ID   POL_MLVAV               Reviewed;        1196 AA.
AC   P03356; P03357;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   16-JUN-2009, entry version 81.
DE   RecName: Full=Pol polyprotein;
DE   Contains:
DE     RecName: Full=Protease;
DE              EC=3.4.23.-;
DE   Contains:
DE     RecName: Full=Reverse transcriptase/ribonuclease H;
DE              Short=RT;
DE              EC=2.7.7.49;
DE              EC=3.1.26.4;
DE   Contains:
DE     RecName: Full=Integrase;
DE              Short=IN;
GN   Name=pol;
OS   AKV murine leukemia virus (AKR (endogenous) murine leukemia virus).
OC   Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC   Gammaretrovirus; Murine leukemia virus.
OX   NCBI_TaxID=11791;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=84115072; PubMed=6319746;
RA   Herr W.;
RT   "Nucleotide sequence of AKV murine leukemia virus.";
RL   J. Virol. 49:471-478(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 353-1196.
RX   MEDLINE=83090450; PubMed=6294621; DOI=10.1093/nar/10.21.6931;
RA   Herr W., Corbin V., Gilbert W.;
RT   "Nucleotide sequence of the 3' half of AKV.";
RL   Nucleic Acids Res. 10:6931-6944(1982).
CC   -!- FUNCTION: During replicative cycle of retroviruses, the reverse-
CC       transcribed viral DNA is integrated into the host chromosome by
CC       the viral integrase enzyme. RNase H activity is associated with
CC       the reverse transcriptase.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Pol
CC       polyprotein.
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC   -!- SIMILARITY: Contains 1 integrase catalytic domain.
CC   -!- SIMILARITY: Contains 1 peptidase A2 domain.
CC   -!- SIMILARITY: Contains 1 reverse transcriptase domain.
CC   -!- SIMILARITY: Contains 1 RNase H domain.
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DR   EMBL; J01998; AAB03091.1; ALT_INIT; Genomic_RNA.
DR   PIR; A03958; GNVWK.
DR   HSSP; P03355; 1I6J.
DR   SMR; P03356; 144-594, 623-788.
DR   MEROPS; A02.008; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004523; F:ribonuclease H activity; IEA:EC.
DR   GO; GO:0003723; F:RNA 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0006278; P:RNA-dependent DNA replication; IEA:InterPro.
DR   GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR   InterPro; IPR000477; DNA_pol_RVTase.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR018061; Pept_A2A_retrovirus_sg.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR001969; Peptidase_aspartic_AS.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   InterPro; IPR002156; RNase_H.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 1.
DR   Pfam; PF00075; RnaseH; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50879; RNASE_H; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; DNA integration; DNA recombination; Endonuclease;
KW   Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Protease; RNA-directed DNA polymerase; Transferase.
FT   CHAIN         1   1196       Pol polyprotein.
FT                                /FTId=PRO_0000259722.
FT   CHAIN         1    103       Protease.
FT                                /FTId=PRO_0000026129.
FT   CHAIN       104      ?       Reverse transcriptase/ribonuclease H.
FT                                /FTId=PRO_0000259723.
FT   CHAIN         ?   1196       Integrase.
FT                                /FTId=PRO_0000259724.
FT   DOMAIN       22     92       Peptidase A2.
FT   DOMAIN      202    393       Reverse transcriptase.
FT   DOMAIN      635    781       RNase H.
FT   DOMAIN      905   1063       Integrase catalytic.
FT   ACT_SITE     27     27       By similarity.
FT   CONFLICT    540    540       R -> T (in Ref. 2).
FT   CONFLICT    996    996       Missing (in Ref. 2).
SQ   SEQUENCE   1196 AA;  133413 MW;  EDBAE9F550839A01 CRC64;
     GGQGQEPPPE PRITLTVGGQ PVTFLVDTGA QHSVLTQNPG PLSDRSAWVQ GATGGKRYRW
     TTDRKVHLAT GKVTHSFLHV PDCPYPLLGR DLLTKLKAQI HFEGSGAQVV GPKGQPLQVL
     TLNLEDEYRL YETSAEPEVS PGSTWLSDFP QAWAETGGMG LAVRQAPLII PLKATSTPVS
     IKQYPMSQEA KLGIKPHIQR LLDQGILVPC QSPWNTPLLP VKKPGTNDYR PVQDLREVNK
     RVEDIHPTVP NPYNLLSGLP PSHRWYTVLD LKDAFFCLRL HPTSQPLFAF EWRDPGMGIS
     GQLTWTRLPQ GFKNSPTLFD EALHRDLADF RIQHPDLILL QYVDDILLAA TSELDCQQGT
     RALLLTLGNL GYRASAKKAQ LCQKQVKYLG YLLKEGQRWL TEARKETVMG QPTPKTPRQL
     REFLGTAGFC RLWIPGFAEM AAPLYPLTKT GTLFNWGPDQ QKAYQEIKQA LLTAPALGLP
     DLTKPFELFV DEKQGYAKGV LTQKLGPWRR PVAYLSKKLD PVAAGWPPCL RMVAAIAVLR
     KDAGKLTMGQ PLVILAPHAV EALVKQPPDR WLSNARMTHY QAMLLDTDRV QFGPVVALNP
     ATLLPLPEEG APHDCLEILA ETHGTRPDLT DQPIPDADHT WYTDGSSFLQ EGQRKAGAAV
     TTETEVIWAR ALPAGTSAQR AELIALTQAL KMAEGKRLNV YTDSRYAFAT AHIHGEIYRR
     RGLLTSEGRE IKNKSEILAL LKALFLPKRL SIIHCLGHQK GDSAEARGNR LADQAAREAA
     IKTPPDTSTL LIEDSTPYTP AYFHYTETDL KKLRELGATY NQSKGYWVFQ GKPVMPDQFV
     FELLDSLHRL THLGYQKMKA LLDRGESPYY MLNRDKTLQY VADSCTVCAQ VNASKAKIGA
     GVRVRGHRPG SHWEIDFTEV KPGLYGYKYL LVFVDTFSGW VEAFPTKRET ARVVSKKLLE
     EIFPRFGMPQ VLGSDNGPAF TSQVSQSVAD LLGIDWKLHC AYRPQSSGQV ERMNRTIKET
     LTKLTLAAGT RDWVLLLPLA LYRARNTPGP HGLTPYEILY GAPPPLVNFH DPDMSELTNS
     PSLQAHLQAL QTVQREIWKP LAEAYRDQLD QPVIPHPFRI GDSVWVRRHQ TKNLEPRWKG
     PYTVLLTTPT ALKVDGISAW IHAAHVKAAT TPPIKPSWRV QRSQNPLKIR LTRGAP
//