POL4_DROME
ID POL4_DROME Reviewed; 1237 AA.
AC P10394;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Retrovirus-related Pol polyprotein from transposon 412;
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; Synonyms=ORF3;
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=2426108; DOI=10.1111/j.1432-1033.1986.tb09767.x;
RA Yuki S., Inouye S., Ishimaru S., Saigo K.;
RT "Nucleotide sequence characterization of a Drosophila retrotransposon,
RT 412.";
RL Eur. J. Biochem. 158:403-410(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; X04132; CAA27750.1; -; Genomic_DNA.
DR PIR; D29349; GNFF42.
DR AlphaFoldDB; P10394; -.
DR SMR; P10394; -.
DR PRIDE; P10394; -.
DR FlyBase; FBgn0043847; 412\ORF3.
DR PRO; PR:P10394; -.
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; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
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; IPR041577; RT_RNaseH_2.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 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..1237
FT /note="Retrovirus-related Pol polyprotein from transposon
FT 412"
FT /id="PRO_0000199558"
FT DOMAIN 58..131
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 338..523
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 957..1119
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ACT_SITE 63
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
SQ SEQUENCE 1237 AA; 143042 MW; AC57F1C159D14B65 CRC64;
QQSEQLQQKQ CQCTSNPRTG QLATAFRYSV EEDRRVYTIN YNLNIFSTFI HAKTGVKLVF
LLDTGADISI LKENSDKFSN IQITNKINIQ GIGQQKIQSR GQTFIEIQTG KYVIPHDFHL
VDKNFPIPCD GIIGIDFIKK YNCQIDLNQE EDWFIIRPNN LKFPIYIPIA YSSGINTTLL
PARSQVVRRL IVSSKDDNIL IPNQEIQTGI YVANTIATSS NTFVRILNTT DSDQLVNMDT
LKYEPLSNYN VVQANSEHRN KTVLSQLKKN FPELFKSQLE NICSEYIDIF ALESEPITVN
NLYKQQLRLK DDEPVYTKNY RSPHSQVEEI QAQVQKLIKD KIVEPSVSQY NSPLLLVPKK
SSPNSDKKKW RLVIDYRQIN KKLLADKFPL PRIDDILDQL GRAKYFSCLD LMSGFHQIEL
DEGSRDITSF STSNGSYRFT RLPFGLKIAP NSFQRMMTIA FSGIEPSQAF LYMDDLIVIG
CSEKHMLKNL TEVFGKCREY NLKLHPEKCS FFMHEVTFLG HKCTDKGILP DDKKYDVIQN
YPVPHDADSA RRFVAFCNYY RRFIKNFADY SRHITRLCKK NVPFEWTDEC QKAFIHLKSQ
LINPTLLQYP DFSKEFCITT DASKQACGAV LTQNHNGHQL PVAYASRAFT KGESNKSTTE
QELAAIHWAI IHFRPYIYGK HFTVKTDHRP LTYLFSMVNP SSKLTRIRLE LEEYNFTVEY
LKGKDNHVAD ALSRITIKEL KDITGNILKV TTRFQSRQKS CAGKEQLDLQ KQTKEIASEP
NVYEVITNDE VRKVVTLQLN DSICLFKHGK KIIARYDVGD LYTNGILDLD QFLQRLELQA
GIYDISQIKM APWKKIFEHV SIDKFKNMGN KILKNLKVAL LNPVTQINNE KEKEAILSTL
HDDPIQGGHT GITKTLAKVK RHYYWKNMSK YIKEYVRKCQ KCQKAKTTKH TKTPMTITET
PEHAFDRVVV DTIGPLPKSE NGNEYAVTLI CDLTKYLVAI PIANKSAKTV AKAIFESFIL
KYGPMKTFIT DMGTEYKNSI ITDLCKYLKI KNITSTAHHH QTVGVVERSH RTLNEYIRSY
ISTDKTDWDV WLQYFVYCFN TTQSMVHNYC PYELVFGRTS NLPKHFNKLH SIEPIYNIDD
YAKESKYRLE VAYARARKLL EAHKEKNKEN YDLKVKDIEL EVGDKVLLRN EVGHKLDFKY
TGPYKIESIG DNNNITLLTN KNKKQIVHKD RLKKFHS