ID   POL_EIAVY               Reviewed;        1145 AA.
AC   P03371;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 157.
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   Equine infectious anemia virus (strain Wyoming) (EIAV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Lentivirus equinfane; Equine infectious anemia virus.
OX   NCBI_TaxID=11672;
OH   NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3003905; DOI=10.1126/science.3003905;
RA   Stephens R.M., Casey J.W., Rice N.R.;
RT   "Equine infectious anemia virus gag and pol genes: relatedness to visna and
RT   AIDS virus.";
RL   Science 231:589-594(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1029-1145.
RX   PubMed=2431539; DOI=10.1016/0042-6822(86)90195-9;
RA   Rushlow K., Olsen K., Stiegler G., Payne S.L., Montelaro R.C., Issel C.J.;
RT   "Lentivirus genomic organization: the complete nucleotide sequence of the
RT   env gene region of equine infectious anemia virus.";
RL   Virology 155:309-321(1986).
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   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The original EMBL accession numbers (M11337 and M14855)
CC       assigned to this isolate (isolate Wyoming) have been made secondary to
CC       M16575 which is from a different isolate (clone 1365). {ECO:0000305}.
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DR   PIR; A03970; GNLJEV.
DR   SMR; P03371; -.
DR   DrugBank; DB03413; Deoxyuridine-5'-Diphosphate.
DR   BRENDA; 3.4.23.B3; 2115.
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; cd09276; Rnase_HI_RT_non_LTR; 1.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   FunFam; 3.30.420.10:FF:000212; Pol polyprotein; 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   InterPro; IPR010661; RVT_thumb.
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; 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   Pfam; PF06817; RVT_thumb; 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; Cleavage on pair of basic residues; DNA integration;
KW   DNA recombination; DNA-binding; Endonuclease; Hydrolase; Metal-binding;
KW   Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Protease;
KW   RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   CHAIN           1..195
FT                   /note="Protease"
FT                   /id="PRO_0000038835"
FT   CHAIN           196..913
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000038836"
FT   CHAIN           914..1145
FT                   /note="Integrase"
FT                   /id="PRO_0000038837"
FT   DOMAIN          100..174
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          230..418
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          616..739
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          920..1077
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         877..918
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   DNA_BIND        1095..1143
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT   REGION          13..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         886
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         890
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         914
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         917
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
SQ   SEQUENCE   1145 AA;  129520 MW;  EE723380950D5D9E CRC64;
     TAWTFLKAMQ KCSKKREARG SREAPETNFP DTTEESAQQI CCTRDSSDSK SVPRSERNKK
     GIQCQGEGSS RGSQPGQFVG VTYNLEKRPT TIVLINDTPL NVLLDTGADT SVLTTAHYNR
     LKYRGRKYQG TGIIGVGGNV ETFSTPVTIK KKGRHIKTRM LVADIPVTIL GRDILQDLGA
     KLVLAQLSKE IKFRKIELKE GTMGPKIPQW PLTKEKLEGA KETVQRLLSE GKISEASDNN
     PYNSPIFVIK KRSGKWRLLQ DLRELNKTVQ VGTEISRGLP HPGGLIKCKH MTVLDIGDAY
     FTIPLDPEFR PYTAFTIPSI NHQEPDKRYV WKCLPQGFVL SPYIYQKTLQ EILQPFRERY
     PEVQLYQYMD DLFVGSNGSK KQHKELIIEL RAILQKGFET PDDKLQEVPP YSWLGYQLCP
     ENWKVQKMQL DMVKNPTLND VQKLMGNITW MSSGVPGLTV KHIAATTKGC LELNQKVIWT
     EEAQKELEEN NEKIKNAQGL QYYNPEEEML CEVEITKNYE ATYVIKQSQG ILWAGKKIMK
     ANKGWSTVKN LMLLLQHVAT ESITRVGKCP TFKVPFTKEQ VMWEMQKGWY YSWLPEIVYT
     HQVVHDDWRM KLVEEPTSGI TIYTDGGKQN GEGIAAYVTS NGRTKQKRLG PVTHQVAERM
     AIQMALEDTR DKQVNIVTDS YYCWKNITEG LGLEGPQNPW WPIIQNIREK EIVYFAWVPG
     HKGIYGNQLA DEAAKIKEEI MLAYQGTQIK EKRDEDAGFD LCVPYDIMIP VSDTKIIPTD
     VKIQVPPNSF GWVTGKSSMA KQGLLINGGI IDEGYTGEIQ VICTNIGKSN IKLIEGQKFA
     QLIILQHHSN SRQPWDENKI SQRGDKGFGS TGVFWVENIQ EAQDEHENWH TSPKILARNY
     KIPLTVAKQI TQECPHCTKQ GSGPAGCVMR SPNHWQADCT HLDNKIILHF VESNSGYIHA
     TLLSKENALC TSLAILEWAR LFSPKSLHTD NGTNFVAEPV VNLLKFLKIA HTTGIPYHPE
     SQGIVERANR TLKEKIQSHR DNTQTLEAAL QLALITCNKG RESMGGQTPW EVFITNQAQV
     IHEKLLLQQA QSSKKFCFYK IPGEHDWKGP TRVLWKGDGA VVVNDEGKGI IAVPLTRTKL
     LIKPN
//