MOS1T_DROMA
ID MOS1T_DROMA Reviewed; 345 AA.
AC Q7JQ07; Q05407; Q05415; Q05417;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Mariner Mos1 transposase;
DE EC=3.1.-.-;
DE AltName: Full=Transposable element Mos1 transposase;
GN Name=mariner\T;
OS Drosophila mauritiana (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3022302; DOI=10.1073/pnas.83.22.8684;
RA Jacobson J.W., Medhora M.M., Hartl D.L.;
RT "Molecular structure of a somatically unstable transposable element in
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8684-8688(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-275.
RX PubMed=8384700; DOI=10.1038/362241a0;
RA Robertson H.M.;
RT "The mariner transposable element is widespread in insects.";
RL Nature 362:241-245(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF MUTANT ALA-216 IN COMPLEX WITH
RP INVERTED REPEAT DNA; MAGNESIUM AND MANGANESE IONS, FUNCTION, SUBUNIT, AND
RP METAL-BINDING SITES.
RX PubMed=19766564; DOI=10.1016/j.cell.2009.07.012;
RA Richardson J.M., Colloms S.D., Finnegan D.J., Walkinshaw M.D.;
RT "Molecular architecture of the Mos1 paired-end complex: the structural
RT basis of DNA transposition in a eukaryote.";
RL Cell 138:1096-1108(2009).
CC -!- FUNCTION: Mediates transposition of transposon Mos1 by a 'cut and
CC paste' mechanism. Transposases are sequence-specific nucleases and
CC strand transferases that catalyze transposition through an ordered
CC series of events: sequence-specific binding of transposase to the
CC terminal inverted repeats (IR) present at each end of the transposon,
CC pairing of the transposon IRs in a paired-end complex (PEC), cleavage
CC of one or both DNA strands at each transposon end, capture of target
CC DNA, and strand transfer to insert the transposon at a new site.
CC {ECO:0000269|PubMed:19766564}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese.;
CC -!- SUBUNIT: Homodimer. The complex has a trans arrangement, with each
CC transposon end recognized by the DNA binding region of one transposase
CC monomer and by the active site of the other monomer.
CC {ECO:0000269|PubMed:19766564}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; M14653; AAA28678.1; -; Genomic_DNA.
DR EMBL; L10449; AAA28698.1; -; Genomic_DNA.
DR EMBL; L10450; AAA28699.1; -; Genomic_DNA.
DR EMBL; L10451; AAA28700.1; -; Genomic_DNA.
DR EMBL; L10452; AAA28701.1; -; Genomic_DNA.
DR EMBL; L10453; AAA28702.1; -; Genomic_DNA.
DR EMBL; L10454; AAA28703.1; -; Genomic_DNA.
DR PIR; S36997; S36997.
DR PIR; S37002; S37002.
DR PDB; 2F7T; X-ray; 2.25 A; A=119-343.
DR PDB; 3HOS; X-ray; 3.50 A; A/B=1-343.
DR PDB; 3HOT; X-ray; 3.25 A; A/B=1-343.
DR PDB; 4MDA; X-ray; 1.70 A; A=121-343.
DR PDB; 4MDB; X-ray; 1.70 A; A=121-343.
DR PDB; 4R79; X-ray; 3.10 A; A/B=1-343.
DR PDB; 4U7B; X-ray; 3.09 A; A/B/G=4-343.
DR PDB; 5HOO; X-ray; 3.30 A; A/B=1-343.
DR PDBsum; 2F7T; -.
DR PDBsum; 3HOS; -.
DR PDBsum; 3HOT; -.
DR PDBsum; 4MDA; -.
DR PDBsum; 4MDB; -.
DR PDBsum; 4R79; -.
DR PDBsum; 4U7B; -.
DR PDBsum; 5HOO; -.
DR AlphaFoldDB; Q7JQ07; -.
DR SMR; Q7JQ07; -.
