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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
 
 
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