POL_OMVVS
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 03-AUG-2022, entry version 141.
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.
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 = diphosphate + dUMP + 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=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};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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:InterPro.
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:viral 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; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
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 Pfam; PF00692; dUTPase; 1.
DR Pfam; PF00552; IN_DBD_C; 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; SSF46919; SSF46919; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
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; 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