DR FlyBase; FBgn0013835; Dmau\mariner\T.
DR EvolutionaryTrace; Q7JQ07; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR041426; Mos1_HTH.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR001888; Transposase_1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF17906; HTH_48; 1.
DR Pfam; PF01359; Transposase_1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA integration; DNA recombination; DNA-binding;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus;
KW Transposable element.
FT CHAIN 1..345
FT /note="Mariner Mos1 transposase"
FT /id="PRO_0000386644"
FT DNA_BIND 24..55
FT /note="H-T-H motif"
FT DNA_BIND 89..110
FT /note="H-T-H motif"
FT REGION 1..112
FT /note="DNA-binding"
FT REGION 113..125
FT /note="Linker"
FT REGION 126..345
FT /note="Catalytic"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT SITE 48
FT /note="Important for base-specific DNA-binding"
FT SITE 100
FT /note="Important for base-specific DNA-binding"
FT SITE 118
FT /note="Important for base-specific DNA-binding"
FT SITE 186
FT /note="Critical for target DNA recognition"
FT SITE 186
FT /note="Important for target DNA recognition and for strand
FT transfer activity"
FT SITE 293
FT /note="Important for base-specific DNA-binding"
FT MUTAGEN 48
FT /note="R->Q: Loss of DNA binding; when associated with R-
FT 100."
FT MUTAGEN 100
FT /note="Q->R: Loss of DNA binding; when associated with Q-
FT 48."
FT MUTAGEN 118
FT /note="R->A: Reduces rate of second strand cleavage; when
FT associated with A-216."
FT MUTAGEN 119
FT /note="W->P: Alters cleavage sites in second strand
FT cleavage."
FT MUTAGEN 186
FT /note="R->A: No effect on second strand cleavage. Strongly
FT reduced strand transfer activity."
FT MUTAGEN 216
FT /note="T->A: Reduces rate of second strand cleavage; when
FT associated with A-118."
FT MUTAGEN 284
FT /note="D->A: Loss of catalytic activity."
FT CONFLICT 152
FT /note="I -> L (in Ref. 2; AAA28701)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> N (in Ref. 2; AAA28698/AAA28699/AAA28700/
FT AAA28701/AAA28702/AAA28703)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="R -> P (in Ref. 2; AAA28698/AAA28699/AAA28700/
FT AAA28701/AAA28702/AAA28703)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="R -> K (in Ref. 2; AAA28703)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..249
FT /note="HD -> YG (in Ref. 2; AAA28703)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="R -> C (in Ref. 2; AAA28703)"
FT /evidence="ECO:0000305"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:4U7B"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:4U7B"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5HOO"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:4U7B"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:4U7B"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:4U7B"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:4U7B"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:4U7B"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4U7B"
FT HELIX 126..145
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4MDA"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:4MDA"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4U7B"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3HOT"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:4MDA"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4MDA"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:4MDA"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:4R79"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:4MDA"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:4MDA"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4MDA"
SQ SEQUENCE 345 AA; 40851 MW; BC8E59E33B966697 CRC64;
MSSFVPNKEQ TRTVLIFCFH LKKTAAESHR MLVEAFGEQV PTVKKCERWF QRFKSGDFDV
DDKEHGKPPK RYEDAELQAL LDEDDAQTQK QLAEQLEVSQ QAVSNRLREM GKIQKVGRWV
PHELNERQME RRKNTCEILL SRYKRKSFLH RIVTGDEKWI FFVSPKRKKS YVDPGQPATS
TARPNRFGKK TMLCVWWDQS GVIYYELLKR GETVNTARYQ QQLINLNRAL QRKRPEYQKR
QHRVIFLHDN APSHTARAVR DTLETLNWEV LPHAAYSPDL APSDYHLFAS MGHALAEQRF
DSYESVKKWL DEWFAAKDDE FYWRGIHKLP ERWEKCVASD GKYLE
