POL_EIAV9
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 03-AUG-2022, entry version 153.
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.
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=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 -!- 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 PDBsum; 1DUC; -.
DR PDBsum; 1DUN; -.
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:InterPro.
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: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 InterPro; IPR010661; RVT_thumb.
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; 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 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 26..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
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
