POL_EIAVY
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 03-AUG-2022, entry version 146.
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.
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=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 -!- 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: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 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 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 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
