POL_EIAVC
ID POL_EIAVC Reviewed; 1146 AA.
AC P32542;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, 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 CL22) (EIAV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=31675;
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=1318398; DOI=10.1128/jvi.66.7.4085-4097.1992;
RA Perry S.T., Flaherty M.T., Kelley M.J., Clabough D.L., Tronick S.R.,
RA Coggins L., Whetter L., Lengel C.R., Fuller F.;
RT "The surface envelope protein gene region of equine infectious anemia virus
RT is not an important determinant of tropism in vitro.";
RL J. Virol. 66:4085-4097(1992).
RN [2]
RP 3D-STRUCTURE MODELING OF 81-184.
RX PubMed=8384880; DOI=10.1021/bi00064a019;
RA Weber I.T., Tozser J., Wu J., Friedman D., Oroszlan S.;
RT "Molecular model of equine infectious anemia virus proteinase and kinetic
RT measurements for peptide substrates with single amino acid substitutions.";
RL Biochemistry 32:3354-3362(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 81-184.
RX PubMed=8844837; DOI=10.1002/pro.5560050802;
RA Gustchina A., Kervinen J., Powell D.J., Zdanov A., Kay J., Wlodawer A.;
RT "Structure of equine infectious anemia virus proteinase complexed with an
RT inhibitor.";
RL Protein Sci. 5:1453-1465(1996).
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}.
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DR EMBL; M87581; AAA43004.1; -; Genomic_RNA.
DR PIR; B41991; GNLJ22.
DR PDB; 1FMB; X-ray; 1.80 A; A=81-184.
DR PDB; 2FMB; X-ray; 1.80 A; A=81-184.
DR PDBsum; 1FMB; -.
DR PDBsum; 2FMB; -.
DR SMR; P32542; -.
DR MEROPS; A02.004; -.
DR BRENDA; 3.4.23.B3; 2115.
DR EvolutionaryTrace; P32542; -.
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; 2.30.30.10; -; 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_0000038832"
FT CHAIN 196..914
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000038833"
FT CHAIN 915..1146
FT /note="Integrase"
FT /id="PRO_0000038834"
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 85..87
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1FMB"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:1FMB"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:1FMB"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:1FMB"
SQ SEQUENCE 1146 AA; 129509 MW; C14058EAF93F3F5D 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 RAILLEKGFE 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
