ID   POL_CAEVC               Reviewed;        1109 AA.
AC   P33459;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 151.
DE   RecName: Full=Pol polyprotein;
DE   Contains:
DE     RecName: Full=Protease;
DE     AltName: Full=Retropepsin;
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=3.1.26.13;
DE     AltName: Full=Exoribonuclease H;
DE              EC=3.1.13.2;
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   Caprine arthritis encephalitis virus (strain Cork) (CAEV-Co).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Lentivirus capartenc; Caprine arthritis encephalitis virus.
OX   NCBI_TaxID=11661;
OH   NCBI_TaxID=9925; Capra hircus (Goat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2171210; DOI=10.1016/0042-6822(90)90303-9;
RA   Saltarelli M., Querat G., Konings D.A.M., Vigne R., Clements J.E.;
RT   "Nucleotide sequence and transcriptional analysis of molecular clones of
RT   CAEV which generate infectious virus.";
RL   Virology 179:347-364(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=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: Specific enzymatic cleavages in vivo yield mature proteins.
CC   -!- MISCELLANEOUS: This protein may be synthesized as a Gag-Pol
CC       polyprotein.
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA91826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M33677; AAA91826.1; ALT_INIT; Genomic_RNA.
DR   PIR; B45345; B45345.
DR   RefSeq; NP_040939.1; NC_001463.1.
DR   AlphaFoldDB; P33459; -.
DR   SMR; P33459; -.
DR   MEROPS; A02.006; -.
DR   GeneID; 1489976; -.
DR   KEGG; vg:1489976; -.
DR   Proteomes; UP000203242; Segment.
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: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: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; cd01645; RT_Rtv; 1.
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; 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; 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; 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   Nucleotidyltransferase; Protease; Reference proteome;
KW   RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   CHAIN           1..152
FT                   /note="Protease"
FT                   /id="PRO_0000038829"
FT   CHAIN           153..865
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000038830"
FT   CHAIN           866..1109
FT                   /note="Integrase"
FT                   /id="PRO_0000038831"
FT   DOMAIN          63..134
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          191..380
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          575..697
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          874..1034
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         832..873
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   DNA_BIND        1051..1103
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT   REGION          16..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..29
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         841
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         869
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         872
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
SQ   SEQUENCE   1109 AA;  127678 MW;  97B2F4B370B03CF3 CRC64;
     TRNHMSQLWK ERTYAKRMQR KERHKGKTAG KREEGDTCGA VRSSYGITSA PPMVQVRIGS
     QQRNLLFDTG ADRTIVRWHE GSGNPAGRIK LQGIGGIVEG EKWNNVELEY KGETRKGTIV
     VLPQSPVEVL GRDNMARFGI KIIMANLEEK RIPITKVKLK EGCTGPHVPQ WPLTEEKLKG
     LTEIIDKLVE EGKLGKAPPH WTCNTPIFCI KKKSGKWRML IDFRELNKQT EDLTEAQLGL
     PHPGGLQKKK HVTILDIGDA YFTIPLYEPY REYTCFTLLS PNNLGPCKRY YWKVLPQGWK
     LSPSVYQFTM QEILEDWIQQ HPEIQFGIYM DDIYIGSDLE IKKHREIVKD LANYIAQYGF
     TLPEEKRQKG YPAKWLGFEL HPQTWKFQKH TLPELTKGTI TLNKLQKLVG ELVWRQSIIG
     KSIPNILKLM EGDRELQSER KIEEVHVKEW EACRKKLEEM EGNYYNKDKD VYGQLAWGDK
     AIEYIVYQEK GKPLWVNVVH NIKNLSIPQQ VIKAAQKLTQ EVIIRTGKIP WILLPGKEED
     WRLELQLGNI TWMPKFWSCY RGHTRWRKRN IIEEVVEGPT YYTDGGKKNK VGSLGFIVST
     GEKFRKHEEG TNQQLELRAI EEALKQGPQT MNLVTDSRYA FEFLLRNWDE EVIKNPIQAR
     IMEIAHKKDR IGVHWVPGHK GIPQNEEIDK YISEIFLAKE GEGILPKREE DAGYDLICPE
     EVTIEPGQVK CIPIELRLNL KKSQWAMIAT KSSMAAKGVF TQGGIIDSGY QGQIQVIMYN
     SNKIAVVIPQ GRKFAQLILM DKKHGKLEPW GESRKTERGE KGFGSTGMYW IENIPLAEED
     HTKWHQDARS LHLEFEIPRT AAEDIVNQCE ICKEARTPAV IRGGNKRGVN HWQVDYTHYE
     NIILLVWVET NSGLIYAEKV KGESGQEFRI KVMHWYALFG PESLQSDNGP AFAAEPTQLL
     MQYLGVKHTT GIPWNPQSQA IVERAHQLLK STLKKFQPQF VAVESAIAAA LVAINIKRKG
     GLGTSPMDIF IYNKEQKRIN NKYNKNSQKI QFCYYRIRKR GHQESGKDQP RYCGKGKEPI
     VVKDIESEKY LVIPYKDAKF IPPPTKEKE
//