ID   YSNA_STRPR              Reviewed;         402 AA.
AC   P54992;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Putative RNA-guided DNA endonuclease {ECO:0000250|UniProtKB:Q7DF80};
DE            EC=3.1.21.- {ECO:0000250|UniProtKB:Q7DF80};
DE   AltName: Full=ORF401;
OS   Streptomyces pristinaespiralis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP92;
RX   PubMed=7665509; DOI=10.1128/jb.177.18.5206-5214.1995;
RA   Blanc V., Lagneaux D., Didier P., Gil P., Lacroix P., Crouzet J.;
RT   "Cloning and analysis of structural genes from Streptomyces
RT   pristinaespiralis encoding enzymes involved in the conversion of
RT   pristinamycin IIB to pristinamycin IIA (PIIA): PIIA synthase and
RT   NADH:riboflavin 5'-phosphate oxidoreductase.";
RL   J. Bacteriol. 177:5206-5214(1995).
CC   -!- FUNCTION: An RNA-guided dsDNA endonuclease. When guided by an RNA
CC       derived from the right-end element of its insertion sequence element
CC       (IS), cleaves DNA downstream of the transposon-associated motif (TAM).
CC       Cleaves supercoiled and linear DNA in a staggered manner 15-21 bases
CC       from the TAM yielding 5'-overhangs. Binds reRNA, an approximately 150
CC       nucleotide base sRNA derived from the 3' end of its own gene, the right
CC       end (RE) of the insertion sequence (IS) plus sequence downstream of the
CC       IS. {ECO:0000250|UniProtKB:Q7DF80}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the transposase 2
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transposase 35
CC       family. {ECO:0000305}.
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DR   EMBL; U21215; AAA83564.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54992; -.
DR   STRING; 38300.SPRI_0184; -.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR   InterPro; IPR001959; Transposase_2.
DR   InterPro; IPR010095; Transposase_IS605_OrfB_C.
DR   InterPro; IPR021027; Transposase_put_HTH.
DR   Pfam; PF12323; HTH_OrfB_IS605; 1.
DR   Pfam; PF01385; OrfB_IS605; 1.
DR   Pfam; PF07282; OrfB_Zn_ribbon; 1.
DR   TIGRFAMs; TIGR01766; tspaseT_teng_C; 1.
PE   3: Inferred from homology;
KW   DNA recombination; DNA-binding; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Transposable element; Transposition; Zinc.
FT   CHAIN           1..402
FT                   /note="Putative RNA-guided DNA endonuclease"
FT                   /id="PRO_0000066503"
FT   REGION          202..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
FT   BINDING         346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7DF80"
SQ   SEQUENCE   402 AA;  45392 MW;  38E2A7AC6BAB2B28 CRC64;
     MMQQVKRAFK YRFYPTDEQA AELSRTFGCV RLVYNKALEG RTRAWYGEQR RVSYVQSSAA
     LTEWKKTEEL AFLSEVSSVP LQQALRHLQT AFANFFAKRS KYPRYKSRKK SRASAEYTRS
     AFTWRNGQLT LAKTAEPLDI RWSRPLPEGA EPTTVTVSRD RAGRWFVSLL CEDTITPAPA
     TTAAVGIDAG ITSLVTLSTG EKITNPKHER RDRARLAKAQ RDVSRKAKGS ANRKKARRKV
     ARVHARITDR RCDFLHKLST RLVRENQTVV IEDLTVRNLL KNGKLARAIS DAAWTELRSM
     LEYKCAWYGR ELVVIDRWFP SSKLCGTCGT VRGKLPLNVR EWTCDCGAVH DRDVNAARNI
     LAAGLAASAC GDGIRPQRES SRTGRSSVKQ EPQRATAGIP RL