
FT MUTAGEN 18
FT /note="H->A: Impairs DNA-binding by a factor of 12."
FT /evidence="ECO:0000269|PubMed:20010837"
FT MUTAGEN 42
FT /note="Q->A: Impairs DNA-binding by a factor of 15."
FT /evidence="ECO:0000269|PubMed:20010837"
FT MUTAGEN 65
FT /note="R->A: Impairs DNA-binding by a factor of 21."
FT /evidence="ECO:0000269|PubMed:20010837"
FT MUTAGEN 66
FT /note="R->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:20010837"
FT MUTAGEN 67
FT /note="R->A: Impairs DNA-binding by a factor of 17."
FT /evidence="ECO:0000269|PubMed:20010837"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:3KDE"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3KDE"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:3KDE"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3KDE"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3KDE"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3KDE"
SQ SEQUENCE 751 AA; 86770 MW; 6D5662D3CDB79C77 CRC64;
MKYCKFCCKA VTGVKLIHVP KCAIKRKLWE QSLGCSLGEN SQICDTHFND SQWKAAPAKG
QTFKRRRLNA DAVPSKVIEP EPEKIKEGYT SGSTQTESCS LFNENKSLRE KIRTLEYEMR
RLEQQLRESQ QLEESLRKIF TDTQIRILKN GGQRATFNSD DISTAICLHT AGPRAYNHLY
KKGFPLPSRT TLYRWLSDVD IKRGCLDVVI DLMDSDGVDD ADKLCVLAFD EMKVAAAFEY
DSSADIVYEP SDYVQLAIVR GLKKSWKQPV FFDFNTRMDP DTLNNILRKL HRKGYLVVAI
VSDLGTGNQK LWTELGISES KTWFSHPADD HLKIFVFSDT PHLIKLVRNH YVDSGLTING
KKLTKKTIQE ALHLCNKSDL SILFKINENH INVRSLAKQK VKLATQLFSN TTASSIRRCY
SLGYDIENAT ETADFFKLMN DWFDIFNSKL STSNCIECSQ PYGKQLDIQN DILNRMSEIM
RTGILDKPKR LPFQKGIIVN NASLDGLYKY LQENFSMQYI LTSRLNQDIV EHFFGSMRSR
GGQFDHPTPL QFKYRLRKYI IGMTNLKECV NKNVIPDNSE SWLNLDFSSK ENENKSKDDE
PVDDEPVDEM LSNIDFTEMD ELTEDAMEYI AGYVIKKLRI SDKVKENLTF TYVDEVSHGG
LIKPSEKFQE KLKELECIFL HYTNNNNFEI TNNVKEKLIL AARNVDVDKQ VKSFYFKIRI
YFRIKYFNKK IEIKNQKQKL IGNSKLLKIK L
