ID   POL2_DROME              Reviewed;        1059 AA.
AC   P20825;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Retrovirus-related Pol polyprotein from transposon 297;
DE   Includes:
DE     RecName: Full=Protease;
DE              EC=3.4.23.-;
DE   Includes:
DE     RecName: Full=Reverse transcriptase;
DE              EC=2.7.7.49;
DE   Includes:
DE     RecName: Full=Endonuclease;
GN   Name=pol;
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 [GENOMIC DNA].
RX   PubMed=2417839; DOI=10.1111/j.1432-1033.1986.tb09414.x;
RA   Inouye S., Yuki S., Saigo K.;
RT   "Complete nucleotide sequence and genome organization of a Drosophila
RT   transposable genetic element, 297.";
RL   Eur. J. Biochem. 154:417-425(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
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DR   EMBL; X03431; CAB57796.1; ALT_SEQ; Genomic_DNA.
DR   PIR; B24872; B24872.
DR   AlphaFoldDB; P20825; -.
DR   SMR; P20825; -.
DR   MEROPS; A02.052; -.
DR   FlyBase; FBgn0027622; 297\pol.
DR   PRO; PR:P20825; -.
DR   GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProt.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041373; RT_RNaseH.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Aspartyl protease; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotidyltransferase; Protease; RNA-directed DNA polymerase; Transferase;
KW   Transposable element.
FT   CHAIN           1..1059
FT                   /note="Retrovirus-related Pol polyprotein from transposon
FT                   297"
FT                   /id="PRO_0000199556"
FT   DOMAIN          230..414
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          812..967
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   REGION          998..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        30
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
SQ   SEQUENCE   1059 AA;  123311 MW;  3905CF38E914173D CRC64;
     TKRKFSVNSS GKYEYIKIVY KGRSYKCLLD TGSTINMINE NIFCLPIQNS RCEVLTSNGP
     ITLNDLIMLP RNSIFKKTEP FYVHRFSNNY DMLIGRKLLK NAQSVINYKN DTVTLFDQTY
     KLITSESERN QNLYIQRTPE SIASSDQESI KKLDFSQFRL DHLNQEETFK LKGLLNKFRN
     LEYKEGEKLT FTNTIKHVLN TTHNSPIYSK QYPLAQTHEI EVENQVQEML NQGLIRESNS
     PYNSPTWVVP KKPDASGANK YRVVIDYRKL NEITIPDRYP IPNMDEILGK LGKCQYFTTI
     DLAKGFHQIE MDEESISKTA FSTKSGHYEY LRMPFGLRNA PATFQRCMNN ILRPLLNKHC
     LVYLDDIIIF STSLTEHLNS IQLVFTKLAD ANLKLQLDKC EFLKKEANFL GHIVTPDGIK
     PNPIKVKAIV SYPIPTKDKE IRAFLGLTGY YRKFIPNYAD IAKPMTSCLK KRTKIDTQKL
     EYIEAFEKLK ALIIRDPILQ LPDFEKKFVL TTDASNLALG AVLSQNGHPI SFISRTLNDH
     ELNYSAIEKE LLAIVWATKT FRHYLLGRQF LIASDHQPLR WLHNLKEPGA KLERWRVRLS
     EYQFKIDYIK GKENSVADAL SRIKIEENHH SEATQHSAEE DNSNLIHLTE KPINYFKKQI
     IFIKSDKNKV EHSKIFGNSI TTIQYDVMTL EKAKQILLDH FIHRNITIYI ESDVDFEIVQ
     RAHIEIVNTT YTKVIRSLFL LKNVGSYAEF KEIILQSHEK LLHPGIQKMT KLFKENHFFP
     NSQLLIQNII NECNICNLAK TEHRNTKMPL KITPNPEHCR EKFVVDIYSS EGKHYISCID
     IYSKFATLEQ IKTKDWIECR NALMRIFNQL GKPKLLKADR DGAFSSLALK RWLEEEEVEL
     QLNTAKNGVA DVERLHKTIN EKIRIINSSD DEEVKLSKIE TILYTYNQKI KHDTTGQRPA
     QIFLYAGHPI LDTQKIKEKK IEKINEDRRE FNIDTNYRKG PLQKGKLENP FKPTKNVEQT
     DPDHYKITNR NRVTHYYKTQ FKKQKKNNKL SISQAPGTR