POL_CAEVC
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 03-AUG-2022, entry version 137.
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.
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=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: 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};
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; M33677; AAA91826.1; ALT_INIT; Genomic_RNA.
DR PIR; B45345; B45345.
DR RefSeq; NP_040939.1; NC_001463.1.
DR SMR; P33459; -.
DR MEROPS; A02.006; -.
DR GeneID; 1489976; -.
DR KEGG; vg:1489976; -.
DR Proteomes; UP000203242; Genome.
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: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: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; 2.40.70.10; -; 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; 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 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 SUPFAM; SSF46919; SSF46919; 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 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 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
