ID   POL_EIAV9               Reviewed;        1146 AA.
AC   P11204;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 165.
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 (isolate 1369) (EIAV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Lentivirus equinfane; Equine infectious anemia virus.
OX   NCBI_TaxID=11670;
OH   NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3035786; DOI=10.1016/0042-6822(87)90202-9;
RA   Kawakami T., Sherman L., Dahlberg J., Gazit A., Yaniv A., Tronick S.R.,
RA   Aaronson S.A.;
RT   "Nucleotide sequence analysis of equine infectious anemia virus proviral
RT   DNA.";
RL   Virology 158:300-312(1987).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAB59862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M16575; AAB59862.1; ALT_INIT; Genomic_RNA.
DR   PIR; B27842; GNLJEW.
DR   PDB; 1DUC; X-ray; 2.05 A; A=742-875.
DR   PDB; 1DUN; X-ray; 1.90 A; A=742-875.
DR   SMR; P11204; -.
DR   MEROPS; A02.004; -.
DR   EvolutionaryTrace; P11204; -.
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; IDA:CAFA.
DR   GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
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:0002134; F:UTP binding; IDA:CAFA.
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:0006226; P:dUMP biosynthetic process; IDA:CAFA.
DR   GO; GO:0046081; P:dUTP catabolic process; IDA:CAFA.
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.
DR   PDBsum; 1DUC; -.
DR   PDBsum; 1DUN; -.
PE   1: Evidence at protein level;
KW   3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
KW   DNA integration; DNA recombination; DNA-binding; Endonuclease; Hydrolase;
KW   Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Protease; RNA-directed DNA polymerase; Transferase;
KW   Viral genome integration; Virus entry into host cell; Zinc; Zinc-finger.
FT   CHAIN           1..195
FT                   /note="Protease"
FT                   /id="PRO_0000038838"
FT   CHAIN           196..914
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000038839"
FT   CHAIN           915..1146
FT                   /note="Integrase"
FT                   /id="PRO_0000038840"
FT   DOMAIN          100..174
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          230..419
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          617..740
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          921..1078
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         878..919
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   DNA_BIND        1096..1144
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         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         891
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         915
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         918
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   STRAND          744..746
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          748..750
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          758..763
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          768..770
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          775..779
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          783..785
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          790..795
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   HELIX           798..802
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          805..808
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          811..813
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          821..826
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          828..830
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          832..834
FT                   /evidence="ECO:0007829|PDB:1DUN"
FT   STRAND          839..847
FT                   /evidence="ECO:0007829|PDB:1DUN"
SQ   SEQUENCE   1146 AA;  129510 MW;  2BEB2E04F93FA36F CRC64;
     TAWTFLKAMQ KCSKKREARG SREAPETNFP DTTEESAQQI CCTRDSSDSK SVPRSERNKK
     GIQCQGEGSS RGSQPGQFVG VTYNLEKRPT TIVLINDTPL NVLLDTGADT SVLTTAHYNR
     LKYRGRKYQG TGIIGVGGNV ETFSTPVTIK KKGRHIKTRM LVADIPVTIL GRDILQDLGA
     KLVLAQLSKE IKFRKIELKE GTMGPKIPQW PLTKEKLEGA KEIVQRLLSE GKISEASDNN
     PYNSPIFVIK KRSGKWRLLQ DLRELNKTVQ VGTEISRGLP HPGGLIKCKH MTVLDIGDAY
     FTIPLDPEFR PYTAFTIPSI NHQEPDKRYV WNCLPQGFVL SPYIYQKTLQ EILQPFRERY
     PEVQLYQYMD DLFVGSNGSK KQHKELIIEL RAILLEEGFE TPDDKLQEVP PYSWLGYQLC
     PENWKVQKMQ LDMVKNPTLN DVQKLMGNIT WMSSGVPGLT VKHIAATTKG CLELNQKVIW
     TEEAQKELEE NNEKIKNAQG LQYYNPEEEM LCEVEITKNY EATYVIKQSQ GILWAGKKIM
     KANKGWSTVK NLMLLLQHVA TESITRVGKC PTFKVPFTKE QVMWEMQKGW YYSWLPEIVY
     THQVVHDDWR MKLVEEPTSG ITIYTDGGKQ NGEGIAAYVT SNGRTKQKRL GPVTHQVAER
     MAIQMALEDT RDKQVNIVTD SYYCWKNITE GLGLEGPQSP WWPIIQNIRE KEIVYFAWVP
     GHKGICGNQL ADEAAKIKEE IMLAYQGTQI KEKRDEDAGF DLCVPYDIMI PVSDTKIIPT
     DVKIQVPPNS FGWVTGKSSM AKQGLLINGG IIDEGYTGEI QVICTNIGKS NIKLIEGQKF
     AQLIILQHHS NSRQPWDENK ISQRGDKGFG STGVFWVENI QEAQDEHENW HTSPKILARN
     YKIPLTVAKQ ITQECPHCTK QGSGPAGCVM RSPNHWQADC THLDNKIILT FVESNSGYIH
     ATLLSKENAL CTSLAILEWA RLFSPKSLHT DNGTNFVAEP VVNLLKFLKI AHTTGIPYHP
     ESQGIVERAN RTLKEKIQSH RDNTQTLEAA LQLALITCNK GRESMGGQTP WEVFITNQAQ
     VIHEKLLLQQ AQSSKKFCFY KIPGEHDWKG PTRVLWKGDG AVVVNDEGKG IIAVPLTRTK
     LLIKPN
//