ID   POL_OMVVS               Reviewed;        1086 AA.
AC   P16901;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Pol polyprotein;
DE   Contains:
DE     RecName: Full=Protease;
DE              EC=3.4.23.-;
DE     AltName: Full=Retropepsin;
DE   Contains:
DE     RecName: Full=Reverse transcriptase/ribonuclease H;
DE              Short=RT;
DE              EC=2.7.7.49;
DE              EC=3.1.26.13;
DE     AltName: Full=Exoribonuclease H;
DE              EC=3.1.13.2;
DE   Contains:
DE     RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE              Short=dUTPase;
DE              EC=3.6.1.23;
DE   Contains:
DE     RecName: Full=Integrase;
DE              Short=IN;
DE              EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE              EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN   Name=pol;
OS   Ovine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine
OS   lentivirus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Lentivirus ovivismae; Visna-maedi virus.
OX   NCBI_TaxID=11664;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2158181; DOI=10.1016/0042-6822(90)90428-t;
RA   Querat G., Audoly G., Sonigo P., Vigne R.;
RT   "Nucleotide sequence analysis of SA-OMVV, a visna-related ovine lentivirus:
RT   phylogenetic history of lentiviruses.";
RL   Virology 175:434-447(1990).
CC   -!- FUNCTION: During replicative cycle of retroviruses, the reverse-
CC       transcribed viral DNA is integrated into the host chromosome by the
CC       viral integrase enzyme. RNase H activity is associated with the reverse
CC       transcriptase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC         cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC         immunodeficiency virus type 1 and Moloney murine leukemia virus
CC         enzymes prefer to cleave the RNA strand one nucleotide away from the
CC         RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC         from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC         away from the primer terminus.; EC=3.1.26.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC         hybrid.; EC=3.1.13.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dUTP + H2O = dUMP + diphosphate + H(+); Xref=Rhea:RHEA:10248,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC   -!- PTM: Cleavage sites that yield the mature proteins remain to be
CC       determined.
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; M31646; AAA66812.1; -; Genomic_RNA.
DR   SMR; P16901; -.
DR   MEROPS; A02.006; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 1.10.10.200; -; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   Gene3D; 3.30.70.270; -; 3.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   InterPro; IPR017856; Integrase-like_N.
DR   InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR   InterPro; IPR001037; Integrase_C_retrovir.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR003308; Integrase_Zn-bd_dom_N.
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; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR010659; RVT_connect.
DR   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   Pfam; PF02022; Integrase_Zn; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF06815; RVT_connect; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
DR   SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS51027; INTEGRASE_DBD; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50876; ZF_INTEGRASE; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; DNA integration; DNA recombination; DNA-binding;
KW   Endonuclease; Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
KW   Nucleotide metabolism; Nucleotidyltransferase; Protease;
KW   RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   CHAIN           1..120
FT                   /note="Protease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038853"
FT   CHAIN           121..671
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038854"
FT   CHAIN           672..805
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038855"
FT   CHAIN           806..1086
FT                   /note="Integrase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038856"
FT   DOMAIN          39..110
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          167..356
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          551..673
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          850..1010
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         808..849
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   DNA_BIND        1027..1079
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         817
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         821
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         845
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         848
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
SQ   SEQUENCE   1086 AA;  124515 MW;  099F9614679FC8BD CRC64;
     SNITAGKQQE GATCGAVRAP YVVTEAPPKI DIKVGTNWKK VLVDTGADRT IVRYHDNSGI
     PTGRIKLQGI GGIIEGEKWD KVVIQYKEKR IEGTIVVLPS SPVEVLGRDN MAKLDIGIIM
     ANLEEKKIPI TQVKLKEGCK GPHIAQWPLT QEKLEGLKEI VDKLEKEGKV GRAPPHWTCN
     TPIFCIKKKS GKWRMLIDFR ELNKQTEDLA EAQLGLPHPG GLQKKKHVTI LDIGDAYFTI
     PLYEPYRPYT CFTMLSPNNL GPCTRYYWKV LPQGWKLSPS VYQFTMQEIL RDWIAKHPMI
     QFGIYMDDIY IGSDLDIMKH REIVEELASY IAQYGFMLPE EKRQEGYPAK WLGFELHPEK
     WRFQKHTLPE IKEGTITLNK LQKLVGDLVW RQSLIGKSIP NILKLMEGDR ALQSERRIEL
     RHVKEWEECR RKLAEMEGNY YDEEKDVYGQ IDWGDKAIEY IVFQERGKPL WVNVVHNIKN
     LSQSQQIIKA AQKLTQEVII RIGKIPWILL PGKEEDWILE LQIGNITWMP SFWSCYRGSI
     RWKKRNVITE VVEGPTYYTD GGKKNGKGSL GFIASTGVKF RKHEEGTNQQ LELRAIEEAC
     KQGPEKMNIV TDSRYAYEFM RRNWDEEVIK NPIQARIMKL VHDKEQIGVH WVPGHKGIPQ
     NEEIDKYISE IFLAREGSGI LPKRAEDAGY DLICPQEVCI PAGQVRKIPI NLRINLKEDQ
     WAMVGTKSSF ASKGVFVQGG IIDSGYQGII QVVVYNSNDK EVIIPQGRKF AQLILMPLIH
     EDLEAWGETR RTERGNQGFG STGAYWIENI PLAEEDHSKW HQDAGSLHLD FGIPRTAAED
     IVQQCEVCQE NKMPSTIRGS NRRGIDHWQV DYTHYEDKII LVWVETNSGL IYAERVKGET
     GQEFRIMTIR WYGLFAPKSL QSDNGPAFVA EPTQLLMKYL GITHTTGIPW NPQSQALVER
     THQTLKNTIE KFVSMFASFD SAIAAALITL NIKRKGGLGT SPMDIFIFNK EQQRIQQQST
     RNQSKFRFCY YRVRKRGHPG EWLGPTQVLW EGEGAIVIKD KNLEKYLVIA KKDVKFIPQP
     KEIQTE
//